The Enzyme Database

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EC 1.14.13.205      
Transferred entry: long-chain fatty acid ω-monooxygenase. Now EC 1.14.14.80, long-chain fatty acid ω-monooxygenase
[EC 1.14.13.205 created 2015, deleted 2018]
 
 
EC 1.14.13.206      
Transferred entry: laurate 7-monooxygenase. Now EC 1.14.14.130, laurate 7-monooxygenase
[EC 1.14.13.206 created 2015, deleted 2018]
 
 
EC 1.14.14.80     
Accepted name: long-chain fatty acid ω-monooxygenase
Reaction: a long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ω-hydroxy-long-chain fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name)
Systematic name: long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Benveniste, I., Tijet, N., Adas, F., Philipps, G., Salaun, J.P. and Durst, F. CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid ω-hydroxylase. Biochem. Biophys. Res. Commun. 243 (1998) 688–693. [DOI] [PMID: 9500987]
2.  Hoch, U., Zhang, Z., Kroetz, D.L. and Ortiz de Montellano, P.R. Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid ω-hydroxylases. Arch. Biochem. Biophys. 373 (2000) 63–71. [DOI] [PMID: 10620324]
3.  Dobritsa, A.A., Shrestha, J., Morant, M., Pinot, F., Matsuno, M., Swanson, R., Møller, B.L. and Preuss, D. CYP704B1 is a long-chain fatty acid ω-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis. Plant Physiol. 151 (2009) 574–589. [DOI] [PMID: 19700560]
4.  Huang, F.C., Peter, A. and Schwab, W. Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola. Appl. Environ. Microbiol. 80 (2014) 766–776. [DOI] [PMID: 24242247]
[EC 1.14.14.80 created 2015 as EC 1.14.13.205, transferred 2018 to EC 1.14.14.80]
 
 
EC 1.14.14.130     
Accepted name: laurate 7-monooxygenase
Reaction: dodecanoate + [reduced NADPH—hemoprotein reductase] + O2 = 7-hydroxydodecanoate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: laurate = dodecanoate
Other name(s): CYP703A2 (gene name)
Systematic name: dodecanoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the synthesis of sporopollenin - a complex polymer found at the outer layer of spores and pollen. It can also act on decanoate (C10), myristate (C14), and palmitate (C16) with lower activity. The enzyme also produces a small amount of products that are hydroxylated at neighboring positions (C-6, C-8 and C-9).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morant, M., Jørgensen, K., Schaller, H., Pinot, F., Møller, B.L., Werck-Reichhart, D. and Bak, S. CYP703 is an ancient cytochrome P450 in land plants catalyzing in-chain hydroxylation of lauric acid to provide building blocks for sporopollenin synthesis in pollen. Plant Cell 19 (2007) 1473–1487. [DOI] [PMID: 17496121]
[EC 1.14.14.130 created 2015 as EC 1.14.13.206, transferred 2018 to EC 1.14.14.130]
 
 
EC 2.3.1.241     
Accepted name: Kdo2-lipid IVA lauroyltransferase
Reaction: a dodecanoyl-[acyl-carrier protein] + Kdo2-lipid IVA = dodecanoyl-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
dodecanoyl = lauroyl
dodecanoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)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
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
Systematic name: dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Clementz, T., Bednarski, J.J. and Raetz, C.R. Function of the htrB high temperature requirement gene of Escherichia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271 (1996) 12095–12102. [DOI] [PMID: 8662613]
2.  Six, D.A., Carty, S.M., Guan, Z. and Raetz, C.R. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47 (2008) 8623–8637. [DOI] [PMID: 18656959]
[EC 2.3.1.241 created 2014]
 
 
EC 2.3.1.243     
Accepted name: lauroyl-Kdo2-lipid IVA myristoyltransferase
Reaction: a tetradecanoyl-[acyl-carrier protein] + dodecanoyl-Kdo2-lipid IVA = dodecanoyl-(tetradecanoyl)-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
dodecanoyl = lauroyl
tetradecanoyl = myristoyl
dodecanoyl-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)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
dodecanoyl-(tetradecanoyl)-Kdo2-lipid IVA = α-Kdo-(2→4)-α-Kdo-(2→6)-2-deoxy-2-[(3R)-3-(dodecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): MsbB acyltransferase; lpxM (gene name); myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
Systematic name: tetradecanoyl-[acyl-carrier protein]:dodecanoyl-Kdo2-lipid IVA O-tetradecanoyltransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Clementz, T., Zhou, Z. and Raetz, C.R. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB. J. Biol. Chem. 272 (1997) 10353–10360. [DOI] [PMID: 9099672]
[EC 2.3.1.243 created 2014]
 
 
EC 4.1.1.56     
Accepted name: 3-oxolaurate decarboxylase
Reaction: 3-oxododecanoate = 2-undecanone + CO2
Other name(s): β-ketolaurate decarboxylase; β-ketoacyl decarboxylase; 3-oxododecanoate carboxy-lyase
Systematic name: 3-oxododecanoate carboxy-lyase (2-undecanone-forming)
Comments: Also decarboxylates other C14 to C16 oxo acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-49-6
References:
1.  Franke, W., Platzeck, A. and Eichhorn, G. [On the knowledge of fatty acid catabolism by mold fungi. III. On a decarboxylase for average β-ketomonocarbonic acids (β-ketolaurate decarboxylase)] Arch. Mikrobiol. 40 (1961) 73–93. [PMID: 13701396]
[EC 4.1.1.56 created 1972]
 
 


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