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Displaying entries 1-50 of 109.
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EC | 2.3.1.243 | Relevance: 100% | ||||||||||||||
Accepted name: | acyl-Kdo2-lipid IVA acyltransferase | |||||||||||||||
Reaction: | a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] + an [acyl-carrier protein] | |||||||||||||||
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here | ||||||||||||||||
Glossary: | Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)2-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-(acyloxy)acyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose |
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Other name(s): | lpxM (gene name); MsbB acyltransferase; myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase; tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase; lauroyl-Kdo2-lipid IVA myristoyltransferase | |||||||||||||||
Systematic name: | fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] O-acyltransferase | |||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 2.3.1.241 | Relevance: 96.9% | ||||||||||||||
Accepted name: | Kdo2-lipid IVA acyltransferase | |||||||||||||||
Reaction: | a fatty acyl-[acyl-carrier protein] + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] = an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] + an [acyl-carrier protein] | |||||||||||||||
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here | ||||||||||||||||
Glossary: | Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose an α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] = 3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→4)-3-deoxy-α-D-manno-oct-2-ulopyranosyl-(2→6)-2-deoxy-2-{[(3R)-3-(acyloxy)acyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phosphono-α-D-glucopyranose |
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Other name(s): | LpxL; htrB (gene name); dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase; lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase; (Kdo)2-lipid IVA lauroyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase; dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase; Kdo2-lipid IVA lauroyltransferase | |||||||||||||||
Systematic name: | fatty acyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] O-acyltransferase | |||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.3.1.242 | Relevance: 80.9% | ||||||||||||||
Accepted name: | Kdo2-lipid IVA palmitoleoyltransferase | |||||||||||||||
Reaction: | a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo2-lipid IVA = (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA + an [acyl-carrier protein] | |||||||||||||||
For diagram of Kdo-Kdo-Lipid IVA metabolism, click here | ||||||||||||||||
Glossary: | Kdo = 3-deoxy-D-manno-oct-2-ulopyranosylonic acid lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA (9Z)-hexadec-9-enoyl = palmitoleoyl (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-{(3R)-3-[(9Z)-hexadec-9-enoyl]tetradecanamido}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate |
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Other name(s): | LpxP; palmitoleoyl-acyl carrier protein-dependent acyltransferase; cold-induced palmitoleoyl transferase; palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase; (Kdo)2-lipid IVA palmitoleoyltransferase; α-Kdo-(2→4)-α-(2→6)-lipid IVA palmitoleoyltransferase | |||||||||||||||
Systematic name: | (9Z)-hexadec-9-enoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase | |||||||||||||||
Comments: | The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.7.4.30 | |||||||||||||||
Transferred entry: | lipid A phosphoethanolamine transferase. Now EC 2.7.8.43, lipid A phosphoethanolamine transferase | |||||||||||||||
EC | 2.7.8.43 | Relevance: 79.9% | ||||||||||||||
Accepted name: | lipid A phosphoethanolamine transferase | |||||||||||||||
Reaction: | (1) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 1-(2-aminoethyl diphosphate) (2) diacylphosphatidylethanolamine + lipid A = diacylglycerol + lipid A 4′-(2-aminoethyl diphosphate) (3) diacylphosphatidylethanolamine + lipid A 1-(2-aminoethyl diphosphate) = diacylglycerol + lipid A 1,4′-bis(2-aminoethyl diphosphate) |
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Glossary: | lipid A (Campylobacter jejuni) = 2,3-dideoxy-2,3-bis[(3R)-3-(hexadecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate lipid A (Escherichia coli) = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate lipid A (Helicobacter pylori) = 2-deoxy-2-[(3R)-3-(octadecanoyloxy)octadecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyhexadecanoyl]-2-[(3R)-3-hydroxyoctadecanamido]-α-D-glucopyranosyl phosphate lipid A (Neisseria meningitidis) = 2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxydodecanoyl]-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate lipid A 1-[(2-aminoethyl) diphosphate] = P1-(2-aminoethyl) P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate lipid A 1,4′-bis(2-aminoethyl diphosphate) = P1-(2-aminoethyl) P2-(2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-(2-aminoethyldiphospho)-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl) diphosphate |
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Other name(s): | lipid A PEA transferase; LptA | |||||||||||||||
Systematic name: | diacylphosphatidylethanolamine:lipid-A ethanolaminephosphotransferase | |||||||||||||||
Comments: | The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-β-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.7.4.29 | Relevance: 76.3% | ||||||||||||||
Accepted name: | Kdo2-lipid A phosphotransferase | |||||||||||||||
Reaction: | ditrans-octacis-undecaprenyl diphosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = ditrans-octacis-undecaprenyl phosphate + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A 1-diphosphate | |||||||||||||||
Glossary: | lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate lipid A 1-diphosphate = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl diphosphate |
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Other name(s): | lipid A undecaprenyl phosphotransferase; LpxT; YeiU | |||||||||||||||
Systematic name: | ditrans-octacis-undecaprenyl-diphosphate:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A phosphotransferase | |||||||||||||||
Comments: | An inner-membrane protein. The activity of the enzyme is regulated by PmrA. In vitro the enzyme can use diacylglycerol 3-diphosphate as the phosphate donor. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.7.8.42 | Relevance: 73.6% | ||||||||||||||
Accepted name: | Kdo2-lipid A phosphoethanolamine 7′′-transferase | |||||||||||||||
Reaction: | (1) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid A (2) diacylphosphatidylethanolamine + α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IVA = diacylglycerol + 7-O-[2-aminoethoxy(hydroxy)phosphoryl]-α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid IVA |
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Glossary: | lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate |
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Other name(s): | eptB (gene name) | |||||||||||||||
Systematic name: | diacylphosphatidylethanolamine:α-D-Kdo-(2→4)-α-D-Kdo-(2→6)-lipid-A 7′′-phosphoethanolaminetransferase | |||||||||||||||
Comments: | The enzyme has been characterized from the bacterium Escherichia coli. It is activated by Ca2+ ions and is silenced by the sRNA MgrR. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.2.43 | Relevance: 62.9% | ||||||||||||||
Accepted name: | lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase | |||||||||||||||
Reaction: | (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-α-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate (2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate (3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate |
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For diagram of lipid IIA biosynthesis, click here | ||||||||||||||||
Glossary: | lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose α-Kdo-(2→4)-α-Kdo-(2→6)-[4′-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose |
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Other name(s): | undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK; arnT (gene name) | |||||||||||||||
Systematic name: | 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl-phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase | |||||||||||||||
Comments: | Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 3.1.2.21 | Relevance: 59.1% | ||||||||||||||
Accepted name: | dodecanoyl-[acyl-carrier-protein] hydrolase | |||||||||||||||
Reaction: | a dodecanoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + dodecanoate | |||||||||||||||
Other name(s): | lauryl-acyl-carrier-protein hydrolase; dodecanoyl-acyl-carrier-protein hydrolase; dodecyl-acyl-carrier protein hydrolase; dodecanoyl-[acyl-carrier protein] hydrolase; dodecanoyl-[acyl-carrier-protein] hydrolase | |||||||||||||||
Systematic name: | dodecanoyl-[acyl-carrier protein] hydrolase | |||||||||||||||
Comments: | Acts on the acyl-carrier-protein thioester of C12 and, with a much lower activity, C14 fatty acids. The derivative of oleic acid is hydrolysed very slowly (cf. EC 3.1.2.14, oleoyl-[acyl-carrier-protein] hydrolase). | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 137903-37-8 | |||||||||||||||
References: |
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EC | 2.3.1.251 | Relevance: 54.3% | ||||||||||||||
Accepted name: | lipid IVA palmitoyltransferase | |||||||||||||||
Reaction: | (1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A (2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB (3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB |
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For diagram of lipid IVB biosynthesis, click here | ||||||||||||||||
Glossary: | palmitoyl = hexadecanoyl hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate lipid IIB = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate lipid IVB = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate |
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Other name(s): | PagP; crcA (gene name) | |||||||||||||||
Systematic name: | 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase | |||||||||||||||
Comments: | Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IVA. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 2.3.3.4 | Relevance: 53.2% | ||||||||||||||
Accepted name: | decylhomocitrate synthase | |||||||||||||||
Reaction: | dodecanoyl-CoA + H2O + 2-oxoglutarate = (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA | |||||||||||||||
For diagram of reaction, click here | ||||||||||||||||
Other name(s): | 2-decylhomocitrate synthase; 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acylating) | |||||||||||||||
Systematic name: | dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming) | |||||||||||||||
Comments: | Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51845-40-0 | |||||||||||||||
References: |
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EC | 2.3.1.97 | Relevance: 43.5% | ||||||||||||||
Accepted name: | glycylpeptide N-tetradecanoyltransferase | |||||||||||||||
Reaction: | tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein] | |||||||||||||||
Glossary: | tetradecanoyl-CoA = myristoyl-CoA | |||||||||||||||
Other name(s): | NMT (gene name); peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase; tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase | |||||||||||||||
Systematic name: | tetradecanoyl-CoA:N-terminal-glycine-[protein] N-tetradecanoyltransferase | |||||||||||||||
Comments: | The enzyme catalyses the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 110071-61-9 | |||||||||||||||
References: |
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EC | 2.1.1.344 | Relevance: 42.8% | ||||||||||||||
Accepted name: | ornithine lipid N-methyltransferase | |||||||||||||||
Reaction: | 3 S-adenosyl-L-methionine + an ornithine lipid = 3 S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid (overall reaction) (1a) S-adenosyl-L-methionine + an ornithine lipid = S-adenosyl-L-homocysteine + an N-methylornithine lipid (1b) S-adenosyl-L-methionine + an N-methylornithine lipid = S-adenosyl-L-homocysteine + an N,N-dimethylornithine lipid (1c) S-adenosyl-L-methionine + an N,N-dimethylornithine lipid = S-adenosyl-L-homocysteine + an N,N,N-trimethylornithine lipid |
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Glossary: | an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine | |||||||||||||||
Other name(s): | olsG (gene name) | |||||||||||||||
Systematic name: | S-adenosyl-L-methionine:ornithine lipid N-methyltransferase | |||||||||||||||
Comments: | The enzyme, characterized from the bacterium Singulisphaera acidiphila, catalyses three successive methylations of the terminal δ-nitrogen in ornithine lipids. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 1.14.99.32 | |||||||||||||||
Transferred entry: | myristoyl-CoA 11-(Z) desaturase. Now classified as EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase. | |||||||||||||||
EC | 2.3.1.301 | Relevance: 38.1% | ||||||||||||||
Accepted name: | mycobacterial β-ketoacyl-[acyl carrier protein] synthase III | |||||||||||||||
Reaction: | dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2 | |||||||||||||||
Glossary: | dodecanoyl-CoA = lauroyl-CoA | |||||||||||||||
Other name(s): | fabH (gene name) (ambiguous); mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III | |||||||||||||||
Systematic name: | dodecanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase | |||||||||||||||
Comments: | The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, β-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 1.14.11.58 | Relevance: 36.2% | ||||||||||||||
Accepted name: | ornithine lipid ester-linked acyl 2-hydroxylase | |||||||||||||||
Reaction: | an ornithine lipid + 2-oxoglutarate + O2 = a 2-hydroxyornithine lipid + succinate + CO2 | |||||||||||||||
Glossary: | an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine a 2-hydroxyornithine lipid = an Nα-[(3R)-3-(2-hydroxyacyloxy)acyl]-L-ornithine |
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Other name(s): | olsC (gene name) | |||||||||||||||
Systematic name: | ornithine lipid,2-oxoglutarate:oxygen oxidoreductase (ester-linked acyl 2-hydroxylase) | |||||||||||||||
Comments: | The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.7.1.235 | Relevance: 35.8% | ||||||||||||||
Accepted name: | lipopolysaccharide core heptose(I) kinase | |||||||||||||||
Reaction: | ATP + an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] | |||||||||||||||
Glossary: | Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It usually consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-β-D-manno-heptose |
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Other name(s): | WaaP; RfaP | |||||||||||||||
Systematic name: | ATP:an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] heptoseI 4-O-phosphotransferase | |||||||||||||||
Comments: | The enzyme catalyses the phosphorylation of L-glycero-D-manno-heptose I (the first heptose added to the lipid, Hep I) in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.7.1.130 | Relevance: 35% | ||||||||||||||
Accepted name: | tetraacyldisaccharide 4′-kinase | |||||||||||||||
Reaction: | ATP + a lipid A disaccharide = ADP + a lipid IVA | |||||||||||||||
For diagram of lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | a lipid A disaccharide = a dephospho-lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose |
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Other name(s): | lpxK (gene name); lipid-A 4′-kinase; ATP:2,2′,3,3′-tetrakis[(3R)-3-hydroxytetradecanoyl]-β-D-glucosaminyl-(1→6)-α-D-glucosaminyl-phosphate 4′-O-phosphotransferase | |||||||||||||||
Systematic name: | ATP:2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose 4′-O-phosphotransferase | |||||||||||||||
Comments: | Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.4.1.182 (lipid-A-disaccharide synthase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 107309-06-8 | |||||||||||||||
References: |
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EC | 7.5.2.6 | Relevance: 34.9% | ||||||||||||||
Accepted name: | ABC-type lipid A-core oligosaccharide transporter | |||||||||||||||
Reaction: | ATP + H2O + lipid A-core oligosaccharide[side 1] = ADP + phosphate + lipid A-core oligosaccharide[side 2] | |||||||||||||||
Other name(s): | MsbA; lipid flippase; ATP-dependent lipid A-core flippase | |||||||||||||||
Systematic name: | ATP phosphohydrolase (ABC-type, lipid A-core oligosaccharide-translocating) | |||||||||||||||
Comments: | An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway. Not to be confused with EC 7.5.2.5, ABC-type lipopolysaccharide transporter (LptB), which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 2.4.99.12 | Relevance: 34.7% | ||||||||||||||
Accepted name: | lipid IVA 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Reaction: | CMP-β-Kdo + a lipid IVA + CMP-β-Kdo = CMP + an α-Kdo-(2→6)-[lipid IVA] | |||||||||||||||
For diagram of Kdo4-Lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | CMP-β-Kdo = CMP-3-deoxy-β-D-manno-octulosonate = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose |
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Other name(s): | waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; lipid IVA KDO transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase; KDO transferase | |||||||||||||||
Systematic name: | CMP-3-deoxy-β-D-manno-oct-2-ulosonate:[lipid IVA] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting) | |||||||||||||||
Comments: | The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyse the transfer of a single 3-deoxy-D-manno-oct-2-ulosonate residue from CMP-3-deoxy-D-manno-oct-2-ulosonate to lipid IVA [2-4]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [5]. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 2.3.1.270 | Relevance: 34.7% | ||||||||||||||
Accepted name: | lyso-ornithine lipid O-acyltransferase | |||||||||||||||
Reaction: | a lyso-ornithine lipid + an acyl-[acyl-carrier protein] = an ornithine lipid + a holo-[acyl-carrier protein] | |||||||||||||||
Glossary: | a lyso-ornithine lipid = an Nα-[(3R)-3-hydroxyacyl]-L-ornithine an ornithine lipid = an Nα-[(3R)-3-(acyloxy)acyl]-L-ornithine |
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Other name(s): | olsA (gene name) | |||||||||||||||
Systematic name: | Nα-[(3R)-hydroxy-acyl]-L-ornithine O-acyltransferase | |||||||||||||||
Comments: | This bacterial enzyme catalyses the second step in the formation of ornithine lipids. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.13 | Relevance: 34.4% | ||||||||||||||
Accepted name: | (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Reaction: | CMP-β-Kdo + an α-Kdo-(2→6)-[lipid IVA] = CMP + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid IVA] | |||||||||||||||
For diagram of Kdo4-Lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate a lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose |
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Other name(s): | waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase; CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase; Kdo transferase (ambiguous) | |||||||||||||||
Systematic name: | CMP-3-deoxy-β-D-manno-oct-2-ulosonate:α-Kdo-(2→6)-[lipid IVA] 3-deoxy-D-manno-oct-2-ulosonate transferase (configuration-inverting) | |||||||||||||||
Comments: | The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.12 [lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [2]. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.1.182 | Relevance: 34.2% | ||||||||||||||
Accepted name: | lipid-A-disaccharide synthase | |||||||||||||||
Reaction: | a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + a lipid X = UDP + a lipid A disaccharide | |||||||||||||||
For diagram of lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate = 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine a lipid A disaccharide = a 2-deoxy-2-{[(3R)-3-hydroxyacyl]amino}-3-O-[(3R)-3-hydroxyacyl]-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-{[(3R)-3-hydroxyacyl]amino}-1-O-phospho-α-D-glucopyranose |
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Other name(s): | lpxB (gene name); UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine:2,3-bis-(3-hydroxytetradecanoyl)-β-D-glucosaminyl-1-phosphate 2,3-bis(3-hydroxytetradecanoyl)-glucosaminyltransferase (incorrect) | |||||||||||||||
Systematic name: | UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine:2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosaminyltransferase | |||||||||||||||
Comments: | Involved with EC 2.3.1.129 (acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase) and EC 2.7.1.130 (tetraacyldisaccharide 4′-kinase) in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-81-0 | |||||||||||||||
References: |
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EC | 2.7.1.166 | Relevance: 33.7% | ||||||||||||||
Accepted name: | 3-deoxy-D-manno-octulosonic acid kinase | |||||||||||||||
Reaction: | α-Kdo-(2→6)-lipid IVA + ATP = 4-O-phospho-α-Kdo-(2→6)-lipid IVA + ADP | |||||||||||||||
Glossary: | (Kdo)-lipid IVA = α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose (4-O-phospho-KDO)-lipid IVA = 4-O-phospho-α-Kdo-(2→6)-lipid IVA = (3-deoxy-4-O-phosphono-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose |
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Other name(s): | kdkA (gene name); Kdo kinase | |||||||||||||||
Systematic name: | ATP:(Kdo)-lipid IVA 3-deoxy-α-D-manno-oct-2-ulopyranose 4-phosphotransferase | |||||||||||||||
Comments: | The enzyme phosphorylates the 4-OH position of Kdo in (Kdo)-lipid IVA. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.26 | Relevance: 33.6% | ||||||||||||||
Accepted name: | O-antigen ligase | |||||||||||||||
Reaction: | a lipid-linked O antigen + a lipid A-core oligosaccharide = a lipopolysaccharide + a polyisoprenyl diphosphate | |||||||||||||||
Other name(s): | waaL (gene name); surface polymer:lipid A-core ligase; rfaL (gene name) | |||||||||||||||
Systematic name: | lipid-linked O-antigen:lipid A-core oligosaccharide O-antigen transferase (configuration-inverting) | |||||||||||||||
Comments: | This Gram-negative bacterial enzyme attaches the polymerized O antigen molecule to the outer core region of the lipid A-core oligosaccharide, finalizing the biosynthesis of the lipopolysaccharide. Prior to the reaction the two substrates are attached to the periplasmic-facing side of the inner membrane, and the enzyme transfers the O-antigen from its polyprenyl diphosphate membrane anchor (usually ditrans,octacis-undecaprenyl diphosphate) to a terminal sugar of the lipid A-core oligosaccharide. Despite the popular name "ligase", the enzyme is not a real ligase, as the reaction does not involve the hydrolysis of a phosphate bond in a triphosphate. The enzyme is embedded in the inner membrane and often has 12 trans-membrane segments. It is a metal-independent inverting glycosyltransferase, and in some cases it can attach surface polymers other than O-antigens to the lipid A-core oligosaccharide. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.15 | Relevance: 33.3% | ||||||||||||||
Accepted name: | (Kdo)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Reaction: | α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP-β-Kdo = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP | |||||||||||||||
For diagram of Kdo4-Lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | (Kdo)3-lipid IVA = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose (Kdo)4-lipid IVA = α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-[(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)]-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate |
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Other name(s): | Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Systematic name: | CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)3-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→4) glycosidic bond-forming] | |||||||||||||||
Comments: | The enzyme from Chlamydia psittaci transfers four Kdo residues to lipid A, forming a branched tetrasaccharide with the structure α-Kdo-(2,8)-[α-Kdo-(2,4)]-α-Kdo-(2,4)-α-Kdo (cf. EC 2.4.99.12 [lipid IVA 3-deoxy-D-manno-octulosonic acid transferase], EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase], and EC 2.4.99.14 [(Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase]). | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.23 | Relevance: 33% | ||||||||||||||
Accepted name: | lipopolysaccharide heptosyltransferase I | |||||||||||||||
Reaction: | ADP-L-glycero-β-D-manno-heptose + an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] | |||||||||||||||
Glossary: | Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-D-manno-heptose |
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Other name(s): | HepI; rfaC (gene name); WaaC; heptosyltransferase I (ambiguous) | |||||||||||||||
Systematic name: | ADP-L-glycero-β-D-manno-heptose:an α-Kdo-(2→4)-α-Kdo-(2→6)-[lipid A] 5-α-heptosyltransferase | |||||||||||||||
Comments: | The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of many Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.24 | Relevance: 32.4% | ||||||||||||||
Accepted name: | lipopolysaccharide heptosyltransferase II | |||||||||||||||
Reaction: | ADP-L-glycero-β-D-manno-heptose + an α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] | |||||||||||||||
Glossary: | Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-D-manno-heptose |
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Other name(s): | HepII; rfaF (gene name); WaaF; heptosyltransferase II | |||||||||||||||
Systematic name: | ADP-L-glycero-β-D-manno-heptose:an α-L-glycero-D-manno-heptosyl-(1→5)-[α-Kdo-(2→4)]-α -Kdo-(2→6)-[lipid A] 3-α-heptosyltransferase | |||||||||||||||
Comments: | The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.14 | Relevance: 31.8% | ||||||||||||||
Accepted name: | (Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Reaction: | α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP-β-Kdo = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + CMP | |||||||||||||||
For diagram of Kdo4-Lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | (Kdo)2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose (Kdo)3-lipid IVA = α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→8)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose CMP-β-Kdo = CMP-3-deoxy-β-D-manno-oct-2-ulopyranosylonate |
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Other name(s): | Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase | |||||||||||||||
Systematic name: | CMP-3-deoxy-D-manno-oct-2-ulosonate:(Kdo)2-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase [(2→8) glycosidic bond-forming] | |||||||||||||||
Comments: | The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.25 | Relevance: 31.7% | ||||||||||||||
Accepted name: | lipopolysaccharide heptosyltransferase III | |||||||||||||||
Reaction: | ADP-L-glycero-β-D-manno-heptose + an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→7)-α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] | |||||||||||||||
Glossary: | Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups. Hep = L-glycero-D-manno-heptose |
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Other name(s): | waaQ (gene name); rfaQ (gene name) | |||||||||||||||
Systematic name: | ADP-L-glycero-β-D-manno-heptose:an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] heptoseI 7-α-heptosyltransferase | |||||||||||||||
Comments: | The enzyme catalyses a glycosylation step in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 1.14.15.14 | Relevance: 30.9% | ||||||||||||||
Accepted name: | methyl-branched lipid ω-hydroxylase | |||||||||||||||
Reaction: | a methyl-branched lipid + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = an ω-hydroxy-methyl-branched lipid + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster | |||||||||||||||
Other name(s): | CYP124 | |||||||||||||||
Systematic name: | methyl-branched lipid,reduced-ferredoxin:oxygen oxidoreductase (ω-hydroxylating) | |||||||||||||||
Comments: | The enzyme, found in pathogenic and nonpathogenic mycobacteria species, actinomycetes, and some proteobacteria, hydroxylates the ω-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate. It is a P-450 heme-thiolate enzyme. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 1.14.19.34 | Relevance: 28.6% | ||||||||||||||
Accepted name: | acyl-lipid (9+3)-(E)-desaturase | |||||||||||||||
Reaction: | (1) an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-octadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) a palmitoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12E)-hexadeca-9,12-dienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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Other name(s): | acyl-lipid 12-(E)-desaturase; DsFAD2-1; FADX | |||||||||||||||
Systematic name: | Δ9 acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase (12,13 trans-dehydrogenating) | |||||||||||||||
Comments: | The enzymes from the plants Dimorphotheca sinuata (African daisy) and Vernicia fordii (tung oil tree) insert a trans double bond in position C-12 of oleate and palmitoleate incorporated into glycerolipids. The enzyme introduces the new double bond at a position three carbons away from an existing double bond at position 9, towards the methyl end of the fatty acid. The enzyme from tung oil tree also possesses the activity of EC 1.14.19.33, Δ12 acyl-lipid conjugase. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 3.6.1.54 | Relevance: 28.2% | ||||||||||||||
Accepted name: | UDP-2,3-diacylglucosamine diphosphatase | |||||||||||||||
Reaction: | a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine + H2O = a lipid X + UMP | |||||||||||||||
For diagram of lipid IVA biosynthesis, click here | ||||||||||||||||
Glossary: | a lipid X = 2-N-[(3R)-3-hydroxyacyl]-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine 1-phosphate = 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine |
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Other name(s): | lpxH (gene name); UDP-2,3-diacylglucosamine hydrolase; UDP-2,3-diacylglucosamine pyrophosphatase; ybbF (gene name); UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-α-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-β-D-glucosaminyl 1-phosphate phosphohydrolase (incorrect); UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosaminyl 1-phosphate phosphohydrolase | |||||||||||||||
Systematic name: | UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxyacyl]-α-D-glucosamine-1-phosphate phosphohydrolase | |||||||||||||||
Comments: | The enzyme catalyses a step in the biosynthesis of lipid A. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||||
References: |
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EC | 1.14.19.16 | Relevance: 28% | ||||||||||||||
Accepted name: | linoleoyl-lipid Δ12 conjugase (11E,13Z-forming) | |||||||||||||||
Reaction: | a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,11E,13Z)-octadeca-9,11,13-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O | |||||||||||||||
Glossary: | punicate = (9Z,11E,13Z)-octadeca-9,11,13-trienoate linoleate = (9Z,12Z)-octadeca-9,12-dienoate |
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Other name(s): | Fac (gene name) | |||||||||||||||
Systematic name: | linoleoyl-lipid,ferrocytochrome-b5:oxygen 11,14 allylic oxidase (11E,13Z-forming) | |||||||||||||||
Comments: | The enzyme, characterized from the plants Punica granatum (pomegranate) and Trichosanthes kirilowii (Mongolian snake-gourd), converts a single cis double bond at position 12 of linoleate incorporated into phosphatidylcholine into conjugated 11-trans and 13-cis double bonds. cf. EC 1.14.19.33, Δ12 acyl-lipid conjugase (11E,13E-forming). | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.99.27 | Relevance: 27.9% | ||||||||||||||
Accepted name: | O-antigen polymerase Wzy | |||||||||||||||
Reaction: | n lipid-linked O-antigen repeat units = a lipid-linked O antigen + (n−1) polyisoprenyl diphosphate | |||||||||||||||
Other name(s): | wzy (gene name); rfc (gene name); Wzy O-antigen polymerase; Wzy polymerase | |||||||||||||||
Systematic name: | lipid-linked O-antigen repeat unit:O-antigen O-antigen repeat-unit transferase | |||||||||||||||
Comments: | The Wzy-type polymerase polymerizes O antigen repeat unit oligosaccharides that are anchored to the periplasmic face of the inner membrane, forming an O antigen polysaccharide that is still anchored to the membrane. A Wzz chain length regulator (sometimes referred to as an O-antigen co-polymerase) normally interacts with Wzy to confer a distinctive modal chain length distribution. The resultant polysaccharide is transferred from the membrane anchor to the lipid A-core oligosaccharide by EC 2.4.99.26, O-antigen ligase, forming a complete lipopolysaccharide structure. There is an enormous diversity of O antigen polymerases with different specificities, reflecting the variability in the structure and composition of O-antigens. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.1.130 | |||||||||||||||
Transferred entry: | dolichyl-phosphate-mannose—glycolipid α-mannosyltransferase. Now covered by EC 2.4.1.258 (Dol-P-Man:Man5GlcNAc2-PP-Dol α-1,3-mannosyltransferase), EC 2.4.1.259 (Dol-P-Man:Man6GlcNAc2-PP-Dol α-1,2-mannosyltransferase), EC 2.4.1.260 (Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase) and EC 2.4.1.261 (Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase). | |||||||||||||||
EC | 1.11.1.12 | Relevance: 27% | ||||||||||||||
Accepted name: | phospholipid-hydroperoxide glutathione peroxidase | |||||||||||||||
Reaction: | 2 glutathione + a hydroperoxy-fatty-acyl-[lipid] = glutathione disulfide + a hydroxy-fatty-acyl-[lipid] + H2O | |||||||||||||||
Other name(s): | peroxidation-inhibiting protein; PHGPX; peroxidation-inhibiting protein:peroxidase,glutathione (phospholipid hydroperoxide-reducing); phospholipid hydroperoxide glutathione peroxidase; hydroperoxide glutathione peroxidase | |||||||||||||||
Systematic name: | glutathione:lipid-hydroperoxide oxidoreductase | |||||||||||||||
Comments: | A protein containing a selenocysteine residue. The products of action of EC 1.13.11.12 lipoxygenase on phospholipids can act as acceptors; H2O2 can also act, but much more slowly (cf. EC 1.11.1.9 glutathione peroxidase). | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-70-8 | |||||||||||||||
References: |
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EC | 2.3.3.2 | Relevance: 26.8% | ||||||||||||||
Accepted name: | decylcitrate synthase | |||||||||||||||
Reaction: | lauroyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA | |||||||||||||||
For diagram of reaction, click here | ||||||||||||||||
Other name(s): | 2-decylcitrate synthase; (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA-acylating) | |||||||||||||||
Systematic name: | dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming) | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-72-8 | |||||||||||||||
References: |
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EC | 7.5.2.14 | Relevance: 25.8% | ||||||||||||||
Accepted name: | ABC-type homopolymeric O-antigen exporter | |||||||||||||||
Reaction: | ATP + a lipid-linked O antigen[cytosol] + H2O = ADP + phosphate + a lipid-linked O antigen[periplasm] | |||||||||||||||
Other name(s): | wzm (gene name); wzt (gene name) | |||||||||||||||
Systematic name: | ATP phosphohydrolase (ABC-type, homopolymeric O-antigen exporting) | |||||||||||||||
Comments: | Unlike heteropolymeric O antigens, which are polymerized in the periplasm by EC 2.4.99.27, O antigen polymerase Wzy, homopolymeric O antigens are polymerized inside the cytoplasm by a progressive transfer of sugar monomers to a growing chain attached to a polyprenyl diphosphate membrane anchor. When the chain reaches its full length it is transported across the cytoplasmic membrane by this ABC-type transporter, which consists of an ATP-binding subunit (Wzt) and an integral membrane protein (Wzm). Wzm proteins are poorly conserved in their primary sequence. Once in the periplasm, the O antigen is ligated to the lipid A-core complex by EC 2.4.99.26, O-antigen ligase. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 1.14.19.47 | Relevance: 25.6% | ||||||||||||||
Accepted name: | acyl-lipid (9-3)-desaturase | |||||||||||||||
Reaction: | (1) an α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a stearidonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a γ-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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Glossary: | stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid | |||||||||||||||
Other name(s): | DES6 (gene name); acyl-lipid 6-desaturase; acyl-lipid Δ6-desaturase; Δ6-desaturase (ambiguous) | |||||||||||||||
Systematic name: | Δ9 acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (6,7-cis-dehydrogenating) | |||||||||||||||
Comments: | The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Δ9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
References: |
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EC | 2.4.1.180 | Relevance: 25.2% | ||||||||||||||
Accepted name: | lipopolysaccharide N-acetylmannosaminouronosyltransferase | |||||||||||||||
Reaction: | UDP-N-acetyl-α-D-mannosaminouronate + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | |||||||||||||||
Glossary: | N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate | |||||||||||||||
Other name(s): | ManNAcA transferase; uridine diphosphoacetylmannosaminuronate-acetylglucosaminylpyrophosphorylundecaprenol acetylmannosaminuronosyltransferase; UDP-N-acetyl-β-D-mannosaminouronate:lipid I N-acetyl-β-D-mannosaminouronosyltransferase (incorrect) | |||||||||||||||
Systematic name: | UDP-N-acetyl-α-D-mannosaminouronate:lipid I N-acetyl-α-D-mannosaminouronosyltransferase | |||||||||||||||
Comments: | Involved in the biosynthesis of common antigen in Enterobacteriaceae. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113478-30-1 | |||||||||||||||
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EC | 2.4.1.325 | Relevance: 25% | ||||||||||||||
Accepted name: | TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase | |||||||||||||||
Reaction: | dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | |||||||||||||||
Glossary: | dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
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Other name(s): | TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name) | |||||||||||||||
Systematic name: | dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase | |||||||||||||||
Comments: | Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 1.14.99.31 | |||||||||||||||
Transferred entry: | myristoyl-CoA 11-(E) desaturase. Now classified as EC 1.14.19.24, myristoyl-CoA 11-(E) desaturase | |||||||||||||||
EC | 1.14.19.39 | Relevance: 24.8% | ||||||||||||||
Accepted name: | acyl-lipid Δ12-acetylenase | |||||||||||||||
Reaction: | linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O | |||||||||||||||
Glossary: | crepenynate = (9Z)-octadec-9-en-12-ynoate | |||||||||||||||
Systematic name: | Δ12 acyl-lipid,ferrocytochrome-b5:oxygen oxidoreductase (12,13-dehydrogenating) | |||||||||||||||
Comments: | The enzyme, characterized from the plant Crepis alpina, converts the double bond at position 12 of linoleate into a triple bond. The product is the main fatty acid found in triacylglycerols in the seed oil of Crepis alpina. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 1.14.19.14 | Relevance: 24.7% | ||||||||||||||
Accepted name: | linoleoyl-lipid Δ9 conjugase | |||||||||||||||
Reaction: | a linoleoyl-[glycerolipid] + reduced acceptor + O2 = an (8E,10E,12Z)-octadeca-8,10,12-trienoyl-[glycerolipid] + acceptor + 2 H2O | |||||||||||||||
Glossary: | calendate = (8E,10E,12Z)-octadeca-8,10,12-trienoate | |||||||||||||||
Systematic name: | linoleoyl-lipid,reduced acceptor:oxygen 8,11-allylic oxidase (8E,10E-forming) | |||||||||||||||
Comments: | The enzyme, characterized from the plant Calendula officinalis, converts a single cis double bond at position 9 of fatty acids incorporated into glycerolipids into two conjugated trans double bonds at positions 8 and 10. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 1.14.19.22 | Relevance: 24.7% | ||||||||||||||
Accepted name: | acyl-lipid ω-6 desaturase (cytochrome b5) | |||||||||||||||
Reaction: | an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O | |||||||||||||||
Other name(s): | oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name) | |||||||||||||||
Systematic name: | 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12,13 cis-dehydrogenating) | |||||||||||||||
Comments: | This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid ω-6 desaturase (ferredoxin). | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72536-70-0 | |||||||||||||||
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EC | 1.14.19.38 | Relevance: 24.2% | ||||||||||||||
Accepted name: | acyl-lipid Δ6-acetylenase | |||||||||||||||
Reaction: | (1) a γ-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12Z)-octadeca-9,12-dien-6-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) a stearidonoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (9Z,12Z,15Z)-octadeca-9,12,15-trien-6-ynoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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Glossary: | γ-linolenoate = (6Z,9Z,12Z)-octadeca-6,9,12-trienoate stearidonate = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoate dicranin = (9Z,12Z,15Z)-octadeca-9,12,15-trien-6-ynoic acid |
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Systematic name: | Δ6 acyl-lipid,ferrocytochrome-b5:oxygen oxidoreductase (6,7-dehydrogenating) | |||||||||||||||
Comments: | The enzyme, characterized from the moss Ceratodon purpureus, converts the double bond at position 6 of γ-linolenate and stearidonate into a triple bond. The product of the latter, dicranin, is the main fatty acid found in C. purpureus. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The enzyme also has the activity of EC 1.14.19.47, acyl-lipid (9-3)-desaturase. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 1.14.19.31 | Relevance: 24.1% | ||||||||||||||
Accepted name: | acyl-lipid (7-3)-desaturase | |||||||||||||||
Reaction: | (1) a (7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) a (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
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Glossary: | (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoate = adrenate | |||||||||||||||
Other name(s): | D4Des (gene name); des1 (gene name); CrΔ4FAD (gene name); acyl-lipid 4-desaturase | |||||||||||||||
Systematic name: | Δ7 acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase (4,5 cis-dehydrogenating) | |||||||||||||||
Comments: | The enzymes from several algae introduce a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Δ7 double bond. The enzyme from the fresh water alga Chlamydomonas reinhardtii acts on the 16 carbon fatty acid (7Z,10Z,13Z)-hexadeca-7,10,13-trienoate [5]. The enzyme contains an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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EC | 2.3.1.129 | Relevance: 24.1% | ||||||||||||||
Accepted name: | acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase | |||||||||||||||
Reaction: | a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-α-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine | |||||||||||||||
For diagram of lipid IVA biosynthesis, click here | ||||||||||||||||
Other name(s): | lpxA (gene name); UDP-N-acetylglucosamine acyltransferase; uridine diphosphoacetylglucosamine acyltransferase; acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase; (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase | |||||||||||||||
Systematic name: | (3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-N-acetyl-α-D-glucosamine 3-O-(3-hydroxyacyl)transferase | |||||||||||||||
Comments: | Involved with EC 2.4.1.182, lipid-A-disaccharide synthase, and EC 2.7.1.130, tetraacyldisaccharide 4′-kinase, in the biosynthesis of the phosphorylated glycolipid, Lipid A, in the outer membrane of Gram-negative bacteria. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105843-69-4 | |||||||||||||||
References: |
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EC | 2.3.2.30 | Relevance: 23.5% | ||||||||||||||
Accepted name: | L-ornithine Nα-acyltransferase | |||||||||||||||
Reaction: | L-ornithine + a (3R)-3-hydroxyacyl-[acyl-carrier protein] = a lyso-ornithine lipid + a holo-[acyl-carrier protein] | |||||||||||||||
Glossary: | a lyso-ornithine lipid = an Nα-[(3R)-hydroxy-acyl]-L-ornithine | |||||||||||||||
Other name(s): | olsB (gene name) | |||||||||||||||
Systematic name: | L-ornithine Nα-(3R)-3-hydroxy-acyltransferase | |||||||||||||||
Comments: | The enzyme, found in bacteria, catalyses the first step in the biosynthesis of ornithine lipids. | |||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||||
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