Glutaconyl-CoA decarboxylase

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glutaconyl-CoA decarboxylase
Identifiers
EC no. 7.2.4.5
CAS no. 84399-93-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

In enzymology, a glutaconyl-CoA decarboxylase (EC 7.2.4.5) is an enzyme that catalyzes the chemical reaction [1]

(2E)-glutaconyl-CoA + H+ + Na+(in) (2E)-butenoyl-CoA + CO
2
+ Na+(out)

Hence, this enzyme has one substrate, (2E)-glutaconyl-CoA, and two products, (2E)-butenoyl-CoA and CO2. During the process, an sodium ion is transported across the membrane. Previously, this enzyme was classified as EC 4.1.1.70. [1] [2]

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming). Other names in common use include glutaconyl coenzyme A decarboxylase, pent-2-enoyl-CoA carboxy-lyase, and 4-carboxybut-2-enoyl-CoA carboxy-lyase. This enzyme participates in benzoate degradation via coa ligation and butanoate metabolism.

As a decarboxylase, the enzyme requires biotin for its function. [1] [2]

Structural studies

As of mid-2024, five structures have been solved for this class of enzymes, with the PDB accession codes 1PIX, 3GF3, 3GF7, 3GLM and 3GMA.

Related Research Articles

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Biotin-dependent malonate decarboxylase (EC 4.1.1.89, malonate decarboxylase (with biotin), malonate decarboxylase) is an enzyme with systematic name malonate carboxy-lyase (biotin-dependent). This enzyme catalyses the following chemical reaction

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References

  1. 1 2 3 "ENZYME - 7.2.4.5 glutaconyl-CoA decarboxylase". enzyme.expasy.org. Retrieved 2024-07-16.
  2. 1 2 Kress, Daniel; Brügel, Daniela; Schall, Iris; Linder, Dietmar; Buckel, Wolfgang; Essen, Lars-Oliver (October 2009). "An Asymmetric Model for Na+-translocating Glutaconyl-CoA Decarboxylases". Journal of Biological Chemistry. 284 (41): 28401–28409. doi: 10.1074/jbc.m109.037762 . ISSN   0021-9258. PMC   2788889 . PMID   19654317.