BRENDA - Enzyme Database
show all sequences of 1.14.13.153

Metabolism of monoterpenes: Demonstration of the hydroxylation of (+)-sabinene to (+)-cis-sabinol by an enzyme preparation from sage (Salvia officinalis) leaves

Karp, F.; Harris, J.; Croteau, R.; Arch. Biochem. Biophys. 256, 179-193 (1987)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
FAD
exogenous, activates the enzyme slightly
Salvia officinalis
FMN
exogenous, activates the enzyme
Salvia officinalis
octyl beta-D-glucoside
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
Salvia officinalis
sodium cholate
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Salvia officinalis
Zwittergent 3-08
12% activation at 0.24% detergent
Salvia officinalis
Inhibitors
Inhibitors
Commentary
Organism
Structure
CO
photoreversible inhibition
Salvia officinalis
NADP+
NADP+ competitively inhibits P-450-dependent reactions, 40-45% inhibition of hydroxylation at 2 mM
Salvia officinalis
octyl beta-D-glucoside
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
Salvia officinalis
sodium cholate
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Salvia officinalis
sodium deoxycholate
80% inhibition at 0.06% detergent
Salvia officinalis
sodium taurocholate
13% inhibition at 0.30% detergent
Salvia officinalis
sodium taurodeoxycholate
91% inhibition at 0.06% detergent
Salvia officinalis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
localization of sabinene hydroxylase in sage leaf homogenates by differential centrifugation indicated that activity is restricted to light membranes
Salvia officinalis
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no effect on enzyme activity by 1-10 mM of Mg2+, Mn2+, Ca2+, Cu2+, and Fe2+
Salvia officinalis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(+)-sabinene + NADPH + H+ + O2
Salvia officinalis
-
(+)-cis-sabinol + NADP+ + H2O
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Salvia officinalis
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
epidermis
-
Salvia officinalis
-
leaf
-
Salvia officinalis
-
seedling
etiolated
Salvia officinalis
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(+)-sabinene + NADPH + H+ + O2
-
717144
Salvia officinalis
(+)-cis-sabinol + NADP+ + H2O
-
-
-
?
(+)-sabinene + NADPH + H+ + O2
the hydroxylase is highly specific for (+)-sabinene as substrate. Addition of sabinene to solubilized microsomes provides a typical type I binding spectrum
717144
Salvia officinalis
(+)-cis-sabinol + NADP+ + H2O
GC product analysis
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Salvia officinalis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
-
Salvia officinalis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.8
8.6
50% of maximal activity at pH 6.8 and pH 8.6
Salvia officinalis
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Salvia officinalis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
FAD
exogenous, activates the enzyme slightly
Salvia officinalis
FMN
exogenous, activates the enzyme
Salvia officinalis
octyl beta-D-glucoside
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
Salvia officinalis
sodium cholate
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Salvia officinalis
Zwittergent 3-08
12% activation at 0.24% detergent
Salvia officinalis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Salvia officinalis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CO
photoreversible inhibition
Salvia officinalis
NADP+
NADP+ competitively inhibits P-450-dependent reactions, 40-45% inhibition of hydroxylation at 2 mM
Salvia officinalis
octyl beta-D-glucoside
35% activation at 0.12% detergent, complete inhibition at 0.48% detergent
Salvia officinalis
sodium cholate
40% activation at 0.30% detergent, 17% inhibition at 0.48% detergent
Salvia officinalis
sodium deoxycholate
80% inhibition at 0.06% detergent
Salvia officinalis
sodium taurocholate
13% inhibition at 0.30% detergent
Salvia officinalis
sodium taurodeoxycholate
91% inhibition at 0.06% detergent
Salvia officinalis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
localization of sabinene hydroxylase in sage leaf homogenates by differential centrifugation indicated that activity is restricted to light membranes
Salvia officinalis
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no effect on enzyme activity by 1-10 mM of Mg2+, Mn2+, Ca2+, Cu2+, and Fe2+
Salvia officinalis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(+)-sabinene + NADPH + H+ + O2
Salvia officinalis
-
(+)-cis-sabinol + NADP+ + H2O
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
epidermis
-
Salvia officinalis
-
leaf
-
Salvia officinalis
-
seedling
etiolated
Salvia officinalis
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(+)-sabinene + NADPH + H+ + O2
-
717144
Salvia officinalis
(+)-cis-sabinol + NADP+ + H2O
-
-
-
?
(+)-sabinene + NADPH + H+ + O2
the hydroxylase is highly specific for (+)-sabinene as substrate. Addition of sabinene to solubilized microsomes provides a typical type I binding spectrum
717144
Salvia officinalis
(+)-cis-sabinol + NADP+ + H2O
GC product analysis
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Salvia officinalis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
-
Salvia officinalis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.8
8.6
50% of maximal activity at pH 6.8 and pH 8.6
Salvia officinalis
General Information
General Information
Commentary
Organism
evolution
the enzyme is a cytochrome P-450-dependent mixed function oxygenase and belongs to the cytochrome P450 oxygenase family
Salvia officinalis
metabolism
the enzyme catalyzes the synthesis of (+)-cis-sabinol, which is a key step in the biosynthesis of C3-oxygenated thujane monoterpenes, overview
Salvia officinalis
additional information
(+)-sabinene is a major olefinic constituent of the volatile oil of immature Salvia oficinalis
Salvia officinalis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme is a cytochrome P-450-dependent mixed function oxygenase and belongs to the cytochrome P450 oxygenase family
Salvia officinalis
metabolism
the enzyme catalyzes the synthesis of (+)-cis-sabinol, which is a key step in the biosynthesis of C3-oxygenated thujane monoterpenes, overview
Salvia officinalis
additional information
(+)-sabinene is a major olefinic constituent of the volatile oil of immature Salvia oficinalis
Salvia officinalis
Other publictions for EC 1.14.13.153
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
717144
Karp
Metabolism of monoterpenes: De ...
Salvia officinalis
Arch. Biochem. Biophys.
256
179-193
1987
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