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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
Published on: June 20, 2014
Purification and properties of beta-alanine synthase from calf liver
Günter Waldmann1, Paul F Cook, Klaus D Schnackerz
1Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
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.
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