Leucine 2,3-aminomutase, an enzyme of leucine catabolism.
The initial step in the fermentation of leucine to acetate, isobutyrate, and ammonia by Clostridium sporogenes is the B12 coenzyme-dependent conversion of alpha-leucine to beta-leucine (3-amino-4-methylpentanoate). The amino group migration reaction, catalyzed by leucine 2,3-aminomutase, is reversible and is inhibited by intrinsic factor. The enzyme activity has been found in several clostridia, in rat, sheep, rhesus, and African green monkey livers, and in human leukocytes.
D000591:Amino Acid Isomerases / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000502:physiology; D003013:Clostridium / Q000201:enzymology*; D019751:Intramolecular Transferases; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D007930:Leucine / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D013045:Species Specificity; D013171:Spores, Bacterial / Q000201:enzymology
D001426:Bacterial Proteins; D000591:Amino Acid Isomerases; D019751:Intramolecular Transferases; C021507:leucine 2,3-aminomutase; D007930:Leucine