BRENDA - Enzyme Database show
show all sequences of 1.1.1.214

Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate

Wilken, D.R.; King, H.L.; Dyar, R.E.; J. Biol. Chem. 250, 2311-2314 (1975)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
?
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-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
form A and form B of the enzyme obtained separated by rupture, centrifugation and column chromatography on DEAE-cellulose and hydroxylapatite
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
keto-omega-methylpantoyl lactone + NADPH
the only compound other than ketopantoyl lactone which is a substrate, 73% relative activity to ketopantoyl lactone with form A enzyme, 56% relative activity to ketopantoyl lactone with form B enzyme
286105
Escherichia coli
methylpantoyl lactone + NADP+
-
286105
Escherichia coli
?
ketopantoyl lactone + NADPH
-
286105
Escherichia coli
pantoyl lactone + NADP+
-
286105
Escherichia coli
?
additional information
both forms of the enzyme are B-specific, the enzyme exhibits opposite stereospecificity from that observed with the Saccharomyces cerevisiae enzyme, which is A-specific, less than 5% relative activity to ketopantoyl lactone with the following 2-keto-gamma-lactones: 2-keto-4-hydroxy-3-methylbutyric acid-gamma-lactone, 2-keto-4-hydroxybutyric acid-gamma-lactone
286105
Escherichia coli
?
-
-
-
-
additional information
the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
286105
Escherichia coli
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no activity observed with NADH
Escherichia coli
NADPH
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no activity observed with NADH
Escherichia coli
NADPH
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
form A and form B of the enzyme obtained separated by rupture, centrifugation and column chromatography on DEAE-cellulose and hydroxylapatite
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
keto-omega-methylpantoyl lactone + NADPH
the only compound other than ketopantoyl lactone which is a substrate, 73% relative activity to ketopantoyl lactone with form A enzyme, 56% relative activity to ketopantoyl lactone with form B enzyme
286105
Escherichia coli
methylpantoyl lactone + NADP+
-
286105
Escherichia coli
?
ketopantoyl lactone + NADPH
-
286105
Escherichia coli
pantoyl lactone + NADP+
-
286105
Escherichia coli
?
additional information
both forms of the enzyme are B-specific, the enzyme exhibits opposite stereospecificity from that observed with the Saccharomyces cerevisiae enzyme, which is A-specific, less than 5% relative activity to ketopantoyl lactone with the following 2-keto-gamma-lactones: 2-keto-4-hydroxy-3-methylbutyric acid-gamma-lactone, 2-keto-4-hydroxybutyric acid-gamma-lactone
286105
Escherichia coli
?
-
-
-
-
additional information
the physiological substrate for the enzyme is uncertain, the physiological function of the enzyme is unknown
286105
Escherichia coli
?
-
-
-
-
Other publictions for EC 1.1.1.214
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)
654311
Kataoka
Gene cloning and overexpressio ...
Candida parapsilosis, Candida parapsilosis IFO 0708
Appl. Microbiol. Biotechnol.
64
359-366
2004
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1
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1
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2
2
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10
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2
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4
1
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2
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1
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347731
Julliard
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Purification and characterizat ...
Spinacia oleracea
Bot. Acta
107
191-200
1994
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2
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1
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1
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1
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5
1
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2
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1
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1
1
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1
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1
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5
1
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-
286105
Wilken
Ketopantoic acid and ketopanto ...
Escherichia coli
J. Biol. Chem.
250
2311-2314
1975
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4
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