Affiliation:
1. Department of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14850
Abstract
α-Isopropylmalate synthase and β-isopropylmalate dehydrogenase activities were detected in extracts of the following organisms:
Chromatium
D,
Rhodopseudomonas spheroides, Hydrogenomonas
H16,
Pseudomonas aeruginosa, Pseudomonas fluorescens, Vibrio extorquens, Rhizobium japonicum, Alcaligenes viscolactis, Escherichia coli
B,
Proteus vulgaris, Aerobacter aerogenes, Salmonella typhimurium, Micrococcus
sp.,
Micrococcus lysodeikticus, Bacillus polymyxa, Bacillus subtilis
, and
Nocardia opaca
. The α-isopropylmalate synthase activity in these extracts was inhibited by low concentrations of
l
-leucine. Taken together with other data, these results suggest that the isopropylmalate pathway is widespread among organisms that can synthesize leucine.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference32 articles.
1. Studies on the metabolic function of branched-chain volatile fattY acids. growth factors for ruminococci. I. Incorporation of isovalerate into leucine. ,J;Allison M. J.;Bacteriol.,1962
2. Importance ot the isovalerate carboxylation pathway of leucine biosynthesis in the rumen;Allison M. J.;Appl. Microbiol.,1966
3. The biosynthesis of valine from isobutyrate bv Peptostreptococcus elsdenii and Bacteroides ruminicola;Allison M. J.;Biochem. J.,1971
4. Nickel dependent chemolithotropic growth of two Hvdrogenomonas strains. ,J;Bartha R.;Bacteriol.,1965
5. Preferential compatibility in Streptomvces uiolaceoruber. .J;Bradlev G. X.;Gen. Microbiol.,1960
Cited by
35 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献