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Your query returned 18 entries. Printable version
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, PDB, CAS registry number: 69403-07-2 | ||||||||||||||||
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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 |
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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 | ||||||||||||||||
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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 | 1.14.13.70 | ||||||||||||||||
Transferred entry: | sterol 14α-demethylase. Now EC 1.14.14.154, sterol 14α-demethylase | ||||||||||||||||
EC | 1.14.13.72 | ||||||||||||||||
Transferred entry: | methylsterol monooxygenase. Now classified as EC 1.14.18.9, methylsterol monooxygenase | ||||||||||||||||
EC | 1.14.13.132 | ||||||||||||||||
Transferred entry: | squalene monooxygenase. Now EC 1.14.14.17, squalene monooxygenase | ||||||||||||||||
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 |
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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 | ||||||||||||||||
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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, PDB, CAS registry number: 9029-62-3 | ||||||||||||||||
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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 |
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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 | ||||||||||||||||
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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 |
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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 | ||||||||||||||||
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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 |
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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 | ||||||||||||||||
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EC | 1.14.99.7 | ||||||||||||||||
Transferred entry: | squalene monooxygenase. Transferred to EC 1.14.13.132, squalene monooxygenase. | ||||||||||||||||
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 | 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 | ||||||||||||||||
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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 | ||||||||||||||||
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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 | ||||||||||||||||
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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 | ||||||||||||||||
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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 | ||||||||||||||||
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