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

FEMS Yeast Res. 2007 Aug;7(5):683-92. doi: 10.1111/j.1567-1364.2007.00259.x. Epub 2007 Jun 16.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Fructose / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / metabolism
  • Gene Expression Regulation, Fungal*
  • Glucokinase* / chemistry
  • Glucokinase* / genetics
  • Glucokinase* / isolation & purification
  • Glucokinase* / metabolism
  • Glucose / metabolism
  • Humans
  • Kluyveromyces / enzymology*
  • Kluyveromyces / genetics
  • Kluyveromyces / growth & development
  • Molecular Sequence Data
  • Phosphorylation
  • Phylogeny
  • Sequence Alignment
  • Substrate Specificity

Substances

  • Fungal Proteins
  • Fructose
  • Glucokinase
  • Glucose