Galactaro δ-lactone isomerase

Lactone isomerization by a member of the amidohydrolase superfamily

Jason T. Bouvier, Fiona P. Groninger-Poe, Matthew Vetting, Steven C. Almo, John Alan Gerlt

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)614-616
Number of pages3
JournalBiochemistry
Volume53
Issue number4
DOIs
StatePublished - Feb 4 2014

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Amidohydrolases
Isomerases
Lactones
Isomerization
4 alpha-glucanotransferase
Hydrolysis
Agrobacterium tumefaciens
Lignin
Catalysis
Carbon
Degradation
Oxidation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Galactaro δ-lactone isomerase : Lactone isomerization by a member of the amidohydrolase superfamily. / Bouvier, Jason T.; Groninger-Poe, Fiona P.; Vetting, Matthew; Almo, Steven C.; Gerlt, John Alan.

In: Biochemistry, Vol. 53, No. 4, 04.02.2014, p. 614-616.

Research output: Contribution to journalArticle

Bouvier, Jason T. ; Groninger-Poe, Fiona P. ; Vetting, Matthew ; Almo, Steven C. ; Gerlt, John Alan. / Galactaro δ-lactone isomerase : Lactone isomerization by a member of the amidohydrolase superfamily. In: Biochemistry. 2014 ; Vol. 53, No. 4. pp. 614-616.
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