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Stereochemical course of hydrolytic reaction catalyzed by alpha-galactosidase from cold adaptable marine bacterium of genus Pseudoalteromonas.

ABSTRACT: The recombinant ?-galactosidase of the marine bacterium (?-PsGal) was synthesized with the use of the plasmid 40Gal, consisting of plasmid pET-40b (+) (Novagen) and the gene corresponding to the open reading frame of the mature ?-galactosidase of marine bacterium Pseudoalteromonas sp. KMM 701, transformed into the Escherichia coli Rosetta(DE3) cells. In order to understand the mechanism of action, the stereochemistry of hydrolysis of 4-nitrophenyl ?-D-galactopyranoside (4-NPGP) by ?-PsGal was measured by (1)H NMR spectroscopy. The kinetics of formation of ?- and ?-anomer of galactose showed that ?-anomer initially formed and accumulated, and then an appreciable amount of ?-anomer appeared as a result of mutarotation. The data clearly show that the enzymatic hydrolysis of 4-NPGP proceeds with the retention of anomeric configuration, probably, due to a double displacement mechanism of reaction.

SUBMITTER: Bakunina IY 

PROVIDER: S-EPMC4195319 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Stereochemical course of hydrolytic reaction catalyzed by alpha-galactosidase from cold adaptable marine bacterium of genus Pseudoalteromonas.

Bakunina Irina Y IY   Balabanova Larissa A LA   Golotin Vasiliy A VA   Slepchenko Lyubov V LV   Isakov Vladimir V VV   Rasskazov Valeriy A VA  

Frontiers in chemistry 20141013

The recombinant α-galactosidase of the marine bacterium (α-PsGal) was synthesized with the use of the plasmid 40Gal, consisting of plasmid pET-40b (+) (Novagen) and the gene corresponding to the open reading frame of the mature α-galactosidase of marine bacterium Pseudoalteromonas sp. KMM 701, transformed into the Escherichia coli Rosetta(DE3) cells. In order to understand the mechanism of action, the stereochemistry of hydrolysis of 4-nitrophenyl α-D-galactopyranoside (4-NPGP) by α-PsGal was me  ...[more]

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