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

for references in articles please use BRENDA:EC1.14.13.153
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The expected taxonomic range for this enzyme is: Salvia officinalis

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EC NUMBER
COMMENTARY hide
1.14.13.153
-
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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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SYSTEMATIC NAME
IUBMB Comments
(+)-sabinene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Requires cytochrome P-450. The enzyme has been characterized from Salvia officinalis (sage).
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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
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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
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(+)-sabinene is a major olefinic constituent of the volatile oil of immature Salvia oficinalis
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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
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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
(+)-sabinene + NADPH + H+ + O2
(+)-cis-sabinol + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO
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photoreversible inhibition
NADP+
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NADP+ competitively inhibits P-450-dependent reactions, 40-45% inhibition of hydroxylation at 2 mM
octyl beta-D-glucoside
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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
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13% inhibition at 0.30% detergent
sodium taurodeoxycholate
-
91% inhibition at 0.06% detergent
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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
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12% activation at 0.24% detergent
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.6
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50% of maximal activity at pH 6.8 and pH 8.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
etiolated
Manually annotated by BRENDA team
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.153)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)