BRENDA - Enzyme Database
show all sequences of 5.1.99.1

Crystal structure of a putative methylmalonyl-coenzyme a epimerase from Thermoanaerobacter tengcongensis at 2.0 Å resolution

Shi, L.; Gao, P.; Yan, X.; Liang, D.; Proteins 77, 994-999 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant protein is expressed in BL21(DE3) Escherichia coli cells
Caldanaerobacter subterraneus subsp. tengcongensis
Crystallization (Commentary)
Crystallization
Organism
at 2.0 A resolutionm, crystals of recombinant enzyme are grown at 20°C using the hanging-drop, vapor-diffusion method, drops consisted of 2 microl of protein solution and 2 microl of mother liquor (0.1 M citric acid, pH 2.6, 1.6 M (NH4)2SO4), crystals are obtained after 7-8 days growth, native and derivative crystals are soaked in 2 M Li2SO4
Caldanaerobacter subterraneus subsp. tengcongensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
enzyme is metal-dependent enzyme, in the active site, metal binding site binds the coenzyme Co2+
Caldanaerobacter subterraneus subsp. tengcongensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-methylmalonyl-CoA
Caldanaerobacter subterraneus subsp. tengcongensis
-
(S)-methylmalonyl-CoA
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Caldanaerobacter subterraneus subsp. tengcongensis
Q8RCQ6
-
-
Purification (Commentary)
Commentary
Organism
lysate is clarified by centrifugation and purified by passage through a nickel-affinity column, and a further purification step is performed by gel filtration
Caldanaerobacter subterraneus subsp. tengcongensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-methylmalonyl-CoA
-
706660
Caldanaerobacter subterraneus subsp. tengcongensis
(S)-methylmalonyl-CoA
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
in solution
Caldanaerobacter subterraneus subsp. tengcongensis
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant protein is expressed in BL21(DE3) Escherichia coli cells
Caldanaerobacter subterraneus subsp. tengcongensis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
at 2.0 A resolutionm, crystals of recombinant enzyme are grown at 20°C using the hanging-drop, vapor-diffusion method, drops consisted of 2 microl of protein solution and 2 microl of mother liquor (0.1 M citric acid, pH 2.6, 1.6 M (NH4)2SO4), crystals are obtained after 7-8 days growth, native and derivative crystals are soaked in 2 M Li2SO4
Caldanaerobacter subterraneus subsp. tengcongensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
enzyme is metal-dependent enzyme, in the active site, metal binding site binds the coenzyme Co2+
Caldanaerobacter subterraneus subsp. tengcongensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-methylmalonyl-CoA
Caldanaerobacter subterraneus subsp. tengcongensis
-
(S)-methylmalonyl-CoA
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
lysate is clarified by centrifugation and purified by passage through a nickel-affinity column, and a further purification step is performed by gel filtration
Caldanaerobacter subterraneus subsp. tengcongensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-methylmalonyl-CoA
-
706660
Caldanaerobacter subterraneus subsp. tengcongensis
(S)-methylmalonyl-CoA
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
in solution
Caldanaerobacter subterraneus subsp. tengcongensis
General Information
General Information
Commentary
Organism
physiological function
second step in the pathway responsible for the degradation of branched amino acids and odd chain fatty acids, MMCE participated in autotrophic CO2 fixation via the 3-hydroxypropionate pathway, in propionate fermentation, the regeneration of glyoxylate and in the biosynthesis of polyketide antibiotics
Caldanaerobacter subterraneus subsp. tengcongensis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
second step in the pathway responsible for the degradation of branched amino acids and odd chain fatty acids, MMCE participated in autotrophic CO2 fixation via the 3-hydroxypropionate pathway, in propionate fermentation, the regeneration of glyoxylate and in the biosynthesis of polyketide antibiotics
Caldanaerobacter subterraneus subsp. tengcongensis
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
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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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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726729
Han
Epimerase (Msed_0639) and muta ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
Appl. Environ. Microbiol.
78
6194-6202
2012
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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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1
1
1
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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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46
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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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706660
Shi
Crystal structure of a putativ ...
Caldanaerobacter subterraneus subsp. tengcongensis
Proteins
77
994-999
2009
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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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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
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1
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676026
Dobson
Homozygous nonsense mutation i ...
Homo sapiens
Mol. Genet. Metab.
88
327-333
2006
-
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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661687
Kühnl
Functional analysis of the met ...
Caenorhabditis elegans
FEBS J.
272
1465-1477
2005
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649408
Bobik
Purification and partial chara ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
63
682-685
2004
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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
1
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649165
McCarthy
Expression, crystallization an ...
Propionibacterium freudenreichii subsp. shermanii
Acta Crystallogr. Sect. D
57
706-708
2001
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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
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5
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2442
Stabler
DL-Methylmalonyl-CoA racemase ...
Rattus norvegicus
Methods Enzymol.
166
400-406
1988
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4
1
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4
2
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2
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2434
Stabler
Isolation and characterization ...
Rattus norvegicus
Arch. Biochem. Biophys.
241
252-264
1985
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1
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13
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13
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2435
Fuller
Proton transfer in methylmalon ...
Homo sapiens, Propionibacterium freudenreichii subsp. shermanii
Biochem. J.
213
643-650
1983
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2436
Leadlay
Proton transfer in methylmalon ...
Propionibacterium freudenreichii subsp. shermanii
Biochem. J.
213
635-642
1983
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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
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1
1
1
1
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5
2
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1
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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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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
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1
1
1
1
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1
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2440
Overath
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Zum Mechanismus der Umlagerung ...
Propionibacterium freudenreichii subsp. shermanii
Biochem. Z.
335
500-518
1962
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2441
Mazumder
Metabolism of propionic acid i ...
Ovis aries
J. Biol. Chem.
237
3065-3068
1962
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