EC |
2.5.1.137 | Relevance: 100% |
Accepted name: |
2-acyl-4-prenylphloroglucinol 6-prenyltransferase |
Reaction: |
(1) prenyl diphosphate + a 2-acyl-4-prenylphloroglucinol = diphosphate + a 2-acyl-4,6-bis(prenyl)phloroglucinol (2) prenyl diphosphate + a 2-acyl-4,6-bis(prenyl)phloroglucinol = diphosphate + a 2-acyl-4,6,6-tris(prenyl)cyclohexa-2,4-dien-1-one |
|
|
Glossary: |
a 2-acyl-4,6,6-tris(prenyl)cyclohexa-2,4-dien-1-one = a β bitter acid |
Other name(s): |
PT2 (gene name); aromatic prenyltransferase (ambiguous); dimethylallyl-diphosphate:2-acyl-4-prenylphloroglucinol 6-dimethylallyltransferase |
Systematic name: |
prenyl-diphosphate:2-acyl-4-prenylphloroglucinol 6-prenyltransferase |
Comments: |
The enzyme, characterized from hop (Humulus lupulus), catalyses two successive prenylations of a 2-acyl-4-prenylphloroglucinol during the synthesis of bitter acids. Forms a complex with EC 2.5.1.136, 2-acylphloroglucinol 4-prenyltransferase, which catalyses the initial prenylation of the substrates. Requires Mg2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, H., Ban, Z., Qin, H., Ma, L., King, A.J. and Wang, G. A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway. Plant Physiol. 167 (2015) 650–659. [DOI] [PMID: 25564559] |
|
[EC 2.5.1.137 created 2017] |
|
|
|
|
EC |
4.2.3.166 | Relevance: 84.1% |
Accepted name: |
(+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol + diphosphate |
|
For diagram of biosynthesis of ent-germacrene sesquiterpenoids, click here |
Glossary: |
(+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol = (1S,2E,6E,10R)-3,7-dimethyl-10-(propan-2-yl)cyclodeca-2,6-dien-1-ol |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [cyclizing, (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol-forming] |
Comments: |
The enzyme has been identified in the bacterium Streptomyces pratensis. It is specific for (2E,6E)-farnesyl diphosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rabe, P., Barra, L., Rinkel, J., Riclea, R., Citron, C.A., Klapschinski, T.A., Janusko, A. and Dickschat, J.S. Conformational analysis, thermal rearrangement, and EI-MS fragmentation mechanism of ((1(10)E,4E,6S,7R)-germacradien-6-ol by 13C-labeling experiments. Angew. Chem. Int. Ed. Engl. 54 (2015) 13448–13451. [DOI] [PMID: 26361082] |
|
[EC 4.2.3.166 created 2017] |
|
|
|
|
EC
|
1.14.99.28
|
Transferred entry: | linalool 8-monooxygenase. Now EC 1.14.14.84, linalool 8-monooxygenase
|
[EC 1.14.99.28 created 1989, deleted 2012] |
|
|
|
|
EC |
3.1.7.10 | Relevance: 78.8% |
Accepted name: |
(13E)-labda-7,13-dien-15-ol synthase |
Reaction: |
geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol + diphosphate |
|
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here and for diagram of sclareol and (13e)-labda-7,13-dien-15-ol biosynthesis, click here |
Other name(s): |
labda-7,13E-dien-15-ol synthase |
Systematic name: |
geranylgeranyl-diphosphate diphosphohydrolase [(13E)-labda-7,13-dien-15-ol-forming] |
Comments: |
The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolysed to the alcohol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mafu, S., Hillwig, M.L. and Peters, R.J. A novel labda-7,13E-dien-15-ol-producing bifunctional diterpene synthase from Selaginella moellendorffii. ChemBioChem 12 (2011) 1984–1987. [DOI] [PMID: 21751328] |
|
[EC 3.1.7.10 created 2012] |
|
|
|
|
EC |
5.4.99.56 | Relevance: 78% |
Accepted name: |
tirucalladienol synthase |
Reaction: |
(3S)-2,3-epoxy-2,3-dihydrosqualene = tirucalla-7,24-dien-3β-ol |
|
For diagram of dammarenediol II and tirucalla-7,24-dien-3β-ol biosynthesis, click here |
Other name(s): |
PEN3 |
Systematic name: |
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, tirucalla-7,24-dien-3β-ol-forming) |
Comments: |
The product from Arabidopsis thaliana is 85% tirucalla-7,24-dien-3β-ol with trace amounts of other triterpenoids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Morlacchi, P., Wilson, W.K., Xiong, Q., Bhaduri, A., Sttivend, D., Kolesnikova, M.D. and Matsuda, S.P. Product profile of PEN3: the last unexamined oxidosqualene cyclase in Arabidopsis thaliana. Org. Lett. 11 (2009) 2627–2630. [DOI] [PMID: 19445469] |
|
[EC 5.4.99.56 created 2011] |
|
|
|
|
EC
|
1.14.13.109
|
Transferred entry: | abieta-7,13-dien-18-ol hydroxylase. Now EC 1.14.14.145, abieta-7,13-dien-18-ol hydroxylase
|
[EC 1.14.13.109 created 2009, modified 2012, deleted 2018] |
|
|
|
|
EC |
1.14.13.146 | Relevance: 73% |
Accepted name: |
taxoid 14β-hydroxylase |
Reaction: |
10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + O2 + NADPH + H+ = 10β,14β-dihydroxytaxa-4(20),11-dien-5α-yl acetate + NADP+ + H2O |
|
For diagram of taxadiene hydroxylation, click here |
Systematic name: |
10β-hydroxytaxa-4(20),11-dien-5α-yl-acetate,NADPH:oxygen 14-oxidoreductase |
Comments: |
Requires cytochrome P450. From the yew Taxus cuspidata. Also acts on taxa-4(20),11-dien-5α-yl acetate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R. Taxoid metabolism: Taxoid 14β-hydroxylase is a cytochrome P450-dependent monooxygenase. Arch. Biochem. Biophys. 413 (2003) 262–270. [DOI] [PMID: 12729625] |
|
[EC 1.14.13.146 created 2012] |
|
|
|
|
EC
|
1.14.13.144
|
Transferred entry: | 9β-pimara-7,15-diene oxidase. Now EC 1.14.14.111, 9β-pimara-7,15-diene oxidase.
|
[EC 1.14.13.144 created 2012, deleted 2018] |
|
|
|
|
EC |
2.3.1.274 | Relevance: 72.6% |
Accepted name: |
phosphate acyltransferase |
Reaction: |
an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein] |
Other name(s): |
plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase |
Systematic name: |
an acyl-[acyl-carrier protein]:phosphate acyltransferase |
Comments: |
The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765–772. [PMID: 16949372] |
2. |
Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7:69 (2007). [PMID: 17645809] |
3. |
Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157–163. [PMID: 19058030] |
4. |
Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59–66. [PMID: 29199103] |
|
[EC 2.3.1.274 created 2018] |
|
|
|
|
EC |
5.4.99.32 | Relevance: 72.4% |
Accepted name: |
protostadienol synthase |
Reaction: |
(3S)-2,3-epoxy-2,3-dihydrosqualene = (17Z)-protosta-17(20),24-dien-3β-ol |
|
For diagram of cucurbitadienol, cycloartenol, lanosterol and prostadienol biosynthesis, click here |
Other name(s): |
PdsA; (S)-2,3-epoxysqualene mutase [cyclizing, (17Z)-protosta-17(20),24-dien-3β-ol-forming] |
Systematic name: |
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase [cyclizing, (17Z)-protosta-17(20),24-dien-3β-ol-forming] |
Comments: |
(17Z)-Protosta-17(20),24-dien-3β-ol is a precursor of the steroidal antibiotic helvolic acid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lodeiro, S., Xiong, Q., Wilson, W.K., Ivanova, Y., Smith, M.L., May, G.S. and Matsuda, S.P. Protostadienol biosynthesis and metabolism in the pathogenic fungus Aspergillus fumigatus. Org. Lett. 11 (2009) 1241–1244. [DOI] [PMID: 19216560] |
|
[EC 5.4.99.32 created 2011] |
|
|
|
|
EC |
1.14.14.145 | Relevance: 72.3% |
Accepted name: |
abieta-7,13-dien-18-ol hydroxylase |
Reaction: |
abieta-7,13-dien-18-ol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = abieta-7,13-dien-18-oate + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction) (1a) abieta-7,13-dien-18-ol + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18,18-diol + [oxidized NADPH—hemoprotein reductase] + H2O (1b) abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O (spontaneous) (1c) abieta-7,13-dien-18-al + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-oate + [oxidized NADPH—hemoprotein reductase] + H2O
|
|
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here |
Glossary: |
abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde |
Other name(s): |
CYP720B1; PtAO; abietadienol hydroxylase (ambiguous) |
Systematic name: |
abieta-7,13-dien-18-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [DOI] [PMID: 8311462] |
2. |
Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380] |
3. |
Ro, D.K., Arimura, G., Lau, S.Y., Piers, E. and Bohlmann, J. Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. USA 102 (2005) 8060–8065. [DOI] [PMID: 15911762] |
|
[EC 1.14.14.145 created 2009 as EC 1.14.13.109, modified 2012, transferred 2018 to EC 1.14.14.145] |
|
|
|
|
EC |
5.5.1.16 | Relevance: 72.3% |
Accepted name: |
halimadienyl-diphosphate synthase |
Reaction: |
geranylgeranyl diphosphate = tuberculosinyl diphosphate |
|
For diagram of diterpenoid biosynthesis, click here |
Glossary: |
tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate |
Other name(s): |
Rv3377c; halimadienyl diphosphate synthase; tuberculosinol diphosphate synthase; halima-5(6),13-dien-15-yl-diphosphate lyase (cyclizing); halima-5,13-dien-15-yl-diphosphate lyase (decyclizing) |
Systematic name: |
halima-5,13-dien-15-yl-diphosphate lyase (ring-opening) |
Comments: |
Requires Mg2+ for activity. This enzyme is found in pathogenic prokaryotes such as Mycobacterium tuberculosis but not in non-pathogens such as Mycobacterium smegmatis so may play a role in pathogenicity. The product of the reaction is subsequently dephosphorylated yielding tuberculosinol (halima-5,13-dien-15-ol). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Nakano, C., Okamura, T., Sato, T., Dairi, T. and Hoshino, T. Mycobacterium tuberculosis H37Rv3377c encodes the diterpene cyclase for producing the halimane skeleton. Chem. Commun. (Camb.) (2005) 1016–1018. [DOI] [PMID: 15719101] |
|
[EC 5.5.1.16 created 2008, modified 2012] |
|
|
|
|
EC |
2.3.1.162 | Relevance: 72% |
Accepted name: |
taxadien-5α-ol O-acetyltransferase |
Reaction: |
acetyl-CoA + taxa-4(20),11-dien-5α-ol = CoA + taxa-4(20),11-dien-5α-yl acetate |
|
For diagram of taxadiene biosynthesis, click here |
Other name(s): |
acetyl coenzyme A:taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase |
Systematic name: |
acetyl-CoA:taxa-4(20),11-dien-5α-ol O-acetyltransferase |
Comments: |
This is the third enzyme in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel), which is widely used in the treatment of carcinomas, sarcomas and melanomas. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 229032-29-5 |
References: |
1. |
Walker, K., Ketchum, R.E., Hezari, M., Gatfield, D., Goleniowski, M., Barthol, A. and Croteau, R. Partial purification and characterization of acetyl coenzyme A: taxa-4(20),11(12)-dien-5α-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis. Arch. Biochem. Biophys. 364 (1999) 273. [DOI] [PMID: 10190984] |
2. |
Walker, K., Schoendorf, A. and Croteau, R. Molecular cloning of a taxa-4(20),11(12)-dien-5α-ol-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coli. Arch. Biochem. Biophys. 374 (2000) 371–380. [DOI] [PMID: 10666320] |
|
[EC 2.3.1.162 created 2002] |
|
|
|
|
EC |
1.2.1.74 | Relevance: 71.9% |
Accepted name: |
abieta-7,13-dien-18-al dehydrogenase |
Reaction: |
abieta-7,13-dien-18-al + H2O + NAD+ = abieta-7,13-dien-18-oate + NADH + H+ |
|
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here |
Glossary: |
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
abieta-7,13-dien-18-oate = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carboxylate |
Other name(s): |
abietadienal dehydrogenase (ambiguous) |
Systematic name: |
abieta-7,13-dien-18-al:NAD+ oxidoreductase |
Comments: |
Abietic acid is the principle component of conifer resin. This enzyme catalyses the last step of the pathway of abietic acid biosynthesis in Abies grandis (grand fir). The activity has been demonstrated in cell-free stem extracts of A. grandis, was present in the cytoplasm, and required NAD+ as cofactor [1]. The enzyme is expressed constitutively at a high level, and is not inducible by wounding of the plant tissue [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [DOI] [PMID: 8311462] |
2. |
Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380] |
|
[EC 1.2.1.74 created 2009, modified 2012] |
|
|
|
|
EC |
1.14.14.69 | Relevance: 71.4% |
Accepted name: |
ent-cassadiene hydroxylase |
Reaction: |
ent-cassa-12,15-diene + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = ent-3β-hydroxycassa-12,15-dien-2-one + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction) (1a) ent-cassa-12,15-diene + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2β-ol + [oxidized NADPH—hemoprotein reductase] + H2O (1b) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O (1b′) ent-cassa-12,15-dien-2β-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-cassa-12,15-diene-2β,3β-diol + [oxidized NADPH—hemoprotein reductase] + H2O (1c) ent-cassa-12,15-dien-2-one + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + H2O (1c′) ent-cassa-12,15-diene-2β,3β-diol + [reduced NADPH—hemoprotein reductase] + O2 = ent-3β-hydroxycassa-12,15-dien-2-one + [oxidized NADPH—hemoprotein reductase] + 2 H2O |
|
For diagram of ent-hydroxycassadiene biosynthesis, click here |
Other name(s): |
CYP71Z7 |
Systematic name: |
ent-cassa-12,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ent-3β-hydroxycassa-12,15-dien-2-one-forming) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein isolated from the plant Oryza sativa (rice) that is involved in phytocassanes biosynthesis. Depending on the order of activities, the enzyme may form either ent-cassa-12,15-dien-2-one or ent-cassa-12,15-diene-2β,3β-diol as an intermediate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kitaoka, N., Wu, Y., Xu, M. and Peters, R.J. Optimization of recombinant expression enables discovery of novel cytochrome P450 activity in rice diterpenoid biosynthesis. Appl. Microbiol. Biotechnol. 99 (2015) 7549–7558. [DOI] [PMID: 25758958] |
|
[EC 1.14.14.69 created 2018] |
|
|
|
|
EC |
2.3.1.51 | Relevance: 71.3% |
Accepted name: |
1-acylglycerol-3-phosphate O-acyltransferase |
Reaction: |
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate |
Other name(s): |
1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase |
Systematic name: |
acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase |
Comments: |
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51901-16-7 |
References: |
1. |
Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629–636. [DOI] [PMID: 6825679] |
2. |
Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029] |
3. |
Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123] |
|
[EC 2.3.1.51 created 1976, modified 1990] |
|
|
|
|
EC |
2.3.1.23 | Relevance: 71.1% |
Accepted name: |
1-acylglycerophosphocholine O-acyltransferase |
Reaction: |
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine |
Other name(s): |
lysolecithin acyltransferase; 1-acyl-sn-glycero-3-phosphocholine acyltransferase; acyl coenzyme A-monoacylphosphatidylcholine acyltransferase; acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase; lysophosphatide acyltransferase; lysophosphatidylcholine acyltransferase |
Systematic name: |
acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase |
Comments: |
Acts preferentially with unsaturated acyl-CoA derivatives. 1-Acyl-sn-glycero-3-phosphoinositol can also act as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-64-9 |
References: |
1. |
Bell, R.M. and Coleman, R.A. Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem. 49 (1980) 459–487. [DOI] [PMID: 6250446] |
2. |
Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029] |
3. |
Miki, Y., Hosaka, K., Yamashita, S., Handa, H. and Numa, S. Acyl-acceptor specificities of 1-acylglycerolphosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase resolved from rat liver microsomes. Eur. J. Biochem. 81 (1977) 433–441. [DOI] [PMID: 598375] |
4. |
van den Bosch, H., van Golde, L.M.G., Eibl, H. and van Deenen, L.L.M. The acylation of 1-acylglycero-3-phosphorylcholines by rat-liver microsomes. Biochim. Biophys. Acta 144 (1967) 613–623. [DOI] [PMID: 6078124] |
|
[EC 2.3.1.23 created 1972] |
|
|
|
|
EC |
4.2.3.167 | Relevance: 71.1% |
Accepted name: |
dolabella-3,7-dien-18-ol synthase |
Reaction: |
geranylgeranyl diphosphate + H2O = (3E,7E)-dolabella-3,7-dien-18-ol + diphosphate |
|
For diagram of biosynthesis of fusicoccane diterpenoids, click here |
Glossary: |
(3E,7E)-dolabella-3,7-dien-18-ol = 2-[(1R,3aR,5E,9E,12aR)-3a,6,10-trimethyl-1,2,3,3a,4,7,8,11,12,12a-decahydrocyclopenta[11]annulen-1-yl]propan-2-ol |
Other name(s): |
TPS20 (gene name) |
Systematic name: |
geranylgeranyl-diphosphate diphosphate-lyase [cyclizing, (3E,7E)-dolabella-3,7-dien-18-ol-forming] |
Comments: |
Isolated from an ecotype of the plant Arabidopsis thaliana from Cape Verde Islands. The enzyme also gives (3E,7E)-dolathalia-3,7,11-triene and traces of other terpenoids. cf. EC 4.2.3.168 dolathalia-3,7,11-triene synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wang, Q., Jia, M., Huh, J.H., Muchlinski, A., Peters, R.J. and Tholl, D. Identification of a dolabellane type diterpene synthase and other root-expressed diterpene synthases in Arabidopsis. Front. Plant Sci. 7:1761 (2016). [DOI] [PMID: 27933080] |
|
[EC 4.2.3.167 created 2017] |
|
|
|
|
EC
|
1.14.13.77
|
Transferred entry: | taxane 13α-hydroxylase. Now EC 1.14.14.106, taxane 13α-hydroxylase
|
[EC 1.14.13.77 created 2002, deleted 2018] |
|
|
|
|
EC |
2.3.1.141 | Relevance: 67.6% |
Accepted name: |
galactosylacylglycerol O-acyltransferase |
Reaction: |
an acyl-[acyl-carrier protein] + a 2-acyl-3-O-(β-D-galactosyl)-sn-glycerol = an [acyl-carrier protein] + a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol |
Other name(s): |
acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase; acyl-ACP:lyso-MGDG acyltransferase; acyl-[acyl-carrier-protein]:D-galactosylacylglycerol O-acyltransferase |
Systematic name: |
acyl-[acyl-carrier protein]:2-acyl-3-O-(β-D-galactosyl)-sn-glycerol O-acyltransferase |
Comments: |
Transfers long-chain acyl groups to the sn-1 position of the glycerol residue. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119129-68-9 |
References: |
1. |
Chen, H.-H., Wickrema, A. and Jaworski, J.G. Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase from the cyanobacterium Anabaena variabilis. Biochim. Biophys. Acta 963 (1988) 493–500. [DOI] [PMID: 3143419] |
|
[EC 2.3.1.141 created 1992] |
|
|
|
|
EC |
3.1.2.20 | Relevance: 67.5% |
Accepted name: |
acyl-CoA hydrolase |
Reaction: |
acyl-CoA + H2O = CoA + a carboxylate |
Other name(s): |
acyl coenzyme A thioesterase; acyl-CoA thioesterase; acyl coenzyme A hydrolase; thioesterase B; thioesterase II; acyl-CoA thioesterase |
Systematic name: |
acyl-CoA hydrolase |
Comments: |
Broad specificity for medium- to long-chain acyl-CoA. Insensitive to NAD+ (cf. EC 3.1.2.19 ADP-dependent medium-chain-acyl-CoA hydrolase) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37270-64-7 |
References: |
1. |
Alexson, S.E.H., Svensson, L.T. and Nedergaard, J. NADH-sensitive propionyl-CoA hydrolase in brown-adipose-tissue mitochondria of the rat. Biochim. Biophys. Acta 1005 (1989) 13–19. [DOI] [PMID: 2570608] |
|
[EC 3.1.2.20 created 1992] |
|
|
|
|
EC |
1.14.14.46 | Relevance: 67.3% |
Accepted name: |
pimeloyl-[acyl-carrier protein] synthase |
Reaction: |
a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction) (1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O (1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O (1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O (1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+ |
Glossary: |
a long-chain acyl-[acyl-carrier protein] = an acyl-[acyl-carrier protein] thioester where the acyl chain contains 13 to 22 carbon atoms.
palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein] |
Other name(s): |
bioI (gene name); P450BioI; CYP107H1 |
Systematic name: |
acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein]-forming) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351–360. [DOI] [PMID: 11368323] |
2. |
Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86–87. [DOI] [PMID: 14737344] |
3. |
Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696–15701. [DOI] [PMID: 18838690] |
4. |
Cryle, M.J. Selectivity in a barren landscape: the P450(BioI)-ACP complex. Biochem. Soc. Trans. 38 (2010) 934–939. [DOI] [PMID: 20658980] |
|
[EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46] |
|
|
|
|
EC |
3.1.2.14 | Relevance: 67.1% |
Accepted name: |
oleoyl-[acyl-carrier-protein] hydrolase |
Reaction: |
an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate |
Other name(s): |
acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase; oleoyl-[acyl-carrier-protein] hydrolase |
Systematic name: |
oleoyl-[acyl-carrier protein] hydrolase |
Comments: |
Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68009-83-6 |
References: |
1. |
Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382–391. [DOI] [PMID: 30409] |
2. |
Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins. Arch. Biochem. Biophys. 172 (1976) 110–116. [DOI] [PMID: 3134] |
|
[EC 3.1.2.14 created 1984] |
|
|
|
|
EC
|
1.14.15.12
|
Transferred entry: | pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase
|
[EC 1.14.15.12 created 2013, deleted 2017] |
|
|
|
|
EC |
3.1.2.21 | Relevance: 66.3% |
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: |
1. |
Pollard, M.R., Anderson, L., Fan, C., Hawkins, D.J., Davies, H.M. A specific acyl-ACP thioesterase implicated in medium-chain fatty acid production in immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 284 (1991) 306–312. [DOI] [PMID: 1989513] |
2. |
Davies, H.M., Anderson, L., Fan, C., Hawkins, D.J. Developmental induction, purification, and further characterization of 12:0-ACP thioesterase from immature cotyledons of Umbellularia californica. Arch. Biochem. Biophys. 290 (1991) 37–45. [DOI] [PMID: 1898097] |
|
[EC 3.1.2.21 created 1999] |
|
|
|
|
EC
|
1.14.13.76
|
Transferred entry: | taxane 10β-hydroxylase. Now EC 1.14.14.105, taxane 10β-hydroxylase
|
[EC 1.14.13.76 created 2002, deleted 2018] |
|
|
|
|
EC |
1.3.3.6 | Relevance: 66.1% |
Accepted name: |
acyl-CoA oxidase |
Reaction: |
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 |
Other name(s): |
fatty acyl-CoA oxidase; acyl coenzyme A oxidase; fatty acyl-coenzyme A oxidase |
Systematic name: |
acyl-CoA:oxygen 2-oxidoreductase |
Comments: |
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61116-22-1 |
References: |
1. |
Kawaguchi, A., Tsubotani, S., Seyama, Y., Yamakawa, T., Osumi, T., Hashimoto, T., Kikuchi, T., Ando, M. and Okuda, S. Stereochemistry of dehydrogenation catalyzed by acyl-CoA oxidase. J. Biochem. (Tokyo) 88 (1980) 1481–1486. [PMID: 7462191] |
2. |
Osumi, T., Hashimoto, T. and Ui, N. Purification and properties of acyl-CoA oxidase from rat liver. J. Biochem. (Tokyo) 87 (1980) 1735–1746. [PMID: 7400120] |
|
[EC 1.3.3.6 created 1986] |
|
|
|
|
EC |
1.3.1.10 | Relevance: 65.3% |
Accepted name: |
enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) |
Reaction: |
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ |
Other name(s): |
acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) |
Systematic name: |
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific) |
Comments: |
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37251-09-5 |
References: |
1. |
Seyama, T., Kasama, T., Yamakawa, T., Kawaguchi, A., Saito, K. and Okuda, S. Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase. J. Biochem. (Tokyo) 82 (1977) 1325–1329. [PMID: 338601] |
|
[EC 1.3.1.10 created 1972, modified 1986, modified 2013, modified 2014, modified 2018] |
|
|
|
|
EC |
2.3.3.20 | Relevance: 65.2% |
Accepted name: |
acyl-CoA:acyl-CoA alkyltransferase |
Reaction: |
2 an acyl-CoA + H2O = a (2R)-2-alkyl-3-oxoalkanoate + 2 CoA |
Other name(s): |
oleA (gene name) |
Systematic name: |
acyl-CoA:acyl-CoA alkyltransferase [(2R)-2-alkyl-3-oxoalkanoate-forming] |
Comments: |
The enzyme, found in certain bacterial species, catalyses a head-to-head non-decarboxylative Claisen condensation of two acyl-CoA molecules, resulting in formation of a 2-alkyl-3-oxoalkanoic acid. It is part of a pathway for the production of olefins. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Sukovich, D.J., Seffernick, J.L., Richman, J.E., Hunt, K.A., Gralnick, J.A. and Wackett, L.P. Structure, function, and insights into the biosynthesis of a head-to-head hydrocarbon in Shewanella oneidensis strain MR-1. Appl. Environ. Microbiol. 76 (2010) 3842–3849. [DOI] [PMID: 20418444] |
2. |
Frias, J.A., Richman, J.E., Erickson, J.S. and Wackett, L.P. Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction. J. Biol. Chem. 286 (2011) 10930–10938. [DOI] [PMID: 21266575] |
3. |
Goblirsch, B.R., Frias, J.A., Wackett, L.P. and Wilmot, C.M. Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids. Biochemistry 51 (2012) 4138–4146. [DOI] [PMID: 22524624] |
4. |
Goblirsch, B.R., Jensen, M.R., Mohamed, F.A., Wackett, L.P. and Wilmot, C.M. Substrate trapping in crystals of the thiolase OleA identifies three channels that enable long chain olefin biosynthesis. J. Biol. Chem. 291 (2016) 26698–26706. [DOI] [PMID: 27815501] |
|
[EC 2.3.3.20 created 2018] |
|
|
|
|
EC |
1.14.18.11 | Relevance: 64.8% |
Accepted name: |
plant 4α-monomethylsterol monooxygenase |
Reaction: |
24-methylidenelophenol + 6 ferrocytochrome b5 + 3 O2 + 6 H+ = 3β-hydroxyergosta-7,24(241)-dien-4α-carboxylate + 6 ferricytochrome b5 + 4 H2O (overall reaction) (1a) 24-methylidenelophenol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-(hydroxymethyl)ergosta-7,24(241)-dien-3β-ol + 2 ferricytochrome b5 + H2O (1b) 4α-(hydroxymethyl)ergosta-7,24(241)-dien-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-formylergosta-7,24(241)-dien-3β-ol + 2 ferricytochrome b5 + 2 H2O (1c) 4α-formylergosta-7,24(241)-dien-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 3β-hydroxyergosta-7,24(241)-dien-4α-carboxylate + 2 ferricytochrome b5 + H2O |
Glossary: |
24-methylidenelophenol = 4α-methyl-5α-ergosta-7,24-dien-3β-ol |
Other name(s): |
SMO2 (gene name) |
Systematic name: |
24-ethylidenelophenol,ferrocytochrome-b5:oxygen oxidoreductase (C-4α-methyl-hydroxylating) |
Comments: |
This plant enzyme catalyses a step in the biosynthesis of sterols. It acts on the methyl group of the 4α-methylated intermediates 24-ethylidenelophenol and 24-methylidenelophenol and catalyses three successive oxidations, turning it into a carboxyl group. The carboxylate is subsequently removed by EC 1.1.1.418, plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating). Unlike the fungal/animal enzyme EC 1.14.18.9, 4α-methylsterol monooxygenase, this enzyme is not able to act on 4,4-dimethylated substrates. That activity, which occurs earlier in the pathway, is performed in plants by a second enzyme, EC 1.14.18.10, plant 4,4-dimethylsterol C-4α-methyl-monooxygenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Pascal, S., Taton, M. and Rahier, A. Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation. J. Biol. Chem. 268 (1993) 11639–11654. [PMID: 8505296] |
2. |
Rahier, A., Smith, M. and Taton, M. The role of cytochrome b5 in 4α-methyl-oxidation and C5(6) desaturation of plant sterol precursors. Biochem. Biophys. Res. Commun. 236 (1997) 434–437. [DOI] [PMID: 9240456] |
3. |
Darnet, S., Bard, M. and Rahier, A. Functional identification of sterol-4α-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4α-methyl oxidation. FEBS Lett. 508 (2001) 39–43. [PMID: 11707264] |
4. |
Darnet, S. and Rahier, A. Plant sterol biosynthesis: identification of two distinct families of sterol 4α-methyl oxidases. Biochem. J. 378 (2004) 889–898. [PMID: 14653780] |
|
[EC 1.14.18.11 created 2019] |
|
|
|
|
EC |
1.3.1.87 | Relevance: 64.7% |
Accepted name: |
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase |
Reaction: |
(1) 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+ = 3-(2,3-dihydroxyphenyl)propanoate + NADH + H+ (2) (2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD+ = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NADH + H+ |
|
For diagram of 3-phenylpropanoate catabolism, click here and for diagram of cinnamate catabolism, click here |
Glossary: |
(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate |
Other name(s): |
hcaB (gene name); cis-dihydrodiol dehydrogenase; 2,3-dihydroxy-2,3-dihydro-phenylpropionate dehydrogenase |
Systematic name: |
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate:NAD+ oxidoreductase |
Comments: |
This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
References: |
1. |
Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915–2923. [PMID: 9603882] |
|
[EC 1.3.1.87 created 2011] |
|
|
|
|
EC |
1.3.1.72 | Relevance: 64.5% |
Accepted name: |
Δ24-sterol reductase |
Reaction: |
5α-cholest-7-en-3β-ol + NADP+ = 5α-cholesta-7,24-dien-3β-ol + NADPH + H+ |
|
For diagram of sterol-sidechain modification, click here |
Glossary: |
desmosterol = cholesta-5,24-dien-3β-ol
lanosterol = 4,4,14-trimethyl-5α-cholesta-8,24-dien-3β-ol
zymostrol = 5α-cholesta-8,24-dien-3β-ol |
Other name(s): |
lanosterol Δ24-reductase |
Systematic name: |
sterol:NADP+ Δ24-oxidoreductase |
Comments: |
Acts on a range of steroids with a 24(25)-double bond, including lanosterol, desmosterol and zymosterol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-57-2 |
References: |
1. |
Bae, S.H. and Paik, Y.K. Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol Δ24-reductase. Biochem. J. 326 (1997) 609–616. [PMID: 9291139] |
|
[EC 1.3.1.72 created 2001] |
|
|
|
|
EC |
1.14.14.111 | Relevance: 64.3% |
Accepted name: |
9β-pimara-7,15-diene oxidase |
Reaction: |
9β-pimara-7,15-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction) (1a) 9β-pimara-7,15-diene + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-ol + [oxidized NADPH—hemoprotein reductase] + H2O (1b) 9β-pimara-7,15-dien-19-ol + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O (1c) 9β-pimara-7,15-dien-19-al + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O
|
|
For diagram of momilactone A biosynthesis, click here |
Glossary: |
syn-pimara-7,15-diene = 9β-pimara-7,15-diene |
Other name(s): |
CYP99A3; 9β-pimara-7,15-diene monooxygenase |
Systematic name: |
9β-pimara-7,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen 19-oxidoreductase |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the phytoalexin momilactone. It also acts similarly on 9β-stemod-13(17)-ene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wang, Q., Hillwig, M.L. and Peters, R.J. CYP99A3: functional identification of a diterpene oxidase from the momilactone biosynthetic gene cluster in rice. Plant J. 65 (2011) 87–95. [DOI] [PMID: 21175892] |
|
[EC 1.14.14.111 created 2012 as EC 1.14.13.144, transferred 2018 to EC 1.14.14.111] |
|
|
|
|
EC
|
1.3.99.3
|
Transferred entry: | acyl-CoA dehydrogenase, now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase
|
[EC 1.3.99.3 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, deleted 2012] |
|
|
|
|
EC |
2.3.1.52 | Relevance: 63.8% |
Accepted name: |
2-acylglycerol-3-phosphate O-acyltransferase |
Reaction: |
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate |
Other name(s): |
2-acylglycerophosphate acyltransferase |
Systematic name: |
acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase |
Comments: |
Saturated acyl-CoA thioesters are the most effective acyl donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51901-17-8 |
References: |
1. |
Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123] |
|
[EC 2.3.1.52 created 1976] |
|
|
|
|
EC |
2.3.1.38 | Relevance: 63.7% |
Accepted name: |
[acyl-carrier-protein] S-acetyltransferase |
Reaction: |
acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein] |
|
For diagram of malonate decarboxylase, click here |
Other name(s): |
acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]-acetyltransferase; [ACP]-acetyltransferase; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase |
Systematic name: |
acetyl-CoA:[acyl-carrier protein] S-acetyltransferase |
Comments: |
This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4]. This is one of the activities associated with β-ketoacyl-[acyl-carrier-protein] synthase III (EC 2.3.1.180) [5]. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-16-2 |
References: |
1. |
Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013] |
2. |
Vance, D.E., Mituhashi, O. and Bloch, K. Purification and properties of the fatty acid synthetase from Mycobacterium phlei. J. Biol. Chem. 248 (1973) 2303–2309. [PMID: 4698221] |
3. |
Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326–2332. [DOI] [PMID: 5330116] |
4. |
Lowe, P.N. and Rhodes, S. Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. Biochem. J. 250 (1988) 789–796. [PMID: 3291856] |
5. |
Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein
synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 (1992) 6807–6814. [PMID: 1551888] |
6. |
Rangan, V.S. and Smith, S. Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J. Biol. Chem. 272 (1997) 11975–11978. [DOI] [PMID: 9115261] |
|
[EC 2.3.1.38 created 1972, modified 2006] |
|
|
|
|
EC |
3.1.4.14 | Relevance: 63.6% |
Accepted name: |
[acyl-carrier-protein] phosphodiesterase |
Reaction: |
holo-[acyl-carrier protein] + H2O = 4′-phosphopantetheine + apo-[acyl-carrier protein] |
Other name(s): |
ACP hydrolyase; ACP phosphodiesterase; AcpH; [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase; holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase |
Systematic name: |
holo-[acyl-carrier protein] 4′-pantetheine-phosphohydrolase |
Comments: |
The enzyme cleaves acyl-[acyl-carrier-protein] species with acyl chains of 6-16 carbon atoms although it appears to demonstrate a preference for the unacylated acyl-carrier protein (ACP) and short-chain ACPs over the medium- and long-chain species [3]. Deletion of the gene encoding this enzyme abolishes ACP cofactor turnover in vivo [3]. Activation of apo-ACP to form the holoenzyme is carried out by EC 2.7.8.7, holo-[acyl-carrier-protein] synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-21-4 |
References: |
1. |
Sobhy, C. Regulation of fatty acid synthetase activity. The 4′-phosphopantetheine hydrolase of rat liver. J. Biol. Chem. 254 (1979) 8561–8566. [DOI] [PMID: 224058] |
2. |
Vagelos, P.R. and Larrabee, A.R. Acyl carrier protein. IX. Acyl carrier protein hydrolase. J. Biol. Chem. 242 (1967) 1776–1781. [DOI] [PMID: 4290442] |
3. |
Thomas, J. and Cronan, J.E. The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization. J. Biol. Chem. 280 (2005) 34675–34683. [DOI] [PMID: 16107329] |
|
[EC 3.1.4.14 created 1972, modified 2006] |
|
|
|
|
EC |
1.3.8.9 | Relevance: 63.2% |
Accepted name: |
very-long-chain acyl-CoA dehydrogenase |
Reaction: |
a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms. |
Other name(s): |
ACADVL (gene name). |
Systematic name: |
very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and Hashimoto, T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 1027–1033. [PMID: 1730632] |
2. |
Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K. and Hashimoto, T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest. 95 (1995) 2465–2473. [DOI] [PMID: 7769092] |
3. |
McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J. and Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 283 (2008) 9435–9443. [DOI] [PMID: 18227065] |
|
[EC 1.3.8.9 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.9] |
|
|
|
|
EC |
2.3.1.41 | Relevance: 63% |
Accepted name: |
β-ketoacyl-[acyl-carrier-protein] synthase I |
Reaction: |
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] |
Glossary: |
acyl-[acyl-carrier protein] = R-CO-[acyl-carrier protein]
malonyl-[acyl-carrier protein] = HOOC-CH2-CO-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] = R-CO-CH2-CO-[acyl-carrier protein] |
Other name(s): |
β-ketoacyl-ACP synthase I; β-ketoacyl synthetase; β-ketoacyl-ACP synthetase; β-ketoacyl-acyl carrier protein synthetase; β-ketoacyl-[acyl carrier protein] synthase; β-ketoacylsynthase; condensing enzyme (ambiguous); 3-ketoacyl-acyl carrier protein synthase; fatty acid condensing enzyme; acyl-malonyl(acyl-carrier-protein)-condensing enzyme; acyl-malonyl acyl carrier protein-condensing enzyme; β-ketoacyl acyl carrier protein synthase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl:ACP synthase I; KASI; KAS I; FabF1; FabB; acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating) |
Systematic name: |
acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating) |
Comments: |
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, β-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Δ9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-10-5 |
References: |
1. |
Alberts, A.W., Majerus, P.W. and Vagelos, P.R. Acetyl-CoA acyl carrier protein transacylase. Methods Enzymol. 14 (1969) 50–53. [DOI] |
2. |
Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [DOI] [PMID: 4561013] |
3. |
Toomey, R.E. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli. J. Biol. Chem. 241 (1966) 1159–1165. [PMID: 5327099] |
4. |
D'Agnolo, G., Rosenfeld, I.S. and Vagelos, P.R. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250 (1975) 5289–5294. [PMID: 237914] |
5. |
Garwin, J.L., Klages, A.L. and Cronan, J.E., Jr.. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier
protein synthases I and II of Escherichia coli. J. Biol. Chem. 255 (1980) 11949–11956. [PMID: 7002930] |
6. |
Wang, H. and Cronan, J.E. Functional replacement of the FabA and FabB proteins of Escherichia coli
fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues. J. Biol. Chem. 279 (2004) 34489–34495. [DOI] [PMID: 15194690] |
7. |
Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636. |
|
[EC 2.3.1.41 created 1972, modified 2006] |
|
|
|
|
EC |
1.2.1.80 | Relevance: 62.3% |
Accepted name: |
long-chain acyl-[acyl-carrier-protein] reductase |
Reaction: |
a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+ |
Glossary: |
a long-chain aldehyde = an aldehyde derived from a fatty acid with an aliphatic chain of 13-22 carbons.
an [acyl-carrier protein] = ACP = [acp] |
Other name(s): |
long-chain acyl-[acp] reductase; fatty acyl-[acyl-carrier-protein] reductase; acyl-[acp] reductase |
Systematic name: |
long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming) |
Comments: |
Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Schirmer, A., Rude, M.A., Li, X., Popova, E. and del Cardayre, S.B. Microbial biosynthesis of alkanes. Science 329 (2010) 559–562. [DOI] [PMID: 20671186] |
|
[EC 1.2.1.80 created 2011] |
|
|
|
|
EC |
1.3.1.39 | Relevance: 62.2% |
Accepted name: |
enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) |
Reaction: |
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ |
Other name(s): |
acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific) |
Systematic name: |
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific) |
Comments: |
This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is one of the activities of EC 2.3.1.85, fatty-acid synthase system. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312–6316. [PMID: 4394955] |
2. |
Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612–42618. [DOI] [PMID: 16215233] |
|
[EC 1.3.1.39 created 1986, modified 2013, modified 2018] |
|
|
|
|
EC |
1.3.8.7 | Relevance: 62.2% |
Accepted name: |
medium-chain acyl-CoA dehydrogenase |
Reaction: |
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
a medium-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 6 to 12 carbon atoms. |
Other name(s): |
fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrogenase (ambiguous); medium-chain acyl-coenzyme A dehydrogenase; acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous); ACADM (gene name). |
Systematic name: |
medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [2]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Crane, F.L., Hauge, J.G. and Beinert, H. Flavoproteins involved in the first oxidative step of the fatty acid cycle. Biochim. Biophys. Acta 17 (1955) 292–294. [DOI] [PMID: 13239683] |
2. |
Crane, F.L., Mii, S., Hauge, J.G., Green, D.E. and Beinert, H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase. J. Biol. Chem. 218 (1956) 701–716. [PMID: 13295224] |
3. |
Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447–466. |
4. |
Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063] |
5. |
Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718–725. [PMID: 7601336] |
6. |
Kim, J.J., Wang, M. and Paschke, R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. USA 90 (1993) 7523–7527. [DOI] [PMID: 8356049] |
7. |
Peterson, K.L., Sergienko, E.E., Wu, Y., Kumar, N.R., Strauss, A.W., Oleson, A.E., Muhonen, W.W., Shabb, J.B. and Srivastava, D.K. Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules. Biochemistry 34 (1995) 14942–14953. [PMID: 7578106] |
8. |
Toogood, H.S., van Thiel, A., Basran, J., Sutcliffe, M.J., Scrutton, N.S. and Leys, D. Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J. Biol. Chem. 279 (2004) 32904–32912. [DOI] [PMID: 15159392] |
|
[EC 1.3.8.7 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.7] |
|
|
|
|
EC |
1.2.1.84 | Relevance: 62.1% |
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] |
|
[EC 1.2.1.84 created 2012] |
|
|
|
|
EC |
1.14.19.38 | Relevance: 61.5% |
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 |
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 |
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 |
References: |
1. |
Sperling, P., Lee, M., Girke, T., Zähringer, U., Stymne, S. and Heinz, E. A bifunctional Δ6-fatty acyl acetylenase/desaturase from the moss Ceratodon purpureus. A new member of the cytochrome b5 superfamily. Eur. J. Biochem. 267 (2000) 3801–3811. [DOI] [PMID: 10848999] |
|
[EC 1.14.19.38 created 2015] |
|
|
|
|
EC
|
4.2.1.58
|
Deleted entry: | crotonoyl-[acyl-carrier-protein] hydratase. The reaction described is covered by EC 4.2.1.59. |
[EC 4.2.1.58 created 1972, deleted 2012] |
|
|
|
|
EC |
1.3.1.104 | Relevance: 61% |
Accepted name: |
enoyl-[acyl-carrier-protein] reductase (NADPH) |
Reaction: |
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ |
Other name(s): |
acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name) |
Systematic name: |
acyl-[acyl-carrier protein]:NADP+ oxidoreductase |
Comments: |
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Heath, R.J., Su, N., Murphy, C.K. and Rock, C.O. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. 275 (2000) 40128–40133. [DOI] [PMID: 11007778] |
2. |
Kim, K.H., Park, J.K., Ha, B.H., Moon, J.H. and Kim, E.E. Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 246–248. [DOI] [PMID: 17329825] |
3. |
Kim, K.H., Ha, B.H., Kim, S.J., Hong, S.K., Hwang, K.Y. and Kim, E.E. Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis. J. Mol. Biol. 406 (2011) 403–415. [DOI] [PMID: 21185310] |
|
[EC 1.3.1.104 created 2013] |
|
|
|
|
EC |
1.14.14.106 | Relevance: 60.6% |
Accepted name: |
taxane 13α-hydroxylase |
Reaction: |
taxa-4(20),11-dien-5α-ol + [reduced NADPH—hemoprotein reductase] + O2 = taxa-4(20),11-dien-5α,13α-diol + [oxidized NADPH—hemoprotein reductase] + H2O |
|
For diagram of taxadiene hydroxylation, click here |
Other name(s): |
CYP725A2 (gene name) |
Systematic name: |
taxa-4(20),11-dien-5α-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (13α-hydroxylating) |
Comments: |
This cytochrome-P-450(heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 399030-58-1 |
References: |
1. |
Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [DOI] [PMID: 11396929] |
2. |
Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [DOI] [PMID: 11707604] |
|
[EC 1.14.14.106 created 2002 as EC 1.14.13.77, transferred 2018 to EC 1.14.14.106] |
|
|
|
|
EC |
4.2.3.22 | Relevance: 60.3% |
Accepted name: |
germacradienol synthase |
Reaction: |
(2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate |
|
For diagram of germacrene-derived sesquiterpenoid biosynthesis, click here |
Other name(s): |
germacradienol/germacrene-D synthase; 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming] |
Systematic name: |
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming] |
Comments: |
Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate [2]. Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16 geosmin synthase), a widely occurring metabolite of many streptomycetes, bacteria and fungi [2]. Also catalyses the reaction of EC 4.2.3.75, (-)-germacrene D synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 211049-88-6 |
References: |
1. |
Cane, D.E. and Watt, R.M. Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 1547–1551. [DOI] [PMID: 12556563] |
2. |
He, X. and Cane, D.E. Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2). J. Am. Chem. Soc. 126 (2004) 2678–2679. [DOI] [PMID: 14995166] |
3. |
Gust, B., Challis, G.L., Fowler, K., Kieser, T. and Chater, K.F. PCR-targeted Streptomyces gene replacement identifies a protein domain
needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. USA 100 (2003) 1541–1546. [DOI] [PMID: 12563033] |
|
[EC 4.2.3.22 created 2006, modified 2011] |
|
|
|
|
EC |
5.3.3.19 | Relevance: 60.3% |
Accepted name: |
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase |
Reaction: |
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate = 3-[(1E,4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
|
|
For diagram of bacilysin biosynthesis, click here |
Glossary: |
L-anticapsin = 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine |
Other name(s): |
BacB |
Systematic name: |
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase |
Comments: |
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme can interconvert the (E) isomer formed in the reaction into the (Z) isomer [2], although this isomerization is not part of the pathway leading to bacilysin [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Mahlstedt, S.A. and Walsh, C.T. Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis. Biochemistry 49 (2010) 912–923. [DOI] [PMID: 20052993] |
2. |
Parker, J.B. and Walsh, C.T. Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis. Biochemistry 51 (2012) 3241–3251. [DOI] [PMID: 22483065] |
3. |
Parker, J.B. and Walsh, C.T. Action and timing of BacC and BacD in the late stages of biosynthesis of the dipeptide antibiotic bacilysin. Biochemistry 52 (2013) 889–901. [DOI] [PMID: 23317005] |
|
[EC 5.3.3.19 created 2015] |
|
|
|
|
EC |
2.3.1.40 | Relevance: 59.8% |
Accepted name: |
acyl-[acyl-carrier-protein]—phospholipid O-acyltransferase |
Reaction: |
an acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = an [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine |
Other name(s): |
acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine O-acyltransferase |
Systematic name: |
acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O-acyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-18-4 |
References: |
1. |
Taylor, S.S. and Heath, E.C. The incorporation of β-hydroxy fatty acids into a phospholipid of Escherichia coli B. J. Biol. Chem. 244 (1969) 6605–6616. [PMID: 4902888] |
|
[EC 2.3.1.40 created 1972] |
|
|
|
|