Leucine 2,3-aminomutase, an enzyme of leucine catabolism

Autor:	J M, Poston
Rok vydání:	1976
Předmět:	Clostridium Spores Bacterial Kinetics Bacterial Proteins Liver Species Specificity Leucine Animals Kidney Intramolecular Transferases Amino Acid Isomerases
Zdroj:	The Journal of biological chemistry. 251(7)
ISSN:	0021-9258
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::b66ef8134c097c0f9ee2e072018c25ed https://pubmed.ncbi.nlm.nih.gov/1270414 Zobrazit plný text záznamu