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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 möglich sobald Postprint bei der ZB eingereicht worden ist.
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).
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
ISSN (print) / ISBN 0006-291X
e-ISSN 1090-2104
Zeitschrift Biochemical and Biophysical Research Communications
Quellenangaben Band: 82, Heft: 3, Seiten: 907-912 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institut für Mikrobiologie