Degradation of pyrimidines in Saccharomyces kluyveri: transamination of beta-alanine
Research output: Contribution to journal › Journal article › Research › peer-review
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.
| Original language | English |
|---|---|
| Journal | Nucleosides, Nucleotides and Nucleic Acids |
| Volume | 27 |
| Issue number | 6 |
| Pages (from-to) | 794-9 |
| Number of pages | 5 |
| ISSN | 1525-7770 |
| DOIs | |
| Publication status | Published - 2008 |
Bibliographical note
Keywords: 4-Aminobutyrate Transaminase; Amination; D-Alanine Transaminase; Kinetics; Pyrimidines; Saccharomyces; Sequence Analysis, DNA; beta-Alanine; gamma-Aminobutyric Acid
ID: 14146202