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Literature summary for 1.14.14.176 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
Search for more literature for 1.14.14.176

Activating Compound

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

Application

Application Comment Organism
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
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

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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

Organism UniProt Comment Textmining
Taxus brevifolia
-
-
-
Taxus cuspidata
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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

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

Cofactor

Cofactor Comment Organism Structure
NADPH absolutely required Taxus cuspidata
NADPH absolutely required Taxus brevifolia