BRENDA - Enzyme Database show
show all sequences of 1.1.1.168

Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase

King, H.L.; Dyar, R.E.; Wilken, D.R.; J. Biol. Chem. 249, 4689-4695 (1974)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
isatin
ketopantoyl lactone, enzyme form A
Saccharomyces cerevisiae
0.031
-
ketopantoyl lactone
enzyme form B
Saccharomyces cerevisiae
0.039
-
NADPH
enzyme form B
Saccharomyces cerevisiae
0.062
-
NADPH
enzyme form A
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
enzyme form A and B, gel filtration
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-dehydropantoyl lactone + NADPH
Saccharomyces cerevisiae
-
(R)-pantoyl lactone + NADP+
-
Saccharomyces cerevisiae
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
2 enzyme forms: A and B with similar properties
-
Purification (Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-dehydropantoyl lactone + NADPH
-
347727
Saccharomyces cerevisiae
(R)-pantoyl lactone + NADP+
-
347727
Saccharomyces cerevisiae
?
isatin + NADPH
-
347727
Saccharomyces cerevisiae
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.1
5.6
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
isatin
ketopantoyl lactone, enzyme form A
Saccharomyces cerevisiae
0.031
-
ketopantoyl lactone
enzyme form B
Saccharomyces cerevisiae
0.039
-
NADPH
enzyme form B
Saccharomyces cerevisiae
0.062
-
NADPH
enzyme form A
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
enzyme form A and B, gel filtration
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-dehydropantoyl lactone + NADPH
Saccharomyces cerevisiae
-
(R)-pantoyl lactone + NADP+
-
Saccharomyces cerevisiae
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-dehydropantoyl lactone + NADPH
-
347727
Saccharomyces cerevisiae
(R)-pantoyl lactone + NADP+
-
347727
Saccharomyces cerevisiae
?
isatin + NADPH
-
347727
Saccharomyces cerevisiae
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.1
5.6
-
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.168
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)
347731
Julliard
-
Purification and characterizat ...
Spinacia oleracea
Bot. Acta
107
191-200
1994
-
-
-
-
-
-
3
4
-
-
1
-
-
1
-
-
1
-
-
-
-
1
6
1
-
-
1
-
1
-
-
1
1
-
-
-
-
-
1
-
-
-
-
3
1
4
-
-
1
-
-
-
-
1
-
-
-
1
6
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
347730
Kataoka
Enzymes involved in the NADPH ...
Candida parapsilosis, Mucor ambiguus, Mucor ambiguus AKU 3006, Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
56
820-821
1992
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
7
-
2
-
-
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-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
347723
Hata
Ketopantoyl-lactone reductase ...
Saccharomyces cerevisiae
FEMS Microbiol. Lett.
58
87-90
1989
-
-
-
-
-
-
3
16
-
-
-
1
-
2
-
-
-
-
-
-
-
-
21
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
16
-
-
-
1
-
-
-
-
-
-
-
-
21
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347724
Hata
Ketopantoyl-lactone reductase ...
Candida parapsilosis
Biochim. Biophys. Acta
990
175-181
1989
-
-
-
1
-
-
11
4
-
-
2
2
-
5
-
-
1
-
-
-
2
-
12
1
1
-
2
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
11
-
4
-
-
2
2
-
-
-
1
-
-
2
-
12
1
1
-
2
-
-
-
2
-
-
-
-
-
-
-
347726
Wilken
Ketopantoyl lactone reductases ...
Saccharomyces cerevisiae
Methods Enzymol.
62
209-215
1979
-
-
-
-
-
1
5
-
-
-
1
1
-
1
-
-
1
-
-
-
1
1
4
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
1
1
-
-
-
1
-
-
1
1
4
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
347725
Wilken
Stereospecificity of pantoyl l ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
189
251-255
1978
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
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-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286105
Wilken
Ketopantoic acid and ketopanto ...
Saccharomyces cerevisiae
J. Biol. Chem.
250
2311-2314
1975
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
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-
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-
1
-
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-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347727
King
Ketopantoyl lactone and ketopa ...
Saccharomyces cerevisiae
J. Biol. Chem.
249
4689-4695
1974
-
-
-
-
-
-
-
4
-
-
1
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
1
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286104
King
-
Separation and preliminary stu ...
Saccharomyces cerevisiae
J. Biol. Chem.
247
4096-4098
1972
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
1
-
-
-
-
-
-
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-
-
-
-
-
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-
-
-
-
-
-
2
-
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-
4
-
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-
1
1
-
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-