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Literature summary extracted from

  • Hefner, J.; Rubenstein, S.M.; Ketchum, R.E.B.; Gibson, D.M.; Williams, R.M.; Croteau, R.
    Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to taxa-4(20),11(12)-dien-5alpha-ol: the first oxygenation step in taxol biosynthesis (1996), Chem. Biol., 3, 479-489.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.176 FAD saturating amounts increase activity Taxus cuspidata
1.14.14.176 FAD saturating amounts increase activity Taxus brevifolia
1.14.14.176 FMN saturating amounts increase activity Taxus cuspidata
1.14.14.176 FMN saturating amounts increase activity Taxus brevifolia

Application

EC Number Application Comment Organism
1.14.14.176 medicine enzyme may be useful in the biological production of the potent antimitotic drug taxol which shows activity against a range of cancers Taxus cuspidata
1.14.14.176 medicine enzyme may be useful in the biological production of the potent antimitotic drug taxol which shows activity against a range of cancers Taxus brevifolia

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.176 clotrimazole 0.003 mM, complete inhibition Taxus brevifolia
1.14.14.176 clotrimazole 0.003 mM, complete inhibition Taxus cuspidata
1.14.14.176 CO inhibits taxadiene hydroxylation in the dark, inhihibition is partially reversed by blue light at 450 nm Taxus brevifolia
1.14.14.176 CO inhibits taxadiene hydroxylation in the dark, inhihibition is partially reversed by blue light at 450 nm Taxus cuspidata
1.14.14.176 cytochrome c 0.4 mM, 50% inhibition Taxus brevifolia
1.14.14.176 cytochrome c 0.4 mM, 50% inhibition Taxus cuspidata
1.14.14.176 miconazole 0.003 mM, complete inhibition Taxus brevifolia
1.14.14.176 miconazole 0.003 mM, complete inhibition Taxus cuspidata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.176 0.006
-
 taxa-4,11-diene approx. value Taxus cuspidata
1.14.14.176 0.006
-
 taxa-4,11-diene approx. value Taxus brevifolia

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.176 microsome 70% activity resides in light membrane fraction, approx. 25% in dense membrane fraction Taxus cuspidata
-
-
1.14.14.176 microsome 70% activity resides in light membrane fraction, approx. 25% in dense membrane fraction Taxus brevifolia
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 Taxus cuspidata reaction is completely dependent on NADPH, enzyme catalyzes the first oxygenating step in taxol biosynthesis pathway taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 Taxus brevifolia reaction is completely dependent on NADPH, enzyme catalyzes the first oxygenating step in taxol biosynthesis pathway taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.176 Taxus brevifolia
-
-
-
1.14.14.176 Taxus cuspidata
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 = taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O requires P450, reaction includes rearrangement of the 4(5)-double bound to a 4(20)-double bond, possibly through allylic oxidation, proposed mechanism Taxus cuspidata
a
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 = taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O requires P450, reaction includes rearrangement of the 4(5)-double bound to a 4(20)-double bond, possibly through allylic oxidation, proposed mechanism Taxus brevifolia
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.176 cell suspension culture
-
 Taxus cuspidata
-
1.14.14.176 stem
-
 Taxus brevifolia
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 reaction is completely dependent on NADPH Taxus cuspidata taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 reaction is completely dependent on NADPH Taxus brevifolia taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 reaction is completely dependent on NADPH, enzyme catalyzes the first oxygenating step in taxol biosynthesis pathway Taxus cuspidata taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
1.14.14.176 taxa-4,11-diene + [reduced NADPH-hemoprotein reductase] + O2 reaction is completely dependent on NADPH, enzyme catalyzes the first oxygenating step in taxol biosynthesis pathway Taxus brevifolia taxa-4(20),11-dien-5alpha-ol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.176 7.2
-
 activity in extracts, approx. 50% of maximal activity at pH 6.2 and pH 8.2 Taxus cuspidata
1.14.14.176 7.2
-
 activity in extracts, approx. 50% of maximal activity at pH 6.2 and pH 8.2 Taxus brevifolia

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.176 NADPH absolutely required Taxus cuspidata
1.14.14.176 NADPH absolutely required Taxus brevifolia