BRENDA - Enzyme Database show
show all sequences of 1.14.14.125

Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA

Barriuso, J.; Nguyen, D.T.; Li, J.W.; Roberts, J.N.; MacNevin, G.; Chaytor, J.L.; Marcus, S.L.; Vederas, J.C.; Ro, D.K.; J. Am. Chem. Soc. 133, 8078-8081 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
the lovA gene in C-terminal FLAG-tagged form is cloned in the same vector coding cpr (cytochrome P450 oxidoreductase), and both lovA and cpr are co-expressed in Saccharomyces cerevisiae
Aspergillus terreus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0062
-
monacolin L acid
pH and temperature not specified in the publication
Aspergillus terreus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus terreus
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus terreus
Q9Y7C8
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-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
727670
Aspergillus terreus
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
-
?
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase
727670
Aspergillus terreus
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a heme-thiolate protein
Aspergillus terreus
Cloned(Commentary) (protein specific)
Commentary
Organism
the lovA gene in C-terminal FLAG-tagged form is cloned in the same vector coding cpr (cytochrome P450 oxidoreductase), and both lovA and cpr are co-expressed in Saccharomyces cerevisiae
Aspergillus terreus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a heme-thiolate protein
Aspergillus terreus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0062
-
monacolin L acid
pH and temperature not specified in the publication
Aspergillus terreus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
Aspergillus terreus
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase. The enzyme is involved in the biosynthesis of lovastatin
727670
Aspergillus terreus
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
-
?
monacolin L acid + [reduced NADPH-hemoprotein reductase] + O2
monacolin L acid i.e. (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid. The enzyme also catalyses the reaction of EC 1.14.13.197, dihydromonacolin L hydroxylase
727670
Aspergillus terreus
monacolin J acid + [oxidized NADPH-hemoprotein reductase] + H2O
monacolin J acid i.e. (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
-
-
?
Other publictions for EC 1.14.14.125
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)
727670
Barriuso
Double oxidation of the cyclic ...
Aspergillus terreus
J. Am. Chem. Soc.
133
8078-8081
2011
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