Comparison of the two isofunctional enol-lactone hydrolases from Acinetobacter calcoaceticus.

Abstract:

:The rates of thermal denaturation and the molecular weights of the two isofunctional enol-lactone hydrolases (ELH I and ELH II) of Acinetobacter calcoaceticus were determined. The molecular weights of ELH I and ELH II were found by gel filtration to be approximately 24,000 and 21,000, respectively. In crude extract at 45 C the two enzymes showed a marked difference in rate of thermal denaturation. After chromatography on Sephadex G-100, however, the rates were nearly identical. The thermolability of ELH II in crude extract was shown to be due to its sensitivity to an unidentified component of the crude extract which modified its rate of thermal denaturation. In the light of the physical similarities of the two enzymes, it is concluded that the different regulatory patterns imposed upon the two enzymes do not provide sufficient evidence that they are the product of two different structural genes.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Katagiri M,Wheelis ML

doi

10.1128/JB.106.2.369-374.1971

subject

Has Abstract

pub_date

1971-05-01 00:00:00

pages

369-74

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

106

pub_type

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