The effects of various n-substituted maleimides on succinic thiokinase of Escherichia coli

J. Michael Matula, Jonathan S. Nishimura

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

1. 1. Even-chained N-alkyl maleimides, up to 10 carbon atoms in chain length, were tested for their ability to inactivate Escherichia coli succinic thiokinase. 2. 2. The pseudo-second-order inactivation constant, k2, was proportional to the chain length of the maleimides. 3. 3. However, the specificity with respect to sulfhydryl groups of the protein attacked appeared to be the same. 4. 4. The presence of ATP or CoA protected the enzyme partially against inactivation by both N-ethylmaleimide and N-hexylmaleimide.

Original languageEnglish (US)
Pages (from-to)213-215
Number of pages3
JournalInternational Journal of Biochemistry
Volume9
Issue number3
DOIs
StatePublished - 1978
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'The effects of various n-substituted maleimides on succinic thiokinase of Escherichia coli'. Together they form a unique fingerprint.

Cite this