Evidence for an isomeric muconolactone isomerase involved in the metabolism of 4-methylmuconolactone by Alcaligenes eutrophus JMP134.
An enzyme specifically induced during 4-methylmuconolactone metabolism by Alcaligenes eutrophus JMP 134 and that exhibited muconolactone isomerizing activity was purified to homogeneity. The enzyme, involved in the isomerization of 3-methylmuconolactone had a high degree of sequence similarity with muconolactone isomerase of Alcaligenes eutrophus JMP 134 and other previously described muconolactone isomerases of the 3-oxoadipate pathway. Kinetic analysis showed that the enzyme has a substrate spectrum and a reaction mechanism similar to those of the muconolactone isomerase, but that it has distinct kinetic properties.
Prucha
M
M
Bereich Mikrobiologie, Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
Peterseim
A
A
Pieper
D H
DH
D000421:Alcaligenes / Q000201:enzymology* / Q000378:metabolism; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D019751:Intramolecular Transferases; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007535:Isomerases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D007783:Lactones / Q000378:metabolism*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
C107899:4-methylmuconolactone; D007527:Isoenzymes; D007783:Lactones; D007535:Isomerases; C061587:4-methylmuconolactone methyl-isomerase; D019751:Intramolecular Transferases