Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.14.183 extracted from

  • Chau, M.; Croteau, R.
    Molecular cloning and characterization of a cytochrome P450 taxoid 2alpha-hydroxylase involved in Taxol biosynthesis (2004), Arch. Biochem. Biophys., 427, 48-57 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in yeast Taxus cuspidata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0105
-
taxusin pH 7.8, 31°C Taxus cuspidata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7beta-hydroxytaxusin + [reduced NADPH-hemoprotein reductase] + O2 Taxus cuspidata
-
2alpha,7beta-dihydroxytaxusin + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
taxusin + [reduced NADPH-hemoprotein reductase] + O2 Taxus cuspidata
-
2alpha-hydroxytaxusin + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Organism

Organism UniProt Comment Textmining
Taxus cuspidata
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7beta-hydroxytaxusin + [reduced NADPH-hemoprotein reductase] + O2
-
Taxus cuspidata 2alpha,7beta-dihydroxytaxusin + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
taxusin + [reduced NADPH-hemoprotein reductase] + O2
-
Taxus cuspidata 2alpha-hydroxytaxusin + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Subunits

Subunits Comment Organism
? x * 55000, SDS-PAGE, recombinant protein Taxus cuspidata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
taxusin pH 7.8, 31°C Taxus cuspidata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
-
Taxus cuspidata

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Taxus cuspidata

General Information

General Information Comment Organism
physiological function taxusin is hydroxylated by both taxoid 7beta-hydroxylase and taxoid 2alpha-hydroxylase, and both enzymes are capable of the reciprocal conversion of their respective pentaol tetraacetate products to the hexaol tetraacetate Taxus cuspidata