Abstract
α-Isopropylmalate synthase (EC 4.1.3.12) is present in extracts of Bacteroides fragilis, Clostridium thermoaceticum, Clostridium formicoacetium, Clostridium pasteurianum, and Clostridium kluyveri with specific activities (μmol α-isopropylmalate formed per min and g protein) of 8.6, 8.9, 2.4, 1.9, and 0.3, respectively. The product α-isopropylmalate was identified by gas chromatography combined with mass spectroscopy. The presence of 5 mM leucine in the growth medium represses the synthesis of α-isopropylmalate synthase in C. thermoaceticum by 40 and 70 %. The enzyme from C. pasteurianum was partially purified to a specific activity of 1413. All studied enzyme properties are similar to those of the enzymes from aerobic bacteria. It is suggested that in these anaerobic bacteria the α-isopropylmalate pathway is present in addition to the pathway via the ferrodoxin-dependent, reductive carboxylation of branched chain fatty acids.
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Abbreviations
- α-KIV:
-
α-Ketoisovalerate
- α-IPM:
-
α-Isopropylmalate
- CoA:
-
Coenzyme A
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Wiegel, J. α-Isopropylmalate synthase as a marker for the leucine biosynthetic pathway in several clostridia and in Bacteroides fragilis . Arch. Microbiol. 130, 385–390 (1981). https://doi.org/10.1007/BF00414605
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DOI: https://doi.org/10.1007/BF00414605