BRENDA - Enzyme Database show
show all sequences of 4.1.3.16

2-keto-4-Hydroxyglutarate aldolase: purification of the homogeneous enzyme from bovine kidney

Dekker, E.E.; Kitson, R.P.; J. Biol. Chem. 267, 10507-10514 (1992)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
50 mM, enhances activity 2fold; activates kidney enzyme
Bos taurus
Inhibitors
Inhibitors
Commentary
Organism
Structure
dithiodipyridine
kidney enzyme
Bos taurus
Hg2+
100% inhibition at 1 microM; kidney enzyme, complete inhibition at 1 mM
Bos taurus
Mn2+
65% inhibition at 10 mM; kidney enzyme, 65% inhibition at 10 mM
Bos taurus
additional information
; not inhibitory: mercaptoethanol, EDTA, 1,10-phenanthroline, alpha,alpha'-dipyridyl, or 8-hydroxyquinoline up to 10 mM
Bos taurus
NaBH4
incubation of the enzyme with either pyruvate or glyoxylate in the presence of NaBH4 causes extensive loss of aldolase activity concomitant with stable binding of about 1.0-1.5 mol of substrate/mol of enzyme
Bos taurus
p-mercuribenzoate
kidney enzyme
Bos taurus
sulfhydryl-reacting reagents
-
Bos taurus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
L-4-hydroxy-2-oxoglutarate
pH 8.3, 37C
Bos taurus
0.031
-
D-4-hydroxy-2-oxoglutarate
pH 8.3, 37C
Bos taurus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no requirement
Bos taurus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35700
-
4 * 35700, SDS-PAGE
Bos taurus
36000
-
4 * 36000, SDS-PAGE, amino acid composition, kidney enzyme
Bos taurus
138000
-
sucrose density gradient centrifugation
Bos taurus
140000
-
gel filtration
Bos taurus
144000
-
gel filtration, sucrose density gradient centrifugation, kidney enzyme
Bos taurus
144500
-
sedimentation equilibrium centrifugation
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
; bovine
-
Purification (Commentary)
Commentary
Organism
; kidney enzyme
Bos taurus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Bos taurus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
9.23
-
kidney enzyme; pH 8.4, 37C
Bos taurus
Storage Stability
Storage Stability
Organism
4C, Tris-HCl buffer, pH 7.4, 40% saturated with ammonium sulfate, 6 months, kidney enzyme
Bos taurus
4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, 40% saturated with ammonium sulfate, 100% of initial activity for at least 6 months
Bos taurus
4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, no substantial loss of enzymatic activity for up to 1 month
Bos taurus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-4-hydroxy-2-oxoglutarate
-
5255
Bos taurus
pyruvate + glyoxylate
-
-
-
r
L-4-hydroxy-2-oxoglutarate
-
5255
Bos taurus
pyruvate + glyoxylate
-
-
-
r
additional information
enzyme shows no stereospecificity in catalyzing the aldol cleavage of the two optical isomers of 2-keto-4-hydroxyglutarate. Enzyme also catalyzes the beta-decarboxylation of oxalacetate, its decarboxylase/aldolae activity ratio is lower than that seen with the pure enzyme from either bovine liver or Escherichia coli
5255
Bos taurus
?
-
-
-
-
Oxaloacetate
-
5255
Bos taurus
CO2 + pyruvate
-
-
-
-
pyruvate + glyoxylate
-
5255
Bos taurus
D-4-hydroxy-2-oxoglutarate
-
-
-
r
Subunits
Subunits
Commentary
Organism
tetramer
4 * 35700, SDS-PAGE; 4 * 36000, SDS-PAGE, amino acid composition, kidney enzyme
Bos taurus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
; 2-keto-4-hydroxyglutarate cleavage
Bos taurus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.3
-
50% of maximum activity
Bos taurus
9.6
-
60% of maximum activity
Bos taurus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
50 mM, enhances activity 2fold; activates kidney enzyme
Bos taurus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
dithiodipyridine
kidney enzyme
Bos taurus
Hg2+
100% inhibition at 1 microM; kidney enzyme, complete inhibition at 1 mM
Bos taurus
Mn2+
65% inhibition at 10 mM; kidney enzyme, 65% inhibition at 10 mM
Bos taurus
additional information
; not inhibitory: mercaptoethanol, EDTA, 1,10-phenanthroline, alpha,alpha'-dipyridyl, or 8-hydroxyquinoline up to 10 mM
Bos taurus
NaBH4
incubation of the enzyme with either pyruvate or glyoxylate in the presence of NaBH4 causes extensive loss of aldolase activity concomitant with stable binding of about 1.0-1.5 mol of substrate/mol of enzyme
Bos taurus
p-mercuribenzoate
kidney enzyme
Bos taurus
sulfhydryl-reacting reagents
-
Bos taurus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
L-4-hydroxy-2-oxoglutarate
pH 8.3, 37C
Bos taurus
0.031
-
D-4-hydroxy-2-oxoglutarate
pH 8.3, 37C
Bos taurus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no requirement
Bos taurus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35700
-
4 * 35700, SDS-PAGE
Bos taurus
36000
-
4 * 36000, SDS-PAGE, amino acid composition, kidney enzyme
Bos taurus
138000
-
sucrose density gradient centrifugation
Bos taurus
140000
-
gel filtration
Bos taurus
144000
-
gel filtration, sucrose density gradient centrifugation, kidney enzyme
Bos taurus
144500
-
sedimentation equilibrium centrifugation
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
; kidney enzyme
Bos taurus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Bos taurus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
9.23
-
kidney enzyme; pH 8.4, 37C
Bos taurus
Storage Stability (protein specific)
Storage Stability
Organism
4C, Tris-HCl buffer, pH 7.4, 40% saturated with ammonium sulfate, 6 months, kidney enzyme
Bos taurus
4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, 40% saturated with ammonium sulfate, 100% of initial activity for at least 6 months
Bos taurus
4C, in either 50 mM Tris-HCl or potassium phosphate, pH 7.4, plus 5 mM 2-mercaptoethanol, 0.02% sodium azide, no substantial loss of enzymatic activity for up to 1 month
Bos taurus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-4-hydroxy-2-oxoglutarate
-
5255
Bos taurus
pyruvate + glyoxylate
-
-
-
r
L-4-hydroxy-2-oxoglutarate
-
5255
Bos taurus
pyruvate + glyoxylate
-
-
-
r
additional information
enzyme shows no stereospecificity in catalyzing the aldol cleavage of the two optical isomers of 2-keto-4-hydroxyglutarate. Enzyme also catalyzes the beta-decarboxylation of oxalacetate, its decarboxylase/aldolae activity ratio is lower than that seen with the pure enzyme from either bovine liver or Escherichia coli
5255
Bos taurus
?
-
-
-
-
Oxaloacetate
-
5255
Bos taurus
CO2 + pyruvate
-
-
-
-
pyruvate + glyoxylate
-
5255
Bos taurus
D-4-hydroxy-2-oxoglutarate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 35700, SDS-PAGE; 4 * 36000, SDS-PAGE, amino acid composition, kidney enzyme
Bos taurus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
; 2-keto-4-hydroxyglutarate cleavage
Bos taurus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.3
-
50% of maximum activity
Bos taurus
9.6
-
60% of maximum activity
Bos taurus
Other publictions for EC 4.1.3.16
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)
746867
Schapfl
Extended substrate range of t ...
Escherichia coli
Appl. Microbiol. Biotechnol.
102
8359-8372
2018
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1
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1
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748294
Mdimegh
HOGA1 gene mutations of prima ...
Homo sapiens
J. Clin. Lab. Anal.
31
e22053
2017
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-
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2
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1
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2
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1
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2
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1
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1
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1
1
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-
747772
MacDonald
Cellular degradation of 4-hyd ...
Homo sapiens
FEBS Lett.
590
1467-1476
2016
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1
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1
1
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1
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1
1
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1
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1
1
-
-
-
746641
Huang
Use of a novel microtitration ...
Bos taurus
Acta Crystallogr. Sect. F
70
1546-1549
2014
-
-
-
1
-
-
-
-
-
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1
1
-
4
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1
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1
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1
1
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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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1
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
721727
Riedel
4-Hydroxy-2-oxoglutarate aldol ...
Homo sapiens
Biochim. Biophys. Acta
1822
1544-1552
2012
-
1
1
-
9
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
1
-
1
1
-
-
-
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1
1
-
-
9
-
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2
-
-
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-
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-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
728378
Williams
The enzyme 4-hydroxy-2-oxoglut ...
Homo sapiens
Nephrol. Dial. Transplant.
27
3191-3195
2012
-
-
1
-
1
-
-
-
-
-
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1
-
2
-
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-
1
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1
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1
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1
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1
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1
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1
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-
1
1
-
-
-
723542
Riedel
Structural and biochemical stu ...
Homo sapiens
PLoS ONE
6
e26021
2011
-
-
1
1
11
-
-
10
-
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2
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2
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2
2
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-
10
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1
-
1
11
-
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-
-
10
-
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2
-
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-
-
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-
-
2
2
-
-
-
10
-
-
-
-
-
-
-
-
10
10
713711
Belostotsky
Mutations in DHDPSL are respon ...
Homo sapiens
Am. J. Hum. Genet.
87
392-399
2010
-
-
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1
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2
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1
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-
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-
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1
1
-
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-
5255
Dekker
2-keto-4-Hydroxyglutarate aldo ...
Bos taurus
J. Biol. Chem.
267
10507-10514
1992
1
-
-
-
-
-
7
2
-
1
6
-
-
4
-
-
1
-
-
5
1
3
5
1
-
-
-
-
1
2
-
-
-
-
-
1
-
-
-
-
-
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7
-
2
-
1
6
-
-
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-
1
-
5
1
3
5
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
5253
Anderson
Rat liver 4-hydroxy-2-ketoglut ...
Rattus norvegicus
Arch. Biochem. Biophys.
236
82-97
1985
-
-
-
-
-
-
10
1
2
1
1
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-
2
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1
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-
2
2
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-
1
-
-
-
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3
-
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-
-
-
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10
3
1
2
1
1
-
-
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1
-
2
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
5252
Scholtz
-
Substrates of hydroxyketogluta ...
Rattus norvegicus
Bioorg. Chem.
12
229-234
1984
-
1
-
-
-
-
-
9
-
1
-
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1
-
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1
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1
2
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3
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1
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9
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1
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1
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1
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5250
Grady
Steady-state kinetics and inhi ...
Bos taurus
Biochemistry
20
2497-2502
1981
2
-
-
-
-
-
13
1
-
1
-
-
-
3
-
-
-
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2
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-
1
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2
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-
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13
-
1
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1
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-
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2
-
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1
-
-
-
-
-
-
-
-
-
-
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-
5247
Lane
Sulfhydryl groups in relation ...
Bos taurus
Biochim. Biophys. Acta
481
212-221
1977
-
-
-
-
-
-
2
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1
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2
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2
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1
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2
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1
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2
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1
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-
-
-
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-
-
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-
-
-
5246
Hansen
Inactivation of bovine liver 2 ...
Bos taurus
Biochemistry
15
2912-2917
1976
-
-
-
-
-
1
1
-
-
1
-
-
-
3
-
-
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-
1
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-
-
-
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-
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1
-
1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5243
Dekker
2-keto-4-Hydroxyglutarate aldo ...
Bos taurus
Methods Enzymol.
42C
280-285
1975
-
-
-
-
-
-
1
3
-
1
1
-
-
2
-
-
1
-
-
2
1
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
1
1
-
-
-
-
1
-
2
1
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2159
Adams
-
Enzymes and intermediates of h ...
Rattus norvegicus
Methods Enzymol.
17B
266-306
1971
-
-
-
-
-
-
2
2
-
1
1
1
-
1
-
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1
-
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1
1
-
4
-
1
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-
-
-
-
-
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-
-
-
-
-
-
-
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2
-
2
-
1
1
1
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1
-
1
1
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
5238
Lane
2-keto-4-Hydroxybutyrate aldol ...
Bos taurus, Mammalia
Biochemistry
10
1353-1364
1971
-
-
-
-
-
-
4
2
-
2
-
2
-
2
-
-
1
-
-
1
2
-
6
-
1
-
1
-
2
2
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4
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2
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2
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2
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1
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1
2
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6
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1
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1
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2
2
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5241
Kobes
Variant properties of bovine l ...
Bos taurus
Biochim. Biophys. Acta
251
238-250
1971
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1
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1
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2
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2
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7
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1
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1
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1
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2
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7
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1
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5237
Kuratomi
The metabolism of gamma-hydrox ...
Rattus norvegicus
Biochim. Biophys. Acta
78
617-628
1963
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7
3
1
1
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1
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1
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3
1
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4
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1
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1
1
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7
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3
1
1
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1
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3
1
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4
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1
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1
1
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