Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein.

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.

• Authors: Philippe Meyer, Dominique Liger, Nicolas Leulliot, Sophie Quevillon-Cheruel, Cong-Zhao Zhou, Franck Borel, Jean-Luc Ferrer, Anne Poupon, Joël Janin, Herman van Tilbeurgh
• Journal: Biochimie (Biochimie) Vol. 87 Issue 12 Pg. 1041-7 (Dec 2005) ISSN: 0300-9084 [Print] France
• PMID: 16226833 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Saccharomyces cerevisiae Proteins
• Transaminases
• AGX1 protein, S cerevisiae

Topics

• Carbohydrate Conformation
• Crystallography, X-Ray
• Kinetics
• Models, Molecular
• Saccharomyces cerevisiae (chemistry, enzymology, metabolism)
• Saccharomyces cerevisiae Proteins (chemistry, metabolism)
• Transaminases (chemistry, metabolism)
• X-Ray Diffraction