Involvement of glycine and aspartate residues in the binding capacity of FAD in the NADH dehydrogenase from an alkaliphilic Bacillus.

Abstract:

:There is a region exhibiting a similarity of amino acid sequence near the carboxyl-terminal segment of each FAD-containing oxidoreductase. In this region, four amino acid residues-Thr, Ala, Gly, and Asp-are highly conserved. To determine the involvement of the four amino acid residues (Thr-469, Ala-476, Gly-478, and Asp-479) in the activity of NADH dehydrogenase of an alkaliphilic Bacillus, mutations of these amino acid residues were conducted. In spite of high conservation, mutations of Thr-469 and Ala-476 to Ala and Ser, respectively, did not lead to a critical loss of enzyme activity. However, mutations of Gly-478 and Asp-479 to Ala caused a complete loss of the activity, which appears to result from the loss of binding capacity of FAD.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Shiraki M,Koyama N

doi

10.1007/s00284-002-3911-6

keywords:

subject

Has Abstract

pub_date

2003-06-01 00:00:00

pages

432-4

issue

6

eissn

0343-8651

issn

1432-0991

journal_volume

46

pub_type

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