Degradation of Pyrimidines in Saccharomyces Kluyveri: Transamination of beta-Alanine.
(2008) In Nucleosides, Nucleotides & Nucleic Acids 27(6). p.794-799- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1181554
- author
- Schnackerz, K D ; Andersen, Gorm LU ; Dobritzsch, D and Piskur, Jure LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Saccharomyces kluyveri, Aminotransferase, gene duplication, γ-aminobutyrate, β-alanine
- in
- Nucleosides, Nucleotides & Nucleic Acids
- volume
- 27
- issue
- 6
- pages
- 794 - 799
- publisher
- Taylor & Francis
- external identifiers
-
- wos:000257338600042
- scopus:46749138244
- pmid:18600542
- ISSN
- 1525-7770
- DOI
- 10.1080/15257770802145983
- language
- English
- LU publication?
- yes
- id
- 2a5ecc46-908d-4a89-afe1-85ebfbd9e942 (old id 1181554)
- date added to LUP
- 2016-04-01 12:17:30
- date last changed
- 2022-01-27 01:34:07
@article{2a5ecc46-908d-4a89-afe1-85ebfbd9e942,
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.}},
author = {{Schnackerz, K D and Andersen, Gorm and Dobritzsch, D and Piskur, Jure}},
issn = {{1525-7770}},
keywords = {{Saccharomyces kluyveri; Aminotransferase; gene duplication; γ-aminobutyrate; β-alanine}},
language = {{eng}},
number = {{6}},
pages = {{794--799}},
publisher = {{Taylor & Francis}},
series = {{Nucleosides, Nucleotides & Nucleic Acids}},
title = {{Degradation of Pyrimidines in Saccharomyces Kluyveri: Transamination of beta-Alanine.}},
url = {{http://dx.doi.org/10.1080/15257770802145983}},
doi = {{10.1080/15257770802145983}},
volume = {{27}},
year = {{2008}},
}