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Involvement of alanine 103 residue in kinetic and physicochemical properties of glucose isomerases from Streptomyces species

The Ala103 to Gly mutation, introduced within the glucose isomerase from Streptomyces sp. SK (SKGI) decreased its catalytic efficiency (kcat/Km) toward D‐glucose from 7.1 to 3 mM–1 min–1. The reverse counterpart replacement Gly103Ala introduced into the glucose isomerase of Streptomyces olivochromog...

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Bibliographic Details
Published in:Biotechnology journal 2007-02, Vol.2 (2), p.254-259
Main Authors: Borgi, Mohamed Ali, Rhimi, Moez, Bejar, Samir
Format: Article
Language:English
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Summary:The Ala103 to Gly mutation, introduced within the glucose isomerase from Streptomyces sp. SK (SKGI) decreased its catalytic efficiency (kcat/Km) toward D‐glucose from 7.1 to 3 mM–1 min–1. The reverse counterpart replacement Gly103Ala introduced into the glucose isomerase of Streptomyces olivochromogenes (SOGI) considerably improved its catalytic efficiency to be 6.7 instead of 3.2 mM–1 min–1. This later mutation also increased the half‐life time of the enzyme from 70 to 95 min at 80°C and mainly modified its pH profile. These results provide evidence that the residue Ala103 plays an essential role in the kinetic and physicochemical properties of glucose isomerases from Streptomyces species.
ISSN:1860-6768
1860-7314
DOI:10.1002/biot.200600085