Aspartokinase III, a new isozyme in Bacillus subtilis 168.

Abstract:

:A previously undetected Bacillus subtilis aspartokinase isozyme, which we have called aspartokinase III, has been characterized. The new isozyme was most readily detected in extracts of cells grown with lysine, which repressed aspartokinase II and induced aspartokinase III, or in extracts of strain VS11, a mutant lacking aspartokinase II. Antibodies against aspartokinase II did not cross-react with aspartokinase III. Aspartokinases II and III coeluted on gel filtration chromatography at Mr 120,000, which accounts for the previous inability to detect it. Aspartokinase III was induced by lysine and repressed by threonine. It was synergistically inhibited by lysine and threonine. Aspartokinase III activity, like aspartokinase II activity, declined rapidly in B. subtilis cells that were starved for glucose. In contrast, the specific activity of aspartokinase I, the diaminopimelic acid-inhibitable isozyme, was constant under all growth conditions examined.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Graves LM,Switzer RL

doi

10.1128/jb.172.1.218-223.1990

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

218-23

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

172

pub_type

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