title: Purification and properties of beta-alanine synthase from calf liver.
abstract: beta-Alanine synthase (EC 3.5.1.6) catalyzes the conversion of N-carbamyl-beta-alanine to beta-alanine, ammonia and CO2. The enzyme has been purified to apparent homogeneity from calf liver. The molecular size, pH optimum and substrate specificity have been determined. Sequence alignment of beta-alanine synthases with N-carbamyl-D-amino acid amidohydrolase from Agrobacter sp. revealed the conservation of a catalytically important triad Glu-Lys-Cys, most likely involved in the breakdown of N-carbamyl-beta-alanine.
authors.affiliation: Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
authors.forename: Günter
authors.initials: G
authors.lastname: Waldmann
authors.forename: Paul F
authors.initials: PF
authors.lastname: Cook
authors.forename: Klaus D
authors.initials: KD
authors.lastname: Schnackerz
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D008099:Liver / Q000201:enzymology*; D051381:Rats
chemical_list: D000581:Amidohydrolases; C021590:beta-ureidopropionase