Literature DB >> 3133246

Thiol reagents are substrates for the ADP-ribosyltransferase activity of pertussis toxin.

M D Lobban1, S van Heyningen.   

Abstract

Thiols such as cysteine and dithiothreitol are substrates for the ADP-ribosyltransferase activity of pertussis toxin. When cysteine was incubated with NAD+ and toxin at pH 7.5, a product containing ADP-ribose and cysteine (presumably ADP-ribosylcysteine) was isolated by high-performance liquid chromatography, and characterized by its composition and release of AMP with phosphodiesterase. Cysteine has a Km of 105 mM at saturating NAD+ concentration. The ability of thiols to act as a substrate is one explanation for the very high concentrations (250 mM or greater) that have been observed to enhance the apparent NAD glycohydrolase activity of the toxin.

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Year:  1988        PMID: 3133246     DOI: 10.1016/0014-5793(88)80432-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

Review 1.  Enzymatic and nonenzymatic ADP-ribosylation of cysteine.

Authors:  L J McDonald; J Moss
Journal:  Mol Cell Biochem       Date:  1994-09       Impact factor: 3.396

Review 2.  Mechanisms of action of nitrates.

Authors:  K E Torfgård; J Ahlner
Journal:  Cardiovasc Drugs Ther       Date:  1994-10       Impact factor: 3.727

3.  The purification of a cysteine-dependent NAD+ glycohydrolase activity from bovine erythrocytes and evidence that it exhibits a novel ADP-ribosyltransferase activity.

Authors:  B A Saxty; S van Heyningen
Journal:  Biochem J       Date:  1995-09-15       Impact factor: 3.857

  3 in total

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