2-pyrone-4,6-dicarboxylate lactonase

In enzymology, 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57) is an enzyme that catalyzes the reversible hydrolytic chemical reaction 2-pyrone-4,6-dicarboxylate + H2O 4-carboxy-2-hydroxyhexa-2,4-dienedioate and 4-oxalomesaconate Thus, the two substrates of this enzyme are 2-pyrone-4,6-dicarboxylate and H2O, whereas its product is a tautomeric mixture of 4-oxalomesaconate and 4-carboxy-2-hydroxymuconate. 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.

2-pyrone-4,6-dicarboxylate lactonase

In enzymology, 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57) is an enzyme that catalyzes the reversible hydrolytic chemical reaction 2-pyrone-4,6-dicarboxylate + H2O 4-carboxy-2-hydroxyhexa-2,4-dienedioate and 4-oxalomesaconate Thus, the two substrates of this enzyme are 2-pyrone-4,6-dicarboxylate and H2O, whereas its product is a tautomeric mixture of 4-oxalomesaconate and 4-carboxy-2-hydroxymuconate. 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.