Enhanced acetohydroxy acid synthase III activity in an ilvH mutant of Escherichia coli K-12.

Abstract:

:The acetohydroxy acid synthase III isozyme, which catalyzes the first common step in the biosynthesis of isoleucine, leucine, and valine in Escherichia coli K-12, is composed of two subunits, the ilvI and ilvH gene products. A missense mutation in ilvH (ilvH612), which reduced the sensitivity of the enzyme to the end product inhibition by valine, also increased its specific activity and lowered the Km for alpha-acetolactate synthesis. The mutation increased the sensitivity of acetohydroxy acid synthase III to dialysis and heat treatment and reduced the requirement for thiamine pyrophosphate addition to the assay mixture for activity. A strain carrying the ilvH612 mutation grew better than a homologous ilvH+ strain in the presence of leucine. The data indicate that this is a consequence of a more active acetohydroxy acid synthase III isozyme rather than the result of an alteration of the leucine-mediated repression of the ilvIH operon.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Ricca E,Limauro D,Lago CT,de Felice M

doi

10.1128/jb.170.11.5197-5199.1988

subject

Has Abstract

pub_date

1988-11-01 00:00:00

pages

5197-9

issue

11

eissn

0021-9193

issn

1098-5530

journal_volume

170

pub_type

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