Information on EC 1.14.13.153 - (+)-sabinene 3-hydroxylase

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The expected taxonomic range for this enzyme is: Salvia officinalis

EC NUMBER
COMMENTARY hide
1.14.13.153
-
RECOMMENDED NAME
GeneOntology No.
(+)-sabinene 3-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(+)-sabinene + NADPH + H+ + O2 = (+)-cis-sabinol + NADP+ + H2O
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
(+)-sabinene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Requires cytochrome P-450. The enzyme has been characterized from Salvia officinalis (sage).
CAS REGISTRY NUMBER
COMMENTARY hide
110639-27-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme is a cytochrome P-450-dependent mixed function oxygenase and belongs to the cytochrome P450 oxygenase family
metabolism
-
the enzyme catalyzes the synthesis of (+)-cis-sabinol, which is a key step in the biosynthesis of C3-oxygenated thujane monoterpenes, overview
additional information
-
(+)-sabinene is a major olefinic constituent of the volatile oil of immature Salvia oficinalis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-sabinene + NADPH + H+ + O2
(+)-cis-sabinol + NADP+ + H2O
show the reaction diagram
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
(+)-sabinene + NADPH + H+ + O2
(+)-cis-sabinol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no effect on enzyme activity by 1-10 mM of Mg2+, Mn2+, Ca2+, Cu2+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO
-
photoreversible inhibition
NADP+
-
NADP+ competitively inhibits P-450-dependent reactions, 40-45% inhibition of hydroxylation at 2 mM
octyl beta-D-glucoside
-
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
sodium cholate
-
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Sodium deoxycholate
-
80% inhibition at 0.06% detergent
sodium taurocholate
-
13% inhibition at 0.30% detergent
sodium taurodeoxycholate
-
91% inhibition at 0.06% detergent
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
exogenous, activates the enzyme slightly
FMN
-
exogenous, activates the enzyme
octyl beta-D-glucoside
-
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
sodium cholate
-
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Zwittergent 3-08
-
12% activation at 0.24% detergent
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.6
-
50% of maximal activity at pH 6.8 and pH 8.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
etiolated
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
localization of sabinene hydroxylase in sage leaf homogenates by differential centrifugation indicated that activity is restricted to light membranes
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Manually annotated by BRENDA team