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Open Access Green as soon as Postprint is submitted to ZB.
Mn++-specific reactivation of edta inactivated α-isopropylmalate synthase from Alcaligenes eutrophusH 16.
Biochem. Biophys. Res. Commun. 82, 907-912 (1978)
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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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
1978
HGF-reported in Year
0
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 82,
Issue: 3,
Pages: 907-912
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institut für Mikrobiologie
PubMed ID
29612
Scopus ID
0017812471
Erfassungsdatum
1978-06-14