@article {Waldmann:2005:0929-8665:69,
title = "Purification and Properties of -Alanine Synthase from Calf Liver",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2005",
volume = "12",
number = "1",
publication date ="2005-01-01T00:00:00",
pages = "69-73",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2005/00000012/00000001/art00010",
doi = "doi:10.2174/0929866053405904",
keyword = "balanine synthases, neurotransmitter, pyrimidine degradation, balanine",
author = "Waldmann, Gunter and Cook, Paul F. and Schnackerz, Klaus D.",
abstract = "-Alanine synthase (EC 3.5.1.6) catalyzes the conversion of N-carbamyl--alanine to -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 -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--alanine.",
}