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Archives of Microbiology

, Volume 150, Issue 2, pp 155–159 | Cite as

Dihydroxyacetone kinase from a methylotrophic yeast, Hansenula polymorpha CBS 4732

Purification, characterization and physiological role
  • Nobuo Kato
  • Hiroshi Yoshikawa
  • Katsuhiko Tanaka
  • Masayuki Shimao
  • Chikahiro Sakazawa
Original Papers

Abstract

Dihydroxyacetone (DHA) kinase was purified to electrophoretic homogeneity from methanol-grown Hansenula polymorpha CBS 4732. The enzyme was a dimer with a molecular weight of 150,000, and had an isoelectric point of 4.9. The enzyme was active toward DHA, and D- and L-glyceraldehydes as phosphorylation acceptors, and only ATP served as a donor. ADP inhibited the enzyme at a physiological concentration. Magnesium ion was essential for the activity and stability. Some other divalent cations can substitute in part the magnesium ion. The DHA kinases found in cells grown on methanol and glycerol were immunologically identical, but were different from those of other methylotrophic yeasts as shown by immunotitration. A mutant (204D) derived from the yeast, which could not grow on methanol or DHA but could so on glycerol, was deficient in DHA kinase. Glycerol kinase activity was found in glycerol-grown 204D cells as well as the parent strain.

Key words

Hansenula polymorpha Dihydroxyacetone kinase Glycerol kinase Methanol Glycerol 

Abbreviation

DHA

dihydroxyacetone

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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • Nobuo Kato
    • 1
  • Hiroshi Yoshikawa
    • 1
  • Katsuhiko Tanaka
    • 1
  • Masayuki Shimao
    • 1
  • Chikahiro Sakazawa
    • 1
  1. 1.Department of Environmental Chemistry and TechnologyTottori UniversityTottoriJapan

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