BRENDA - Enzyme Database show
show all sequences of 1.14.14.159

Discovery, biosynthesis and stress-related accumulation of dolabradiene-derived defenses in maize

Mafu, S.; Ding, Y.; Murphy, K.M.; Yaacoobi, O.; Addison, J.B.; Wang, Q.; Shen, Z.; Briggs, S.P.; Bohlmann, J.; Castro-Falcon, G.; Hughes, C.C.; Betsiashvili, M.; Huffaker, A.; Schmelz, E.A.; Zerbe, P.; Plant Physiol. 176, 2677-2690 (2018)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Zea mays
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
Zea mays
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
Zea mays
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
root
-
Zea mays
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a cytochrome P-450 (heme thiolate) enzyme
Zea mays
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Zea mays
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a cytochrome P-450 (heme thiolate) enzyme
Zea mays
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
Zea mays
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
Zea mays
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
root
-
Zea mays
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
15,16-epoxydolabrene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
3beta-hydroxy-15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme is involved in biosynthesis of dolabralexin. It catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
dolabradiene + O2 + [reduced NADPH-hemoprotein reductase]
the enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3
748992
Zea mays
15,16-epoxydolabrene + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
Expression
Organism
Commentary
Expression
Zea mays
no increase of transcript level after inoculation with live spores of Fusarium verticillioides and Fusarium graminearum
additional information
Zea mays
increased transcript levels under abiotic stress condition (root treatments with 1 mM CuSO4)
up
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in biosynthesis of dolabralexin
Zea mays
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in biosynthesis of dolabralexin
Zea mays
Expression (protein specific)
Organism
Commentary
Expression
Zea mays
no increase of transcript level after inoculation with live spores of Fusarium verticillioides and Fusarium graminearum
additional information
Zea mays
increased transcript levels under abiotic stress condition (root treatments with 1 mM CuSO4)
up
Other publictions for EC 1.14.14.159
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)
748992
Mafu
Discovery, biosynthesis and s ...
Zea mays
Plant Physiol.
176
2677-2690
2018
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