Distribution of the isopropylmalate pathway to leucine among diverse bacteria.
alpha-Isopropylmalate synthase and beta-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 alpha-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.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D002474:Cell-Free System; D003998:Dicarboxylic Acids / Q000096:biosynthesis / Q000378:metabolism*; D007930:Leucine / Q000096:biosynthesis* / Q000494:pharmacology; D007652:Oxo-Acid-Lyases / Q000037:antagonists & inhibitors / Q000378:metabolism; D013045:Species Specificity; D014631:Valerates
D003998:Dicarboxylic Acids; D014631:Valerates; D000429:Alcohol Oxidoreductases; D007652:Oxo-Acid-Lyases; D007930:Leucine