Information on EC 1.14.13.147 - taxoid 7beta-hydroxylase

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The expected taxonomic range for this enzyme is: Taxus cuspidata

EC NUMBER
COMMENTARY hide
1.14.13.147
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RECOMMENDED NAME
GeneOntology No.
taxoid 7beta-hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
taxusin + O2 + NADPH + H+ = 7beta-hydroxytaxusin + NADP+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2alpha;,7beta-dihydroxylation of taxusin
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SYSTEMATIC NAME
IUBMB Comments
taxusin,NADPH:oxygen 7-oxidoreductase
Requires cytochrome P-450. From the yew tree Taxus cuspidata. Does not act on earlier intermediates in taxol biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-taxusin + O2 + NADPH + H+
7beta-hydroxytaxusin + NADP+ + H2O
show the reaction diagram
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i.e. taxadien-5alpha,9alpha,10beta,13alpha-tetraol tetraacetate
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-
?
taxusin + O2 + NADPH + H+
7beta-hydroxytaxusin + NADP+ + H2O
show the reaction diagram
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-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
taxusin + O2 + NADPH + H+
7beta-hydroxytaxusin + NADP+ + H2O
show the reaction diagram
Q6JTJ0
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0076
(+)-taxusin
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pH 7.5, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
taxhydroxylase activity is slightly higher in HEPES than in Tris-HCl, however, hydrolytic activity (enzymatic deacylation of both substrate and product) is also more prominent in HEPES7
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a Spodoptera fugiperda-baculovirus-based expression system
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