The Enzyme Database

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EC 1.3.1.70     
Accepted name: Δ14-sterol reductase
Reaction: 4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol + NADP+ = 4,4-dimethyl-5α-cholesta-8,14,24-trien-3β-ol + NADPH + H+
For diagram of the modification of sterol rings B, C and D, click here
Systematic name: 4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol:NADP+ Δ14-oxidoreductase
Comments: This enzyme acts on a range of steroids with a 14(15)-double bond.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69403-07-2
References:
1.  Bottema, C.K. and Parks, L.W. Δ14-Sterol reductase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 531 (1978) 301–307. [DOI] [PMID: 32908]
2.  Paik, Y.K., Trzaskos, J.M., Shafice, A. and Gaylor, J.L. Microsomal enzymes of cholesterol biosynthesis from lanosterol. Characterization, solubilization, and partial purification of NADPH-dependent Δ8,14-steroid 14-reductase. J. Biol. Chem. 259 (1984) 13413–13423. [PMID: 6444198]
[EC 1.3.1.70 created 2001]
 
 
EC 1.3.1.72     
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 1.14.1.3      
Deleted entry: squalene hydroxylase. Activity is covered by EC 1.14.99.7, squalene monooxygenase and EC 5.4.99.7, lanosterol synthase
[EC 1.14.1.3 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, deleted 1972]
 
 
EC 1.14.13.70      
Transferred entry: sterol 14α-demethylase. Now EC 1.14.14.154, sterol 14α-demethylase
[EC 1.14.13.70 created 2001, modified 2013, deleted 2018]
 
 
EC 1.14.13.72      
Transferred entry: methylsterol monooxygenase. Now classified as EC 1.14.18.9, methylsterol monooxygenase
[EC 1.14.13.72 created 1972 as EC 1.14.99.16, transferred 2002 to EC 1.14.13.72, deleted 2017]
 
 
EC 1.14.13.132      
Transferred entry: squalene monooxygenase. Now EC 1.14.14.17, squalene monooxygenase
[EC 1.14.13.132 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7, transferred 2011 to EC 1.14.13.132, deleted 2015]
 
 
EC 1.14.13.246     
Accepted name: 4β-methylsterol monooxygenase
Reaction: a 3β-hydroxy-4,4-dimethylsteroid + 3 NADH + 3 H+ + 3 O2 = a 3β-hydroxy-4α-methylsteroid-4β-carboxylate + 3 NAD+ + 4 H2O (overall reaction)
(1a) a 3β-hydroxy-4,4-dimethylsteroid + NADH + H+ + O2 = a 3β-hydroxy-4β-hydroxymethyl-4α-methylsteroid + NAD+ + H2O
(1b) a 3β-hydroxy-4β-hydroxymethyl-4α-methylsteroid + NADH + H+ + O2 = a 3β-hydroxy-4β-formyl-4α-methylsteroid + NAD+ + 2 H2O
(1c) a 3β-hydroxy-4β-formyl-4α-methylsteroid + NADH + H+ + O2 = a 3β-hydroxy-4α-methylsteroid-4β-carboxylate + NAD+ + H2O
Other name(s): sdmA (gene name)
Systematic name: 3β-hydroxy-4,4-dimethylsteroid,NADH:oxygen oxidoreductase (C-4mβ-hydroxylating)
Comments: Contains a Rieske [2Fe-2S] iron-sulfur cluster. This bacterial enzyme (SdmA) participates in the biosynthesis of bacterial sterols. Together with SdmB it forms an enzyme system that removes one methyl group from the C-4 position of 4,4-dimethylated steroid molecules. SdmA catalyses three successive oxidations of the C-4β methyl group, turning it into a carboxylate group; the second enzyme, SdmB, is a bifunctional enzyme that catalyses two different activities. As EC 1.1.1.417, 3β-hydroxysteroid-4β-carboxylate 3-dehydrogenase (decarboxylating), it catalyses an oxidative decarboxylation that results in reduction of the 3β-hydroxy group at the C-3 carbon to an oxo group. As EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase, it reduces the 3-oxo group back to a 3β-hydroxyl. Unlike the animal/fungal enzyme EC 1.14.18.9, 4α-methylsterol monooxygenase, and the plant enzymes EC 1.14.18.10, plant 4,4-dimethylsterol C-4α-methyl-monooxygenase, and EC 1.14.18.11, plant 4α-monomethylsterol monooxygenase, this enzyme acts preferentially on the 4β-methyl group. Since no epimerization of the remaining C-4α methyl group occurs, the enzyme can only remove one methyl group, leaving a 4α-monomethylated product. Known substrates include 4,4-dimethyl-5α-cholest-8-en-3β-ol and 14-demethyllanosterol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, A.K., Banta, A.B., Wei, J.H., Kiemle, D.J., Feng, J., Giner, J.L. and Welander, P.V. C-4 sterol demethylation enzymes distinguish bacterial and eukaryotic sterol synthesis. Proc. Natl. Acad. Sci. USA 115 (2018) 5884–5889. [PMID: 29784781]
[EC 1.14.13.246 created 2019]
 
 
EC 1.14.14.17     
Accepted name: squalene monooxygenase
Reaction: squalene + [reduced NADPH—hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of α-onocerin biosynthesis, click here and for diagram of triterpenoid biosynthesis, click here
Other name(s): squalene epoxidase; squalene-2,3-epoxide cyclase; squalene 2,3-oxidocyclase; squalene hydroxylase; squalene oxydocyclase; squalene-2,3-epoxidase
Systematic name: squalene,NADPH—hemoprotein:oxygen oxidoreductase (2,3-epoxidizing)
Comments: A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7, lanosterol synthase, was formerly known as squalene oxidocyclase. The electron donor is EC 1.6.2.4, NADPH—hemoprotein reductase [5,7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-62-3
References:
1.  Corey, E.J., Russey, W.E. and Ortiz de Montellano, P.R. 2,3-Oxidosqualene, an intermediate in the biological synthesis of sterols from squalene. J. Am. Chem. Soc. 88 (1966) 4750–4751. [PMID: 5918046]
2.  Tchen, T.T. and Bloch, K. On the conversion of squalene to lanosterol in vitro. J. Biol. Chem. 226 (1957) 921–930. [PMID: 13438881]
3.  van Tamelen, E.E., Willett, J.D., Clayton, R.B. and Lord, K.E. Enzymic conversion of squalene 2,3-oxide to lanosterol and cholesterol. J. Am. Chem. Soc. 88 (1966) 4752–4754. [PMID: 5918048]
4.  Yamamoto, S. and Bloch, K. Studies on squalene epoxidase of rat liver. J. Biol. Chem. 245 (1970) 1670–1674. [PMID: 5438357]
5.  Ono, T. and Bloch, K. Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. 250 (1975) 1571–1579. [PMID: 234459]
6.  Satoh, T., Horie, M., Watanabe, H., Tsuchiya, Y. and Kamei, T. Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae. Biol. Pharm. Bull. 16 (1993) 349–352. [PMID: 8358382]
7.  Chugh, A., Ray, A. and Gupta, J.B. Squalene epoxidase as hypocholesterolemic drug target revisited. Prog. Lipid Res. 42 (2003) 37–50. [DOI] [PMID: 12467639]
8.  He, F., Zhu, Y., He, M. and Zhang, Y. Molecular cloning and characterization of the gene encoding squalene epoxidase in Panax notoginseng. DNA Seq 19 (2008) 270–273. [DOI] [PMID: 17852349]
[EC 1.14.14.17 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7, transferred 2011 to EC 1.14.13.132, transferred 2015 to EC 1.14.14.17]
 
 
EC 1.14.14.154     
Accepted name: sterol 14α-demethylase
Reaction: a 14α-methylsteroid + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = a Δ14-steroid + formate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) a 14α-methylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-hydroxymethylsteroid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 14α-hydroxysteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-formylsteroid + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) a 14α-formylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a Δ14-steroid + formate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of sterol ring B, C, D modification, click here
Glossary: obtusifoliol = 4α,14α-dimethyl-5α-ergosta-8,24(28)-dien-3β-ol or 4α,14α-dimethyl-24-methylene-5α-cholesta-8-en-3β-ol
Other name(s): obtusufoliol 14-demethylase; lanosterol 14-demethylase; lanosterol 14α-demethylase; sterol 14-demethylase; CYP51 (gene name); ERG11 (gene name)
Systematic name: sterol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)
Comments: This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14α-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-87-8
References:
1.  Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R. The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis. J. Chem. Soc. Chem. Commun. (1972) 383–385.
2.  Yoshida, Y. and Aoyama, Y. Yeast cytochrome P-450 catalyzing lanosterol 14 α-demethylation. I. Purification and spectral properties. J. Biol. Chem. 259 (1984) 1655–1660. [PMID: 6363414]
3.  Aoyama, Y., Yoshida, Y. and Sato, R. Yeast cytochrome P-450 catalyzing lanosterol 14 α-demethylation. II. Lanosterol metabolism by purified P-45014DM and by intact microsomes. J. Biol. Chem. 259 (1984) 1661–1666. [PMID: 6420412]
4.  Aoyama, Y. and Yoshida, Y. Different substrate specificities of lanosterol 14α-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol. Biochem. Biophys. Res. Commun. 178 (1991) 1064–1071. [DOI] [PMID: 1872829]
5.  Aoyama, Y. and Yoshida, Y. The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases. Biochem. Biophys. Res. Commun. 183 (1992) 1266–1272. [DOI] [PMID: 1567403]
6.  Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11 (1997) 191–201. [DOI] [PMID: 9076987]
[EC 1.14.14.154 created 2001 as EC 1.14.13.70, modified 2013, transferred 2018 EC 1.14.14.154]
 
 
EC 1.14.15.36     
Accepted name: sterol 14α-demethylase (ferredoxin)
Reaction: a 14α-methylsteroid + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = a Δ14-steroid + formate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O (overall reaction)
(1a) a 14α-methylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14α-hydroxymethylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) a 14α-hydroxymethylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a 14α-formylsteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1c) a 14α-formylsteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = a Δ14-steroid + formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Other name(s): cyp51 (gene name)
Systematic name: sterol,reduced ferredoxin:oxygen oxidoreductase (14-methyl cleaving)
Comments: A cytochrome P-450 (heme-thiolate) protein found in several bacterial species. The enzyme, which is involved in sterol biosynthesis, catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. The enzyme from Methylococcus capsulatus is fused to the ferredoxin by an alanine-rich linker. cf. EC 1.14.14.154, sterol 14α-demethylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jackson, C.J., Lamb, D.C., Marczylo, T.H., Warrilow, A.G., Manning, N.J., Lowe, D.J., Kelly, D.E. and Kelly, S.L. A novel sterol 14α-demethylase/ferredoxin fusion protein (MCCYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J. Biol. Chem. 277 (2002) 46959–46965. [PMID: 12235134]
2.  Rezen, T., Debeljak, N., Kordis, D. and Rozman, D. New aspects on lanosterol 14α-demethylase and cytochrome P450 evolution: lanosterol/cycloartenol diversification and lateral transfer. J. Mol. Evol. 59 (2004) 51–58. [PMID: 15383907]
3.  Desmond, E. and Gribaldo, S. Phylogenomics of sterol synthesis: insights into the origin, evolution, and diversity of a key eukaryotic feature. Genome Biol Evol 1 (2009) 364–381. [PMID: 20333205]
[EC 1.14.15.36 created 2019]
 
 
EC 1.14.18.9     
Accepted name: 4α-methylsterol monooxygenase
Reaction: 4,4-dimethyl-5α-cholest-7-en-3β-ol + 6 ferrocytochrome b5 + 3 O2 + 6 H+ = 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carboxylate + 6 ferricytochrome b5 + 4 H2O (overall reaction)
(1a) 4,4-dimethyl-5α-cholest-7-en-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-hydroxymethyl-4β-methyl-5α-cholest-7-en-3β-ol + 2 ferricytochrome b5 + H2O
(1b) 4α-hydroxymethyl-4β-methyl-5α-cholest-7-en-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carbaldehyde + 2 ferricytochrome b5 + 2 H2O
(1c) 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carbaldehyde + 2 ferrocytochrome b5 + O2 + 2 H+ = 3β-hydroxy-4β-methyl-5α-cholest-7-ene-4α-carboxylate + 2 ferricytochrome b5 + H2O
For diagram of sterol ring A modification, click here
Other name(s): methylsterol hydroxylase (ambiguous); 4-methylsterol oxidase (ambiguous); 4,4-dimethyl-5α-cholest-7-en-3β-ol,hydrogen-donor:oxygen oxidoreductase (hydroxylating) (ambiguous); methylsterol monooxygenase (ambiguous); ERG25 (gene name); MSMO1 (gene name); 4,4-dimethyl-5α-cholest-7-en-3β-ol,ferrocytochrome-b5:oxygen oxidoreductase (hydroxylating) (ambiguous)
Systematic name: 4,4-dimethyl-5α-cholest-7-en-3β-ol,ferrocytochrome-b5:oxygen oxidoreductase (C4α-methyl-hydroxylating)
Comments: This enzyme is found in fungi and animals and catalyses a step in the biosynthesis of important sterol molecules such as ergosterol and cholesterol, respectively. The enzyme acts on the 4α-methyl group. Subsequent decarboxylation by EC 1.1.1.170, 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating), occurs concomitantly with epimerization of the remaining 4β-methyl into the 4α position, thus making it a suitable substrate for a second round of catalysis. cf. EC 1.14.13.246, 4β-methylsterol monooxygenase; EC 1.14.18.10, plant 4,4-dimethylsterol C-4α-methyl-monooxygenase; and EC 1.14.18.11, plant 4α-monomethylsterol monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-80-7
References:
1.  Miller, W.L., Kalafer, M.E., Gaylor, J.L. and Delwicke, C.V. Investigation of the component reactions of oxidative sterol demethylation. Study of the aerobic and anaerobic processes. Biochemistry 6 (1967) 2673–2678. [PMID: 4383278]
2.  Gaylor, J.L. and Mason, H.S. Investigation of the component reactions of oxidative sterol demethylation. Evidence against participation of cytochrome P-450. J. Biol. Chem. 243 (1968) 4966–4972. [PMID: 4234469]
3.  Sharpless, K.B., Snyder, T.E., Spencer, T.A., Maheshwari, K.K. and Nelson, J.A. Biological demethylation of 4,4-dimethyl sterols, Evidence for enzymic epimerization of the 4β-methyl group prior to its oxidative removal. J. Am. Chem. Soc. 91 (1969) 3394–3396. [PMID: 5791927]
4.  Brady, D.R., Crowder, R.D. and Hayes, W.J. Mixed function oxidases in sterol metabolism. Source of reducing equivalents. J. Biol. Chem. 255 (1980) 10624–10629. [PMID: 7430141]
5.  Fukushima, H., Grinstead, G.F. and Gaylor, J.L. Total enzymic synthesis of cholesterol from lanosterol. Cytochrome b5-dependence of 4-methyl sterol oxidase. J. Biol. Chem. 256 (1981) 4822–4826. [PMID: 7228857]
6.  Kawata, S., Trzaskos, J.M. and Gaylor, J.L. Affinity chromatography of microsomal enzymes on immobilized detergent-solubilized cytochrome b5. J. Biol. Chem. 261 (1986) 3790–3799. [PMID: 3949790]
[EC 1.14.18.9 created 1972 as EC 1.14.99.16, transferred 2002 to EC 1.14.13.72, transferred 2017 to EC 1.14.18.9, modified 2019]
 
 
EC 1.14.99.7      
Transferred entry: squalene monooxygenase. Transferred to EC 1.14.13.132, squalene monooxygenase.
[EC 1.14.99.7 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 1.14.99.7 rest to EC 5.4.99.7, deleted 2011]
 
 
EC 1.99.1.13      
Deleted entry: squalene cyclohydroxylase, covered by EC 1.14.99.7 (squalene monooxygenase) and by EC 5.4.99.7 (lanosterol synthase)
[EC 1.99.1.13 created 1961, deleted 1965]
 
 
EC 5.4.99.7     
Accepted name: lanosterol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol
For diagram of lanosterol and cycloartenol biosynthesis, click here
Other name(s): 2,3-epoxysqualene lanosterol cyclase; squalene-2,3-oxide-lanosterol cyclase; lanosterol 2,3-oxidosqualene cyclase; squalene 2,3-epoxide:lanosterol cyclase; 2,3-oxidosqualene sterol cyclase; oxidosqualene cyclase; 2,3-oxidosqualene cyclase; 2,3-oxidosqualene-lanosterol cyclase; oxidosqualene-lanosterol cyclase; squalene epoxidase-cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lanosterol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-71-7
References:
1.  Dean, P.D.G., Oritz de Montellano, P.R., Bloch, K. and Corey, E.J. A soluble 2,3-oxidosqualene sterol cyclase. J. Biol. Chem. 242 (1967) 3014–3015. [PMID: 6027261]
[EC 5.4.99.7 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 5.4.99.7 rest to EC 1.14.99.7]
 
 
EC 5.4.99.8     
Accepted name: cycloartenol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = cycloartenol
For diagram of lanosterol and cycloartenol biosynthesis, click here
Other name(s): 2,3-epoxysqualene cycloartenol-cyclase; squalene-2,3-epoxide-cycloartenol cyclase; 2,3-epoxysqualene-cycloartenol cyclase; 2,3-oxidosqualene-cycloartenol cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, cycloartenol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-25-6
References:
1.  Rees, H.H., Goad, L.J. and Goodwin, T.W. 2,3-Oxidosqualene cycloartenol cyclase from Ochromonas malhamensis. Biochim. Biophys. Acta 176 (1969) 892–894. [DOI] [PMID: 5797101]
[EC 5.4.99.8 created 1972]
 
 
EC 5.4.99.32     
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 5.4.99.33     
Accepted name: cucurbitadienol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = cucurbitadienol
For diagram of cucurbitadienol, cycloartenol, lanosterol and prostadienol biosynthesis, click here
Other name(s): CPQ (gene name); (S)-2,3-epoxysqualene mutase (cyclizing, cucurbitadienol-forming)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, cucurbitadienol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Adachi, S., and Ebizuka, Y. Cucurbitadienol synthase, the first committed enzyme for cucurbitacin biosynthesis, is a distinct enzyme from cycloartenol synthase for phytosterol biosynthesis. Tetrahedron 60 (2004) 6995–7003.
[EC 5.4.99.33 created 2011]
 
 
EC 5.4.99.47     
Accepted name: parkeol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = parkeol
For diagram of cucurbitadienol, cycloartenol, lanosterol and prostadienol biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, parkeol-forming)
Comments: The enzyme from rice (Oryza sativa) produces parkeol as a single product [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ito, R., Mori, K., Hashimoto, I., Nakano, C., Sato, T. and Hoshino, T. Triterpene cyclases from Oryza sativa L.: cycloartenol, parkeol and achilleol B synthases. Org. Lett. 13 (2011) 2678–2681. [DOI] [PMID: 21526825]
[EC 5.4.99.47 created 2011]
 
 


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