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Degradation of pyrimidines in Saccharomyces kluyveri: transamination of beta-alanine
Karolinska Institutet. (Molecular Structural Biology)
2008 (English)In: Nucleosides, Nucleotides & Nucleic Acids, ISSN 1525-7770, E-ISSN 1532-2335, Vol. 27, no 6, 794-799 p.Article in journal (Refereed) Published
Abstract [en]

Beta-alanine is an intermediate in the reductive degradation of uracil. Recently we have identified and characterized the Saccharomyces kluyveri PYD4 gene and the corresponding enzyme beta -alanine aminotransferase ((Sk)Pyd4p), highly homologous to eukaryotic gamma-aminobutyrate aminotransferase (GABA-AT). S. kluyveri has two aminotransferases, GABA aminotransferase ((Sk)Uga1p) with 80% and (Sk)Pyd4p with 55% identity to S. cerevisiae GABA-AT. (Sk)Pyd4p is a typical pyridoxal phosphate-dependent aminotransferase, specific for alpha-ketoglutarate (alpha KG), beta-alanine (BAL) and gamma-aminobutyrate (GABA), showing a ping-pong kinetic mechanism involving two half-reactions and substrate inhibition. (Sk)Uga1p accepts only alpha KG and GABA but not BAL, thus only (Sk)Pydy4p belongs to the uracil degradative pathway.

Place, publisher, year, edition, pages
2008. Vol. 27, no 6, 794-799 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-214424DOI: 10.1080/15257770802145983PubMedID: 18600542OAI: oai:DiVA.org:uu-214424DiVA: diva2:685003
Available from: 2014-01-08 Created: 2014-01-08 Last updated: 2014-01-09Bibliographically approved

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