Acetohydroxy acid synthase activity from a mutation at ilvF in Escherichia coli K-12.

Abstract:

:Examination of the ilvF locus at 54 min on the Escherichia coli K-12 chromosome revealed that it is a cryptic gene for expression of a valine-resistant acetohydroxy acid synthase (acetolactate synthase; EC 4.1.3.18) distinct from previously reported isozymes. A spontaneous mutation, ilvF663, yielded IlvF+ enzyme activity that was multivalently repressed by all three branched-chain amino acids, was completely insensitive to feedback inhibition, was highly stable at elevated temperatures, and expressed optimal activity at 50 degrees C. The IlvF+ enzyme activity was expressed in strains in which isozyme II was inactive because of the ilvG frameshift in the wild-type strain K-12 and isozymes I and III were inactivated by point mutations or deletions. Tn5 insertional mutagenesis yielded two IlvF- mutants, with the insertion in ilvF663 in each case. These observations suggest that the ilvF663 locus may be a coding region for a unique acetohydroxy acid synthase activity.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Alexander-Caudle C,Latinwo LM,Jackson JH

doi

10.1128/jb.172.6.3060-3065.1990

subject

Has Abstract

pub_date

1990-06-01 00:00:00

pages

3060-5

issue

6

eissn

0021-9193

issn

1098-5530

journal_volume

172

pub_type

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