Author/Editor		Schnackerz, KD; Andersen, G; Dobritzsch, D; Piškur, J
Title		Degradation of pyrimidines in Saccharomyces kluyveri: transamination of beta-alanine
Type		članek
Source		Nucleosides Nucleotides Nucleic Acids
Vol. and No.		Letnik 27, št. 6
Publication year		2008
Volume		str. 794-9
Language		eng
Abstract		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.
Descriptors		AMINATION KINETICS PYRIMIDINES SACCHAROMYCES SEQUENCE ANALYSIS, DNA BETA-ALANINE