EC |
1.1.1.73 |
Accepted name: |
octanol dehydrogenase |
Reaction: |
octan-1-ol + NAD+ = octanal + NADH + H+ |
Other name(s): |
1-octanol dehydrogenase; octanol:NAD+ oxidoreductase |
Systematic name: |
octan-1-ol:NAD+ oxidoreductase |
Comments: |
Acts, less rapidly, on other long-chain alcohols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-31-6 |
References: |
1. |
Roche, B. and Azoulay, E. Régulation des alcool-déshydrogénases chez Saccharomyces cerevisiae. Eur. J. Biochem. 8 (1969) 426–434. [DOI] [PMID: 4308448] |
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[EC 1.1.1.73 created 1972] |
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EC |
1.1.1.164 |
Accepted name: |
hexadecanol dehydrogenase |
Reaction: |
hexadecanol + NAD+ = hexadecanal + NADH + H+ |
Systematic name: |
hexadecanol:NAD+ oxidoreductase |
Comments: |
The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-59-6 |
References: |
1. |
Kolattukuday, P.E. Reduction of fatty acids to alcohols by cell-free preparations of Euglena gracilis. Biochemistry 9 (1970) 1095–1102. [PMID: 4313936] |
2. |
Stoffel, W., Le Kim, D. and Heyn, G. Metabolism of sphingosine bases. XIV. Sphinganine (dihydrosphingosine), an effective donor of the alk-1-enyl chain of plasmalogens. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 875–883. [PMID: 5432753] |
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[EC 1.1.1.164 created 1976] |
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EC |
1.1.1.192 |
Accepted name: |
long-chain-alcohol dehydrogenase |
Reaction: |
a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+ |
Other name(s): |
long-chain alcohol dehydrogenase; fatty alcohol oxidoreductase |
Systematic name: |
long-chain-alcohol:NAD+ oxidoreductase |
Comments: |
Hexadecanol is a good substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 76774-36-2 |
References: |
1. |
Lee, T.-C. Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver. J. Biol. Chem. 254 (1979) 2892–2896. [PMID: 34610] |
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[EC 1.1.1.192 created 1984] |
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EC |
1.1.3.20 |
Accepted name: |
long-chain-alcohol oxidase |
Reaction: |
a long-chain alcohol + O2 = a long-chain aldehyde + H2O2 |
Other name(s): |
long-chain fatty alcohol oxidase; fatty alcohol oxidase; fatty alcohol:oxygen oxidoreductase; long-chain fatty acid oxidase |
Systematic name: |
long-chain-alcohol:oxygen oxidoreductase |
Comments: |
Oxidizes long-chain fatty alcohols; best substrate is dodecyl alcohol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 129430-50-8 |
References: |
1. |
Moreau, R.A. and Huang, A.H.C. Oxidation of fatty alcohol in the cotyledons of jojoba seedlings. Arch. Biochem. Biophys. 194 (1979) 422–430. [DOI] [PMID: 36040] |
2. |
Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813. |
3. |
Cheng, Q., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Functional identification of AtFao3, a membrane bound long chain alcohol oxidase in Arabidopsis thaliana. FEBS Lett. 574 (2004) 62–68. [DOI] [PMID: 15358540] |
4. |
Zhao, S., Lin, Z., Ma, W., Luo, D. and Cheng, Q. Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in Lotus japonicus. Biotechnol. Prog. 24 (2008) 773–779. [DOI] [PMID: 18396913] |
5. |
Cheng, Q., Sanglard, D., Vanhanen, S., Liu, H.T., Bombelli, P., Smith, A. and Slabas, A.R. Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochim. Biophys. Acta 1735 (2005) 192–203. [DOI] [PMID: 16046182] |
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[EC 1.1.3.20 created 1984, modified 2010] |
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EC |
1.2.1.84 |
Accepted name: |
alcohol-forming fatty acyl-CoA reductase |
Reaction: |
a long-chain acyl-CoA + 2 NADPH + 2 H+ = a long-chain alcohol + 2 NADP+ + CoA |
Glossary: |
a long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 13 to 22 carbon atoms. |
Other name(s): |
FAR (gene name); long-chain acyl-CoA:NADPH reductase |
Systematic name: |
NADPH:long-chain acyl-CoA reductase |
Comments: |
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Metz, J.G., Pollard, M.R., Anderson, L., Hayes, T.R. and Lassner, M.W. Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed. Plant Physiol. 122 (2000) 635–644. [PMID: 10712526] |
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[EC 1.2.1.84 created 2012] |
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EC |
2.3.1.75 |
Accepted name: |
long-chain-alcohol O-fatty-acyltransferase |
Reaction: |
acyl-CoA + a long-chain alcohol = CoA + a long-chain ester |
Other name(s): |
wax synthase; wax-ester synthase |
Systematic name: |
acyl-CoA:long-chain-alcohol O-acyltransferase |
Comments: |
Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64060-40-8 |
References: |
1. |
Wu, X.-Y., Moreau, R.A. and Stumpf, P.K. Studies of biosynthesis of waxes by developing jojoba seed. 3. Biosynthesis of wax esters from acyl-CoA and long-chain alcohols. Lipids 16 (1981) 897–902. |
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[EC 2.3.1.75 created 1984] |
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EC |
2.5.1.26 |
Accepted name: |
alkylglycerone-phosphate synthase |
Reaction: |
1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion |
Glossary: |
a long-chain alcohol = an alcohol derived from a fatty acid with an aliphatic chain of 13-22 carbons.
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Other name(s): |
alkyldihydroxyacetonephosphate synthase; alkyldihydroxyacetone phosphate synthetase; alkyl DHAP synthetase; alkyl-DHAP; dihydroxyacetone-phosphate acyltransferase (ambiguous); DHAP-AT |
Systematic name: |
1-acyl-glycerone-3-phosphate:long-chain-alcohol O-3-phospho-2-oxopropanyltransferase |
Comments: |
The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 64060-42-0, 102484-74-2 |
References: |
1. |
Brown, A.J. and Snyder, F. Alkyldihydroxyacetone-P synthase. Solubilization, partial purification, new assay method, and evidence for a ping-pong mechanism. J. Biol. Chem. 257 (1982) 8835–8839. [PMID: 7096336] |
2. |
Wykle, R.L., Piantadosi, C. and Snyder, F. The role of acyldihydroxyacetone phosphate, reduced nicotinamide adenine dinucleotide, and reduced nicotinamide adenine dinucleotide phosphate in the biosynthesis of O-alkyl glycerolipids by microsomal enzymes of Ehrlich ascites tumor. J. Biol. Chem. 247 (1972) 2944–2948. [PMID: 4401994] |
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[EC 2.5.1.26 created 1984] |
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EC |
3.1.1.50 |
Accepted name: |
wax-ester hydrolase |
Reaction: |
a wax ester + H2O = a long-chain alcohol + a long-chain carboxylate |
Other name(s): |
jojoba wax esterase; WEH |
Systematic name: |
wax-ester acylhydrolase |
Comments: |
Also acts on long-chain acylglycerol, but not diacyl- or triacylglycerols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66625-78-3 |
References: |
1. |
Huang, A.H.C., Moreau, R.A. and Liu, K.D.F. Development and properties of a wax ester hydrolase in the cotyledons of jojoba seedlings. Plant Physiol. 61 (1978) 339–341. [PMID: 16660288] |
2. |
Moreau, R.A. and Huang, A.H.C. Enzymes of wax ester catabolism in jojoba. Methods Enzymol. 71 (1981) 804–813. |
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[EC 3.1.1.50 created 1984] |
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EC |
3.1.1.55 |
Accepted name: |
acetylsalicylate deacetylase |
Reaction: |
acetylsalicylate + H2O = salicylate + acetate |
Other name(s): |
aspirin esterase; aspirin esterase; acetylsalicylic acid esterase; aspirin hydrolase |
Systematic name: |
acetylsalicylate O-acetylhydrolase |
Comments: |
Not identical with EC 3.1.1.1 (carboxylesterase), EC 3.1.1.2 (arylesterase), EC 3.1.1.7 (acetylcholinesterase) or EC 3.1.1.8 (cholinesterase). The activity of the liver cytosol enzyme is highest with acetyl esters of aryl alcohols, and thioesters are also hydrolysed; the microsomal enzyme also hydrolyses some other negatively charged esters, with highest activity on esters of salicylate with long-chain alcohols. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87348-04-7 |
References: |
1. |
Ali, B. and Kaur, S. Mammalian tissue acetylsalicylic acid esterase(s): identification, distribution and discrimination from other esterases. J. Pharmacol. Exp. Ther. 226 (1983) 589–594. [PMID: 6875867] |
2. |
Kim, D.-H., Yang, Y.-S. and Jakoby, W.B. Aspirin hydrolyzing esterases from rat liver cytosol. Biochem. Pharmacol. 40 (1990) 481–487. [DOI] [PMID: 2383281] |
3. |
White, K.N. and Hope, D.B. Partial purification and characterization of a microsomal carboxylesterase specific for salicylate esters from guinea-pig liver. Biochim. Biophys. Acta 785 (1984) 138–147. [DOI] [PMID: 6704404] |
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[EC 3.1.1.55 created 1986, modified 1989] |
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