KEGG   ENZYME: 4.1.1.70Help
Entry
EC 4.1.1.70                 Enzyme                                 

Name
glutaconyl-CoA decarboxylase;
glutaconyl coenzyme A decarboxylase;
pent-2-enoyl-CoA carboxy-lyase;
4-carboxybut-2-enoyl-CoA carboxy-lyase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming)
Reaction(IUBMB)
4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO2 [RN:R03028]
Reaction(KEGG)
Substrate
4-carboxybut-2-enoyl-CoA [CPD:C02411]
Product
but-2-enoyl-CoA [CPD:C00877];
CO2 [CPD:C00011]
Comment
The enzyme from Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.
History
EC 4.1.1.70 created 1986, modified 2003
Pathway
Benzoate degradation
Butanoate metabolism
Microbial metabolism in diverse environments
Orthology
K01615  
glutaconyl-CoA decarboxylase
Genes
VPR: 
AFN: 
FNU: 
Taxonomy
Reference
1  [PMID:6628393]
  Authors
Buckel W, Semmler R.
  Title
Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria.
  Journal
Eur. J. Biochem. 136 (1983) 427-34.
  Organism
Acidaminococcus fermentans, Peptococcus aerogenes, Clostridium symbiosum, Clostridium tetanomorphum
Reference
2  [PMID:11248185]
  Authors
Buckel W.
  Title
Sodium ion-translocating decarboxylases.
  Journal
Biochim. Biophys. Acta. 1505 (2001) 15-27.
  Organism
Acidaminococcus fermentans
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
84399-93-9

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