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HERO ID
4824489
Reference Type
Journal Article
Title
Malic enzyme: its purification and characterization fromMucor circinelloides and occurrence in other oleaginous fungi
Author(s)
Savitha, J; Wynn, JP; Ratledge, C
Year
1997
Is Peer Reviewed?
1
Journal
World Journal of Microbiology and Biotechnology
ISSN:
0959-3993
EISSN:
1573-0972
Publisher
Springer Science & Business Media
Volume
13
Issue
1 (Jan 1997)
Page Numbers
7
Abstract
Malic enzyme was purified 43-fold from Mucor circinelloides. The enzyme was dependent on Mg^sup 2+^ or Mn^sup 2+^ for activity, was not active with Dmalate and had a pH optimum at 7.8. The apparent K^sub m^ values for malate and NADP^sup +^ were 488 ΜM and 41 Μm respectively. The M^sub r^ of the native enzyme was 160 kDa. Five metabolic analogues of malate: oxaloacetate, tartronic acid, 1-methylenecyclopropane trans-2,3-dicarboxyIic acid, malonic acid and glutaric acid, were found to inhibit malic enzyme activity at 10 mM. Four oleaginous fungi, Mucor circinelloides, Mortierella alpina, Mortierella elongata and Pythium ultimum, were also examined, all possessed a soluble malic enzyme, two also possessed a microsomal malic enzyme.[PUBLICATION ABSTRACT]
Keywords
Enzymes; Acids; Bacteria
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