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Your query returned 15 entries. Printable version
EC | 1.2.1.31 | ||||||||||||||||||
Accepted name: | L-aminoadipate-semialdehyde dehydrogenase | ||||||||||||||||||
Reaction: | (S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ (overall reaction) (1a) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous) (1b) (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD(P)+ + 2 H2O = L-2-aminoadipate + NAD(P)H + H+ |
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For diagram of lysine catabolism, click here and for diagram of L-Lysine synthesis, click here | |||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate |
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Other name(s): | aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate δ-semialdehyde oxidoreductase; L-α-aminoadipate δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase; L-2-aminoadipate 6-semialdehyde:NAD(P)+ 6-oxidoreductase | ||||||||||||||||||
Systematic name: | (S)-2-amino-6-oxohexanoate:NAD(P)+ 6-oxidoreductase | ||||||||||||||||||
Comments: | (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-87-2 | ||||||||||||||||||
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EC | 1.2.1.95 | ||||||||||||||||||
Accepted name: | L-2-aminoadipate reductase | ||||||||||||||||||
Reaction: | (S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP (overall reaction) (1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP (1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+ |
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Glossary: | L-2-aminoadipate = (2S)-2-aminohexanedioate | ||||||||||||||||||
Other name(s): | LYS2; α-aminoadipate reductase | ||||||||||||||||||
Systematic name: | (S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming) | ||||||||||||||||||
Comments: | This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
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EC | 1.4.1.18 | ||||||||||||||||||
Accepted name: | lysine 6-dehydrogenase | ||||||||||||||||||
Reaction: | L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction) (1a) L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3 (1b) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous) |
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For diagram of reaction, click here and for diagram of L-lysine synthesis, click here | |||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate |
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Other name(s): | L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH | ||||||||||||||||||
Systematic name: | L-lysine:NAD+ 6-oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 89400-30-6 | ||||||||||||||||||
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EC | 1.4.3.13 | ||||||||||||||||||
Accepted name: | protein-lysine 6-oxidase | ||||||||||||||||||
Reaction: | [protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2 | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-allysine | ||||||||||||||||||
Other name(s): | lysyl oxidase | ||||||||||||||||||
Systematic name: | protein-L-lysine:oxygen 6-oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate [6]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99676-44-5 | ||||||||||||||||||
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EC | 1.4.3.20 | ||||||||||||||||||
Accepted name: | L-lysine 6-oxidase | ||||||||||||||||||
Reaction: | L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3 | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine | ||||||||||||||||||
Other name(s): | L-lysine-ε-oxidase; Lod; LodA; marinocine | ||||||||||||||||||
Systematic name: | L-lysine:oxygen 6-oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is also a substrate, but N6-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1116448-48-6 | ||||||||||||||||||
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EC | 1.5.1.9 | ||||||||||||||||||
Accepted name: | saccharopine dehydrogenase (NAD+, L-glutamate-forming) | ||||||||||||||||||
Reaction: | N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ | ||||||||||||||||||
Glossary: | saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
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Other name(s): | dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) | ||||||||||||||||||
Systematic name: | N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) | ||||||||||||||||||
Comments: | The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-26-1 | ||||||||||||||||||
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EC | 1.5.1.10 | ||||||||||||||||||
Accepted name: | saccharopine dehydrogenase (NADP+, L-glutamate-forming) | ||||||||||||||||||
Reaction: | N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+ | ||||||||||||||||||
Glossary: | L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
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Other name(s): | saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) | ||||||||||||||||||
Systematic name: | N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-55-0 | ||||||||||||||||||
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EC | 1.5.3.7 | ||||||||||||||||||
Accepted name: | L-pipecolate oxidase | ||||||||||||||||||
Reaction: | L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 | ||||||||||||||||||
Glossary: | L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
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Other name(s): | pipecolate oxidase; L-pipecolic acid oxidase | ||||||||||||||||||
Systematic name: | L-pipecolate:oxygen 1,6-oxidoreductase | ||||||||||||||||||
Comments: | The product reacts with water to form (S)-2-amino-6-oxohexanoate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81669-65-0 | ||||||||||||||||||
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EC | 1.5.3.18 | ||||||||||||||||||
Accepted name: | L-saccharopine oxidase | ||||||||||||||||||
Reaction: | N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 = (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2 | ||||||||||||||||||
Glossary: | L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
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Other name(s): | FAP2 | ||||||||||||||||||
Systematic name: | L-saccharopine:oxygen oxidoreductase (L-glutamate-forming) | ||||||||||||||||||
Comments: | The enzyme is involved in pipecolic acid biosynthesis. A flavoprotein (FAD). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
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EC | 1.5.99.3 | ||||||||||||||||||
Accepted name: | L-pipecolate dehydrogenase | ||||||||||||||||||
Reaction: | L-pipecolate + acceptor = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate |
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Other name(s): | L-pipecolate:(acceptor) 1,6-oxidoreductase | ||||||||||||||||||
Systematic name: | L-pipecolate:acceptor 1,6-oxidoreductase | ||||||||||||||||||
Comments: | The product reacts with water to form (S)-2-amino-6-oxohexanoate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-63-5 | ||||||||||||||||||
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EC | 2.6.1.36 | ||||||||||||||||||
Accepted name: | L-lysine 6-transaminase | ||||||||||||||||||
Reaction: | L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate |
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Other name(s): | lysine 6-aminotransferase; lysine ε-aminotransferase; lysine ε-transaminase; lysine:2-ketoglutarate 6-aminotransferase; L-lysine-α-ketoglutarate aminotransferase; L-lysine-α-ketoglutarate 6-aminotransferase | ||||||||||||||||||
Systematic name: | L-lysine:2-oxoglutarate 6-aminotransferase | ||||||||||||||||||
Comments: | A pyridoxal-phosphate protein. The product (L-allysine) is converted into the intramolecularly dehydrated form, (S)-2,3,4,5-tetrahydropyridine-2-carboxylate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-68-6 | ||||||||||||||||||
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EC | 2.6.1.71 | ||||||||||||||||||
Accepted name: | lysine—pyruvate 6-transaminase | ||||||||||||||||||
Reaction: | L-lysine + pyruvate = (S)-2-amino-6-oxohexanoate + L-alanine | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine | ||||||||||||||||||
Other name(s): | lysine-pyruvate aminotransferase; Lys-AT | ||||||||||||||||||
Systematic name: | L-lysine:pyruvate aminotransferase | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114189-79-6 | ||||||||||||||||||
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EC | 2.6.1.105 | ||||||||||||||||||
Accepted name: | lysine—8-amino-7-oxononanoate transaminase | ||||||||||||||||||
Reaction: | L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate | ||||||||||||||||||
Glossary: | (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine | ||||||||||||||||||
Other name(s): | DAPA aminotransferase (ambiguous); bioA (gene name) (ambiguous); bioK (gene name) | ||||||||||||||||||
Systematic name: | L-lysine:8-amino-7-oxononanoate aminotransferase | ||||||||||||||||||
Comments: | A pyridoxal 5′-phosphate enzyme [2]. Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine—8-amino-7-oxononanoate transaminase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
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EC | 2.6.1.121 | ||||||||||||||||||
Accepted name: | 8-amino-7-oxononanoate carboxylating dehydrogenase | ||||||||||||||||||
Reaction: | (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + CO2 = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate (overall reaction) (1a) (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + NAD(P)H + H+ = [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + H2O + NAD(P)+ (1b) [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + CO2 + H2O + NAD(P)+ = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate + NAD(P)H + H+ |
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Other name(s): | bioU (gene name) | ||||||||||||||||||
Systematic name: | (8S)-8-amino-7-oxononanoate:[protein]-L-lysine aminotransferase (N-carboxylating) | ||||||||||||||||||
Comments: | The enzyme, which participates in biotin biosynthesis, is found in haloarchaea and some cyanobacteria. It forms a conjugant between (7R,8S)-8-amino-7-oxononanoate and an internal lysine residue and catalyses multiple reactions, including a reduction, a carboxylation of the ε-amino group of the lysine residue, and an oxidative cleavage of the conjugate to release (7R,8S)-8-amino-7-(carboxyamino)nonanoate. During this process the lysine residue serves as an amino donor and is converted to (S)-2-amino-6-oxohexanoate, resulting in inactivation of the enzyme following a single turnover. cf. EC 2.6.1.105, lysine—8-amino-7-oxononanoate transaminase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
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EC | 4.2.3.134 | ||||||||||||||||||
Accepted name: | 5-phosphooxy-L-lysine phospho-lyase | ||||||||||||||||||
Reaction: | (5R)-5-phosphooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH3 + phosphate | ||||||||||||||||||
Other name(s): | 5-phosphohydroxy-L-lysine ammoniophospholyase; AGXT2L2 (gene name); (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming); 5-phosphonooxy-L-lysine phospho-lyase | ||||||||||||||||||
Systematic name: | (5R)-5-phosphooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming) | ||||||||||||||||||
Comments: | A pyridoxal-phosphate protein. Has no activity with phosphoethanolamine (cf. EC 4.2.3.2, ethanolamine-phosphate phospho-lyase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
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