Information on EC 5.4.99.63 - ethylmalonyl-CoA mutase

for references in articles please use BRENDA:EC5.4.99.63
Word Map on EC 5.4.99.63
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.63
-
RECOMMENDED NAME
GeneOntology No.
ethylmalonyl-CoA mutase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular
-
isomerization
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered)
-
-
ethylmalonyl-CoA pathway
Glyoxylate and dicarboxylate metabolism
-
-
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
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
gene ecm
UniProt
Manually annotated by BRENDA team
Rhodobacter sphaeroides ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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)-ethylmalonyl-CoA
(2S)-methylsuccinyl-CoA
show the reaction diagram
(R)-2-methylmalonyl-CoA
succinyl-CoA
show the reaction diagram
additional information
?
-
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
additional information
?
-
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
0.05
pH 7.8, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
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
additional information