BRENDA - Enzyme Database
show all sequences of 5.1.99.1

Isolation and characterization of DL-methylmalonyl-coenzyme A racemase from rat liver

Stabler, S.P.; Marcell, P.D.; Allen, R.H.; Arch. Biochem. Biophys. 241, 252-264 (1985)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
a simple direct assay for DL-methylmalonyl-coenzyme A racemase which is based on the fact that the proton on C-2 of methylmalonyl-CoA is replaced by a proton in the medium during racemization
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Rattus norvegicus
butyryl-CoA
-
Rattus norvegicus
Cd2+
-
Rattus norvegicus
CoA
-
Rattus norvegicus
Cu2+
-
Rattus norvegicus
EDTA
reactivation by Co2+
Rattus norvegicus
glutaryl-CoA
-
Rattus norvegicus
heptanoyl-CoA
-
Rattus norvegicus
malonyl-CoA
-
Rattus norvegicus
octanoyl-CoA
-
Rattus norvegicus
propionyl-CoA
-
Rattus norvegicus
succinyl-CoA
-
Rattus norvegicus
Zn2+
-
Rattus norvegicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
DL-methylmalonyl-CoA
-
Rattus norvegicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
most potent activator, Km: 0.0002 mM, binds 2 mol Co2+ per mol of racemase
Rattus norvegicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
16000
-
2 * 16000, subunits not connected by disulfide bonds, SDS-PAGE in presence and absence of 2-mercaptoethanol
Rattus norvegicus
32000
-
gel filtration
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Rattus norvegicus
enzyme is involved in the flow of DL-methylmalonyl-CoA to L-methylmalonyl-CoA
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Rattus norvegicus
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
8400
-
-
Rattus norvegicus
Storage Stability
Storage Stability
Organism
-20C, stable for at least 3 months
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(R)-2-Methyl-3-oxopropanoyl-CoA
-
2434
Rattus norvegicus
(S)-2-Methyl-3-oxopropanoyl-CoA
-
2434
Rattus norvegicus
-
additional information
enzyme is involved in the flow of DL-methylmalonyl-CoA to L-methylmalonyl-CoA
2434
Rattus norvegicus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 16000, subunits not connected by disulfide bonds, SDS-PAGE in presence and absence of 2-mercaptoethanol
Rattus norvegicus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4170
-
DL-methylmalonyl-CoA
-
Rattus norvegicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Rattus norvegicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
8.5
50% of maximal activity at pH 5.5 and 8.5
Rattus norvegicus
Application (protein specific)
Application
Commentary
Organism
analysis
a simple direct assay for DL-methylmalonyl-coenzyme A racemase which is based on the fact that the proton on C-2 of methylmalonyl-CoA is replaced by a proton in the medium during racemization
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Rattus norvegicus
butyryl-CoA
-
Rattus norvegicus
Cd2+
-
Rattus norvegicus
CoA
-
Rattus norvegicus
Cu2+
-
Rattus norvegicus
EDTA
reactivation by Co2+
Rattus norvegicus
glutaryl-CoA
-
Rattus norvegicus
heptanoyl-CoA
-
Rattus norvegicus
malonyl-CoA
-
Rattus norvegicus
octanoyl-CoA
-
Rattus norvegicus
propionyl-CoA
-
Rattus norvegicus
succinyl-CoA
-
Rattus norvegicus
Zn2+
-
Rattus norvegicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
DL-methylmalonyl-CoA
-
Rattus norvegicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
most potent activator, Km: 0.0002 mM, binds 2 mol Co2+ per mol of racemase
Rattus norvegicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
16000
-
2 * 16000, subunits not connected by disulfide bonds, SDS-PAGE in presence and absence of 2-mercaptoethanol
Rattus norvegicus
32000
-
gel filtration
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Rattus norvegicus
enzyme is involved in the flow of DL-methylmalonyl-CoA to L-methylmalonyl-CoA
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
8400
-
-
Rattus norvegicus
Storage Stability (protein specific)
Storage Stability
Organism
-20C, stable for at least 3 months
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(R)-2-Methyl-3-oxopropanoyl-CoA
-
2434
Rattus norvegicus
(S)-2-Methyl-3-oxopropanoyl-CoA
-
2434
Rattus norvegicus
-
additional information
enzyme is involved in the flow of DL-methylmalonyl-CoA to L-methylmalonyl-CoA
2434
Rattus norvegicus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 16000, subunits not connected by disulfide bonds, SDS-PAGE in presence and absence of 2-mercaptoethanol
Rattus norvegicus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4170
-
DL-methylmalonyl-CoA
-
Rattus norvegicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Rattus norvegicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
8.5
50% of maximal activity at pH 5.5 and 8.5
Rattus norvegicus
Other publictions for EC 5.1.99.1
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
Synonyms
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)
748590
Gonzalez-Garcia
Awakening sleeping beauty Pro ...
Acidipropionibacterium acidipropionici, Acidipropionibacterium acidipropionici DSM 20272
Microb. Cell Fact.
16
121
2017
-
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4
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1
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1
1
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-
747542
Hamed
Use of methylmalonyl-CoA epim ...
Homo sapiens
ChemBioChem
17
471-473
2016
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1
1
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1
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1
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2
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726729
Han
Epimerase (Msed_0639) and muta ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
Appl. Environ. Microbiol.
78
6194-6202
2012
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1
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3
2
4
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2
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1
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4
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2
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1
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1
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3
2
4
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1
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1
1
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4
2
2
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1
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1
1
1
1
-
-
714552
Boghigian
Multi-factorial engineering of ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Biotechnol. Bioeng.
108
1360-1371
2011
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1
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727331
Yang
-
Construction of an engineered ...
Streptomyces coelicolor
Chin. J. Antibiot.
36
191-196
2011
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1
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1
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706660
Shi
Crystal structure of a putativ ...
Caldanaerobacter subterraneus subsp. tengcongensis
Proteins
77
994-999
2009
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1
1
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1
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1
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2
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1
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1
1
3
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1
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1
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1
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1
1
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1
1
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693174
Erb
Ethylmalonyl-CoA mutase from R ...
Rhodobacter sphaeroides
J. Biol. Chem.
283
32283-32293
2008
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1
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1
2
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3
-
1
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1
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1
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3
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1
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1
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2
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1
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1
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3
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673023
Gross
Metabolic engineering of Pseud ...
Sorangium cellulosum
Chem. Biol.
13
1253-1264
2006
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1
1
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673947
Bikker
A homozygous nonsense mutation ...
Homo sapiens
Hum. Mutat.
27
640-643
2006
-
1
-
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2
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1
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676026
Dobson
Homozygous nonsense mutation i ...
Homo sapiens
Mol. Genet. Metab.
88
327-333
2006
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1
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1
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1
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1
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-
-
676032
Chandler
Propionyl-CoA and adenosylcoba ...
Caenorhabditis elegans
Mol. Genet. Metab.
89
64-73
2006
-
1
1
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-
-
-
1
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3
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1
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661687
Khnl
Functional analysis of the met ...
Caenorhabditis elegans
FEBS J.
272
1465-1477
2005
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1
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1
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649408
Bobik
Purification and partial chara ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
63
682-685
2004
-
-
1
-
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1
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1
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4
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1
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1
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1
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1
1
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1
1
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649165
McCarthy
Expression, crystallization an ...
Propionibacterium freudenreichii subsp. shermanii
Acta Crystallogr. Sect. D
57
706-708
2001
-
-
1
1
-
-
-
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3
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653930
McCarthy
Crystal structure of methylmal ...
Propionibacterium freudenreichii subsp. shermanii
Structure
9
637-646
2001
-
-
-
1
-
-
-
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-
1
-
1
-
5
-
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2
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1
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2442
Stabler
DL-Methylmalonyl-CoA racemase ...
Rattus norvegicus
Methods Enzymol.
166
400-406
1988
-
-
-
-
-
-
4
1
-
4
2
-
-
2
-
-
1
-
-
2
1
-
1
1
-
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-
-
1
1
1
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4
-
1
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4
2
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1
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2
1
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1
1
-
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-
1
1
1
-
-
-
-
-
-
-
-
2434
Stabler
Isolation and characterization ...
Rattus norvegicus
Arch. Biochem. Biophys.
241
252-264
1985
-
1
-
-
-
-
13
1
-
1
2
1
-
3
-
-
1
-
-
2
1
1
2
1
-
-
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-
1
1
1
-
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-
-
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1
-
-
-
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-
-
13
-
1
-
1
2
1
-
-
-
1
-
2
1
1
2
1
-
-
-
1
1
1
-
-
-
-
-
-
-
-
2435
Fuller
Proton transfer in methylmalon ...
Homo sapiens, Propionibacterium freudenreichii subsp. shermanii
Biochem. J.
213
643-650
1983
-
-
-
-
-
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-
3
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1
-
1
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-
2
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-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
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-
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2436
Leadlay
Proton transfer in methylmalon ...
Propionibacterium freudenreichii subsp. shermanii
Biochem. J.
213
635-642
1983
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2
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1
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1
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1
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-
-
-
-
-
-
-
-
-
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2437
Leadlay
Purification and characterizat ...
Propionibacterium freudenreichii subsp. shermanii
Biochem. J.
197
413-419
1981
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5
2
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-
2
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-
1
-
-
-
1
1
1
1
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-
-
-
-
-
-
-
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-
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5
2
-
-
-
-
1
-
-
1
1
1
1
-
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2438
Allen
-
Methylmalonyl-CoA racemase fro ...
Propionibacterium freudenreichii subsp. shermanii
Methods Enzymol.
13
194-198
1969
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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
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1
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2439
Mazumder
-
Methylmalonyl-CoA racemase fro ...
Ovis aries
Methods Enzymol.
13
190-194
1969
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1
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1
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1
1
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1
1
1
1
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1
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1
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1
1
1
1
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2440
Overath
-
Zum Mechanismus der Umlagerung ...
Propionibacterium freudenreichii subsp. shermanii
Biochem. Z.
335
500-518
1962
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1
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1
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1
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1
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2441
Mazumder
Metabolism of propionic acid i ...
Ovis aries
J. Biol. Chem.
237
3065-3068
1962
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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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1
1
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1
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