Purification and Properties of β-Alanine Synthase from Calf Liver

Title: Purification and Properties of β-Alanine Synthase from Calf Liver

Volume: 12 Issue: 1

Author(s): Gunter Waldmann, Paul F. Cook and Klaus D. Schnackerz

Affiliation:

Keywords: balanine, balanine synthases, pyrimidine degradation, neurotransmitter

Abstract: β-Alanine synthase (EC 3.5.1.6) catalyzes the conversion of N-carbamyl-β-alanine to β-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 β-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-β-alanine.

Cite this article as:

Waldmann Gunter, Cook F. Paul and Schnackerz D. Klaus, Purification and Properties of β-Alanine Synthase from Calf Liver, Protein & Peptide Letters 2005; 12 (1) . https://dx.doi.org/10.2174/0929866053405904

DOI https://dx.doi.org/10.2174/0929866053405904	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305