PMID: 7026235Jul 1, 1981Paper

Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli

European Journal of Biochemistry
A Garrido-Peritierra, R A Cooper

Abstract

The possible involvement of an isomerase in the 4-hydroxyphenylacetate meta-cleavage pathway has been studied. 5-Carboxymethyl-2-hydroxymuconate has been shown to undergo both spontaneous and enzyme-catalysed isomerisation to give 5-carboxymethyl-2-oxo-hex-3-ene-1,5-dioate, a compound with an absorbance maximum at 246 nm. The latter compound rather than the former is the substrate for a decarboxylase that produces 2-hydroxyhepta-2,4-diene,1,7-dioate. The isomerase and decarboxylase enzymes have been purified to over 90% homogeneity. Mg2+ is required for the decarboxylase reaction but not for the isomerase.

Citations

Nov 24, 2004·Biological Chemistry·Babu A ManjasettyUdo Heinemann
Dec 1, 2001·Microbiology and Molecular Biology Reviews : MMBR·E DíazJ L García
Apr 14, 1988·Biochimica Et Biophysica Acta·M SànchezA Garrido-Pertierra
Jul 25, 2020·Protein and Peptide Letters·Eser ÜnsaldıGülay Özcengiz

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