Site-directed mutagenesis of conserved residues of Clostridium thermocellum endoglucanase CelC.

Abstract:

:Four conserved residues of Clostridium thermocellum endoglucanase CelC were replaced by site-directed mutagenesis. Proteins mutated in His-90, Asn-139 and Glu-140 showed strongly reduced activity, in agreement with predictions of sequence alignments. Mutations in Glu-140 did not result in any detectable change in Km, or apparent size, suggesting that Glu-140 is directly involved in catalysis. The pH optimum of the proteins carrying the Glu-140/Ala and Glu140/Gln mutations was lower than that of the wild type, whereas the activity vs. pH profile of Glu-140/Asp CelC was similar to that of the wild type, suggesting that Glu-140 may act as a proton donor.

authors

Navas J,Béguin P

doi

10.1016/0006-291x(92)92274-2

subject

Has Abstract

pub_date

1992-12-15 00:00:00

pages

807-12

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)92274-2

journal_volume

189

pub_type

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