Information on EC 5.4.99.63 - ethylmalonyl-CoA mutase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.63
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RECOMMENDED NAME
GeneOntology No.
ethylmalonyl-CoA mutase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered)
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ethylmalonyl-CoA pathway
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Glyoxylate and dicarboxylate metabolism
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ethylmalonyl-CoA pathway
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SYSTEMATIC NAME
IUBMB Comments
(2R)-ethylmalonyl-CoA CoA-carbonylmutase
The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Requires coenzyme B12 for activity.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ecm
UniProt
Manually annotated by BRENDA team
strain 2.4.1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
the metabolism of one- and two-carbon compounds by the methylotrophic bacterium Methylobacterium extorquens AM1 involves high carbon flux through the ethylmalonyl-CoA pathway (EMC pathway), metabolic pathway for two carbon metabolism, overview. During growth on ethylamine, the EMC pathway operates as a linear pathway carrying the full assimilatory flux to produce glyoxylate, malate, and succinate, metabolite profiles. Assimilatory carbon enters the ethylmalonyl-CoA pathway directly as acetyl-CoA, bypassing pathways for formaldehyde oxidation/assimilation and the regulatory mechanisms controlling them
physiological function
the ethylmalonyl-CoA pathway, ethylmalonyl-CoA mutase is a metabolic control point to restrict the production of glyoxylate
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-ethylmalonyl-CoA
(2S)-methylsuccinyl-CoA
show the reaction diagram
(R)-2-methylmalonyl-CoA
succinyl-CoA
show the reaction diagram
0.2% of the activity with (2R)-ethylmalonyl-CoA
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?
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
(2R)-ethylmalonyl-CoA
(2S)-methylsuccinyl-CoA
show the reaction diagram
C7C6S9
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r
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosylcobalamin
dependent on
vitamin B12
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
(2R)-ethylmalonyl-CoA
pH 7.8, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
wild-type Methylobacterium extorquens cells grown at steady state on a limiting concentration of succinate, are then switched to ethylamine as growth substrate, a condition where the cell must make a sudden switch from utilizing the tricarboxylic acid cycle to using the ethylmalonyl-CoA pathway for assimilation
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
2 * 75000, SDS-PAGE, 2 * 74000, calculated
75000
2 * 75000, SDS-PAGE, 2 * 74000, calculated
153000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 75000, SDS-PAGE, 2 * 74000, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
computational modeling using the methylmalonyl-CoA mutase substrate complex from P. freudenreichii subsp. shermanii, Protein Data Bank code 4REQ as template
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli
recombinant enzyme. Purified recombinant Ecm is unable to form methylsuccinyl-CoA from ethylmalonyl-CoA when ethylmalonyl-CoA is produced by reductive carboxylation of crotonyl-CoA carboxylase/reductase. Addition of cell extract of the gene insertion mutant ecm::kan to the enzyme assay restores ethylmalonyl-CoA mutase activity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ecm, quantitative enzyme expression analysis, transcriptional profile of EMC pathway genes during the transition from growth on succinate to growth on ethylamine, overview. Recombinant expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
up
growth on ethylamide induces the enzyme, the ethylmalonyl-CoA mutase activity increases to a level sufficient for the observed growth rate at 9 h, which correlates with an upregulation of RNA transcripts for ecm and a decrease in the levels of ethylmalonyl-CoA
additional information