BRENDA - Enzyme Database show
show all sequences of 1.14.14.146

Geranylgeraniol-18-hydroxylase: the last enzyme in the plaunotol biosynthetic pathway in Croton sublyratus

Tansakul, P.; De-Eknamkul, W.; Phytochemistry 47, 1241-1246 (1998)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
Croton sublyratus
this enzyme is involved in the final step of the biosynthetic pathway of plaunotol, an antipeptic ulcer constituent accumulated in this plant
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Croton sublyratus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Croton sublyratus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
-
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
this enzyme is involved in the final step of the biosynthetic pathway of plaunotol, an antipeptic ulcer constituent accumulated in this plant
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
NADH shows about 70% of the activity with NADPH
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
activity in the heated cell-free extract increases steadily during the first 30 min of the treatment. Thereafter, the enzyme activity declines rapidly and is almost undetectable after 60 min
Croton sublyratus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
assay at
Croton sublyratus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
above and below the pH optimum (pH 5) activity declines rapidly and is undetectable after 60 min
Croton sublyratus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
Croton sublyratus
this enzyme is involved in the final step of the biosynthetic pathway of plaunotol, an antipeptic ulcer constituent accumulated in this plant
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Croton sublyratus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
-
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
this enzyme is involved in the final step of the biosynthetic pathway of plaunotol, an antipeptic ulcer constituent accumulated in this plant
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
geranylgeraniol + [reduced NADPH-hemoprotein reductase] + O2
NADH shows about 70% of the activity with NADPH
694596
Croton sublyratus
18-hydroxygeranylgeraniol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
activity in the heated cell-free extract increases steadily during the first 30 min of the treatment. Thereafter, the enzyme activity declines rapidly and is almost undetectable after 60 min
Croton sublyratus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
assay at
Croton sublyratus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
above and below the pH optimum (pH 5) activity declines rapidly and is undetectable after 60 min
Croton sublyratus
Other publictions for EC 1.14.14.146
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
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)
693849
Chanama
-
Improvement of thin-layer chro ...
Croton stellatopilosus, Croton stellatopilosus Ohba
J. Planar Chromatogr.
22
49-53
2009
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2
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2
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1
1
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2
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1
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1
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2
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1
1
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2
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1
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1
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706809
Battilana
The 1-deoxy-D: -xylulose 5-pho ...
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
Theor. Appl. Genet.
118
653-669
2009
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2
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2
2
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694596
Tansakul
-
Geranylgeraniol-18-hydroxylase ...
Croton sublyratus
Phytochemistry
47
1241-1246
1998
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1
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1
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