PuSH - Publication Server of Helmholtz Zentrum München

Wiegel, J.W.

Mn++-specific reactivation of edta inactivated α-isopropylmalate synthase from Alcaligenes eutrophusH 16.

Biochem. Biophys. Res. Commun. 82, 907-912 (1978)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
The α-isopropylmalate synthase (EC 4.1.3.12) from AlcaligeneseutrophusH 16 was inactivated by EDTA in a time-dependent reaction. Only the addition of Mn++ plus dithiothreitol could restore the activity. The substrate, α-ketoisovalerate, prevented the inactivation; the feedback inhibitor, leucine, and it's antagonist, valine, increased the rate of inactivation. Except for α,α′-bipyridyl, chelating reagents, other than EDTA had no effect on the enzyme stability. It is suggested that the α-isopropylmalate synthase is a metallo enzyme - the evidence points to Mn++ as the metal ion - and that this enzyme uses a mechanism of catalysis which differs from that of the analogous malate synthase (EC 4.1.3.2) and citrate synthase (EC 4.1.3.4).
Altmetric
Additional Metrics?
[➜Log in]
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 0006-291X
e-ISSN 1090-2104
Journal Biochemical and Biophysical Research Communications
Quellenangaben Volume: 82, Issue: 3, Pages: 907-912 Article Number: , Supplement: ,
Publisher Elsevier
Reviewing status Peer reviewed
Institute(s) Institut für Mikrobiologie