2-pyrone-4,6-dicarboxylate lactonase

Class of enzymes 2-pyrone-4,6-dicarboxylate lactonase (LigI) 3.1.1.57 84177-55-9 0047554 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57, LigI) is an enzyme that catalyzes the reversible hydrolytic reaction 60% Q27102682 2-oxo-2H-pyran-4,6-dicarboxylic acid 0.7 reversible H2O H2O Q61041491 4-oxalmesaconic acid The enzyme characterised from Pseudomonas species hydrolyses 2-oxo-2H-pyran-4,6-dicarboxylic acid to 4-oxalmesaconic acid.Kersten PJ, Dagley S, Whittaker JW, Arciero DM, Lipscomb JD 1982 2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species J. Bacteriol. 152 1154–62 7142106 3 10.1128/jb.152.3.1154-1162.1982 221622 Maruyama K February 1983 Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase J. Biochem. 93 557–65 6841353 2 10.1093/oxfordjournals.jbchem.a134210 free The reaction is part of the degradation pathwy for gallic acid.Nogales Juan Canales Ángeles Jiménez-Barbero Jesús Serra Beatriz Pingarrón José Manuel García José Luis Díaz Eduardo 3 Unravelling the gallic acid degradation pathway in bacteria: The gal cluster from Pseudomonas putida Molecular Microbiology 2011 79 2 359–374 10.1111/j.1365-2958.2010.07448.x 21219457 It plays an important role in the metabolism of lignin-derived aromatic compounds in both the syringate degradation pathway http://metacyc.org/META/NEW-IMAGE?type=PATHWAY&object=PWY-6339&detail-level=3&detail-level=2 Syringate degradation SRI International MetaCyc and the protocatechuate 4,5-cleavage pathway. http://metacyc.org/META/NEW-IMAGE?type=PATHWAY&object=P184-PWY&detail-level=3+ Protocatechuate degradation I (meta-cleavage pathway) SRI International MetaCyc The enzyme belongs to the amidohydrolase superfamily and is a member of Cluster of Orthologous Groups (COG) 3618. LigI from Sphingomonas is of particular interest as it has been shown to be the first amidohydrolase not to require a divalent metal cation for catalytic activity. The systematic name of this enzyme is 2-oxo-2H-pyran-4,6-dicarboxylate lactonohydrolase.3.1.1.57 Mechanism The mechanism of catalysis of LigI has been determined by crystallography and NMR analysis. The hydrolytic water molecule is activated by the transfer of a proton to Asp-248 whereas the carbonyl group of the 2-pyrone-4,6-dicarboxylate (PDC) lactone substrate is activated by hydrogen bonding interactions with His-180, His-31, and His-33.Hobbs ME, Malashkevich V, Williams HJ, Xu C, Sauder JM, Burley SK, Almo SC, Raushel FM Structure and Catalytic Mechanism of LigI: Insight into the Amidohydrolase Enzymes of cog3618 and Lignin Degradation Biochemistry 51 16 3497–507 April 2012 22475079 10.1021/bi300307b 3416963 References Biology no Category:EC 3.1.1 Category:Enzymes of known structure