Carboxymethylenebutenolidase
carboxymethylenebutenolidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.1.1.45 | ||||||||
CAS no. | 76689-22-0 | ||||||||
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 | ||||||||
|
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
[edit]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
[edit]- 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.