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Identification and characterization of a novel glucose-phosphorylating enzyme in Kluyveromyces lactis.

Authors
  • Kettner, Karina
  • Müller, Eva-Christina
  • Otto, Albrecht
  • Rödel, Gerhard
  • Breunig, Karin D
  • Kriegel, Thomas M
Type
Published Article
Journal
FEMS yeast research
Publication Date
Aug 01, 2007
Volume
7
Issue
5
Pages
683–692
Identifiers
PMID: 17573926
Source
Medline
License
Unknown

Abstract

Recent data suggest that hexokinase KlHxk1 (Rag5) represents the only glucose-phosphorylating enzyme of Kluyveromyces lactis, which also is required for glucose signalling. Long-term growth studies of a K. lactis rag5 mutant, however, reveal slow growth on glucose, but no growth on fructose. Isolation of the permissive glucose-phosphorylating enzyme, mass spectrometric tryptic peptide analysis and determination of basic kinetic data identify a novel glucokinase (KlGlk1) encoded by ORF KLLA0C01,155g. In accordance with the growth characteristics of the rag5 mutant, KlGlk1 phosphorylates glucose, but fails to act on fructose as a sugar substrate. Multiple sequence alignment indicates the presence of at least one glucokinase gene in all sequenced yeast genomes.

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