Carboxymethylenebutenolidase

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carboxymethylenebutenolidase
Identifiers
EC no.3.1.1.45
CAS no.76689-22-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a carboxymethylenebutenolidase (EC 3.1.1.45, also known as CMBL and dienelactone hydrolase) is an enzyme that catalyzes the chemical reaction

4-carboxymethylenebut-2-en-4-olide + H2O 4-oxohex-2-enedioate

Thus, the two substrates of this enzyme are 4-carboxymethylenebut-2-en-4-olide and H2O, whereas its product is 4-oxohex-2-enedioate.

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-carboxymethylenebut-2-en-4-olide lactonohydrolase. Other names in common use include maleylacetate enol-lactonase, dienelactone hydrolase, and carboxymethylene butenolide hydrolase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1DIN, 1GGV, 1ZI6, 1ZI8, 1ZI9, 1ZIC, 1ZIX, 1ZIY, 1ZJ4, and 1ZJ5.

References

  • Schmidt E, Knackmuss HJ (1980). "Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid". Biochem. J. 192 (1): 339–47. doi:10.1042/bj1920339. PMC 1162339. PMID 7305906.