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Biochemistry. 2014 Feb 4;53(4):614-6. doi: 10.1021/bi5000492. Epub 2014 Jan 24.

Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.

Author information

1
Department of Biochemistry, ‡Department of Chemistry, and §Institute for Genomic Biology, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.

Abstract

Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to D-galactaro-1,5-lactone. We have identified a novel enzyme, D-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone. GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. The ability of GLI to catalyze lactone isomerization instead of hydrolysis can be explained by the absence of the general basic catalysis used by 2-pyrone-4,6-dicarboxylate lactonase.

PMID:
24450804
PMCID:
PMC3977579
DOI:
10.1021/bi5000492
[Indexed for MEDLINE]
Free PMC Article

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