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Degradation of Pyrimidines in Saccharomyces Kluyveri: Transamination of beta-Alanine.

Schnackerz, K D; Andersen, Gorm LU ; Dobritzsch, D and Piskur, Jure LU (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)
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author
organization
publishing date
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
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
2008-09-29 13:58:12
date last changed
2017-01-01 05:00:51
@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},
  keyword      = {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},
  volume       = {27},
  year         = {2008},
}