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Comparative study of two trehalases from Candida utilis.

J C Argüelles1, M Gacto

  • 1Departamento de Microbiologia, Facultad de Biologia, Universidad de Murcia, Spain.

Microbiologia (Madrid, Spain)
|October 1, 1986
PubMed
Summary

Candida utilis possesses two distinct trehalase enzymes: a high molecular weight (500 kDa) non-regulatory enzyme and a smaller (280 kDa) regulatory enzyme activated by phosphorylation. These enzymes differ in kinetics, inhibition, and activation properties.

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Science and culture.

International microbiology : the official journal of the Spanish Society for Microbiology·2002

Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Physiology

Background:

  • Trehalase enzymes are crucial for trehalose metabolism in microorganisms.
  • Understanding the distinct properties of trehalase isoforms is key to elucidating their specific roles.

Purpose of the Study:

  • To characterize the two intracellular trehalase enzymes in Candida utilis ATCC 60459.
  • To differentiate their molecular weights, kinetic properties, and regulatory mechanisms.

Main Methods:

  • Ion-exchange chromatography to separate enzymes.
  • Kinetic analysis to determine enzyme properties.
  • Investigating effects of various ions (acetate, Zn2+, Ca2+, Mn2+) and phosphorylation (cAMP, ATP) on enzyme activity.

Main Results:

  • Two trehalases identified: 500 kDa (non-regulatory, acetate-inhibited) and 280 kDa (regulatory, cAMP-activated, cation-modulated).
  • The 500 kDa enzyme constitutes less than 30% of total activity.
  • The 280 kDa enzyme is cryptic, activated by phosphorylation, and modulated by divalent cations (Zn2+, Ca2+, Mn2+).

Conclusions:

  • Candida utilis harbors distinct regulatory and non-regulatory trehalase enzymes.
  • The 280 kDa enzyme exhibits characteristics of a regulatory trehalase, while the 500 kDa enzyme acts as a non-regulatory type.
  • Differential regulation and properties suggest specialized functions for each trehalase isoform.

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