Information on EC 5.1.99.1 - Methylmalonyl-CoA epimerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
5.1.99.1
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RECOMMENDED NAME
GeneOntology No.
Methylmalonyl-CoA epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
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3-hydroxypropanoate/4-hydroxybutanate cycle
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anaerobic energy metabolism (invertebrates, mitochondrial)
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Carbon fixation pathways in prokaryotes
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CO2 fixation in Crenarchaeota
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ethylmalonyl-CoA pathway
Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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methylaspartate cycle
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Microbial metabolism in diverse environments
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Propanoate metabolism
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propanoyl CoA degradation I
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propionate fermentation
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pyruvate fermentation to propanoate I
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Valine, leucine and isoleucine degradation
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SYSTEMATIC NAME
IUBMB Comments
methylmalonyl-CoA 2-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-03-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
promiscuous ethylmalonyl-CoA/methylmalonyl-CoA epimerase
Uniprot
Manually annotated by BRENDA team
Polyangium cellulosum, myxobacterium
SWISSPROT
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-methylmalonyl-CoA
(2S)-methylmalonyl-CoA
show the reaction diagram
(2S)-ethylmalonyl-CoA
(2R)-ethylmalonyl-CoA
show the reaction diagram
-
-
-
?
(R)-2-Methyl-3-oxopropanoyl-CoA
(S)-2-Methyl-3-oxopropanoyl-CoA
show the reaction diagram
(R)-methylmalonyl-CoA
(S)-methylmalonyl-CoA
show the reaction diagram
(S)-methylmalonyl-CoA
(R)-methylmalonyl-CoA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-methylmalonyl-CoA
(S)-methylmalonyl-CoA
show the reaction diagram
(S)-methylmalonyl-CoA
(R)-methylmalonyl-CoA
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co3+
-
lower level of activation than Co2+ at higher concentrations
Fe2+
-
lower level of activation than Co2+ at higher concentrations
Mg2+
activates; the enzyme is activated by divalent cations (Ni2+, Co2+, and Mg2+)
Zn2+
-
increases activity to a smaller extent than Co2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
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Butyryl-CoA
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glutaryl-CoA
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heptanoyl-CoA
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malonyl-CoA
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Octanoyl-CoA
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propionyl-CoA
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succinyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
(2S)-ethylmalonyl-CoA
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0.08
(S)-methylmalonyl-CoA
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0.1
DL-methylmalonyl-CoA
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0.079
methylmalonyl-CoA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4170
DL-methylmalonyl-CoA
Rattus norvegicus
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240
methylmalonyl-CoA
Pyrococcus horikoshii
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.35
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218
75C, pH not specified in the publication; purified recombinant enzyme, pH 7.0, 75C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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50% of maximal activity at pH 5.5 and 8.5
5.5 - 8.5
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50% of maximal activity at pH 5.5 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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low speed sedimentation without reaching equilibrium
32000
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gel filtration
32100
gel filtration; recombinant His-tagged enzyme, gel filtration
33000 - 35000
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gel filtration, sedimentation equilibrium studies
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 2.0 A resolutionm, crystals of recombinant enzyme are grown at 20C 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
crystallization of native, Co2+-substituted and SeMet-substituted enzyme by hanging-drop vapour-diffusion method
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity after repeated freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, fairly stable
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-20C, pH 8.5, indefinitely stable
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-20C, stable for at least 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant N-terminally His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography
lysate is clarified by centrifugation and purified by passage through a nickel-affinity column, and a further purification step is performed by gel filtration
recombinant MCE-1
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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expression in Escherichia coli as native enzyme and as selenomethionine derivative
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expression in Escherichia coli; gene Msed_0639, DNA and amino acid sequence determination, phylogenetic tree, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
expression in Eschserichia coli
expression in Pseudomonas putida, KT2440
gene epi, functional exxpression in Pseudomonas putida strain KT2440, coexpression with the methylmalonyl-CoA mutase from Escherichia coli leading to production of (2S)-methylmalonyl-CoA in the recombinant strain
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high level expression in Escherichia coli
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in a RNAi vector in Escherichia coli
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recombinant protein is expressed in BL21(DE3) Escherichia coli cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the gene is significantly upregulated under autotrophic compared to heterotrophic growth conditions, implying a role in CO2 fixation; the enzyme expression is significantly upregulated under autotrophic compared to heterotrophic growth conditions
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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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
medicine
synthesis
production of polyketides like myxothiazol requiring methylmalonyl-CoA as an extender unit
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