2-pyrone-4,6-dicarboxylate lactonase
Class of enzymes / From Wikipedia, the free encyclopedia
The enzyme 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57, LigI) catalyzes the reversible hydrolytic reaction
- 2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
Quick Facts Identifiers, EC no. ...
2-pyrone-4,6-dicarboxylate lactonase (LigI) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.1.1.57 | ||||||||
CAS no. | 84177-55-9 | ||||||||
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 | ||||||||
|
Close
This enzyme belongs to the Amidohydrolase superfamily of enzymes and is a member of Cluster of Orthologous Groups (COG) 3618. The systematic name of this enzyme is 2-oxo-2H-pyran-4,6-dicarboxylate lactonohydrolase. This enzyme is found to play an important role in the metabolism of lignin-derived aromatic compounds in both the syringate degradation pathway[1] and the protocatechuate 4,5-cleavage pathway.[2]
LigI from Sphingomonas is of particular interest as it has been shown to be the first member of the amidohydrolase superfamily to not require a divalent metal cation for catalytic activity.[3]