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.
Keywords: balanine, balanine synthases, pyrimidine degradation, neurotransmitter
Protein & Peptide Letters
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.
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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 |
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