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Carboxymethylenebutenolidase

From Wikipedia, the free encyclopedia
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

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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

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  • 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.