KEGG   ENZYME: 7.2.4.3Help
Entry
EC 7.2.4.3                  Enzyme                                 

Name
(S)-methylmalonyl-CoA decarboxylase (sodium-transporting);
methylmalonyl-coenzyme A decarboxylase (ambiguous);
(S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect);
(S)-methylmalonyl-CoA carboxy-lyase (ambiguous)
Class
Translocases;
Catalysing the translocation of inorganic cations;
Linked to decarboxylation
BRITE hierarchy
Sysname
(S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)
Reaction(IUBMB)
(S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]
Substrate
(S)-methylmalonyl-CoA [CPD:C00683];
Na+[side 1];
H+[side 2]
Product
propanoyl-CoA [CPD:C00100];
CO2 [CPD:C00011];
Na+[side 2]
Comment
This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
History
EC 7.2.4.3 created 1972 as EC 4.1.1.41, modified 1983, modified 1986, transferred 2018 to EC 7.2.4.3
Reference
1  [PMID:5646172]
  Authors
Galivan JH, Allen SH.
  Title
Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus.
  Journal
J Biol Chem 243:1253-61 (1968)
Reference
2  [PMID:7070502]
  Authors
Hilpert W, Dimroth P.
  Title
Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient.
  Journal
Nature 296:584-5 (1982)
Reference
3  [PMID:2920730]
  Authors
Hoffmann A, Hilpert W, Dimroth P.
  Title
The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens.
  Journal
Eur J Biochem 179:645-50 (1989)
DOI:10.1111/j.1432-1033.1989.tb14596.x
Reference
4  [PMID:7601825]
  Authors
Huder JB, Dimroth P
  Title
Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli.
  Journal
J Bacteriol 177:3623-30 (1995)
DOI:10.1128/JB.177.13.3623-3630.1995
  Sequence
Reference
5  [PMID:9428714]
  Authors
Bott M, Pfister K, Burda P, Kalbermatter O, Woehlke G, Dimroth P
  Title
Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex.
  Journal
Eur J Biochem 250:590-9 (1997)
DOI:10.1111/j.1432-1033.1997.0590a.x
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 7.2.4.3
IUBMB Enzyme Nomenclature: 7.2.4.3
ExPASy - ENZYME nomenclature database: 7.2.4.3
BRENDA, the Enzyme Database: 7.2.4.3
CAS: 37289-44-4

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