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  • Title: Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.
    Author: Meyer P, Liger D, Leulliot N, Quevillon-Cheruel S, Zhou CZ, Borel F, Ferrer JL, Poupon A, Janin J, van Tilbeurgh H.
    Journal: Biochimie; 2005 Dec; 87(12):1041-7. PubMed ID: 16226833.
    Abstract:
    We have determined the three-dimensional crystal structure of the protein encoded by the open reading frame YFL030w from Saccharomyces cerevisiae to a resolution of 2.6 A using single wavelength anomalous diffraction. YFL030w is a 385 amino-acid protein with sequence similarity to the aminotransferase family. The structure of the protein reveals a homodimer adopting the fold-type I of pyridoxal 5'-phosphate (PLP)-dependent aminotransferases. The PLP co-factor is covalently bound to the active site in the crystal structure. The protein shows close structural resemblance with the human alanine:glyoxylate aminotransferase (EC 2.6.1.44), an enzyme involved in the hereditary kidney stone disease primary hyperoxaluria type 1. In this paper we show that YFL030w codes for an alanine:glyoxylate aminotransferase, highly specific for its amino donor and acceptor substrates.
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