Comparative study of two trehalases from Candida utilis.
Candida utilis ATCC 60459 contains two intracellular trehalase enzymes clearly distinguishable by molecular weight, behaviour in ion-exchange chromatography and kinetic properties. The high molecular weight trehalase (500 kDa trehalase) is specifically inhibited by acetate and accounts for less than 30% of the total trehalase activity found in cell extracts. The smaller trehalase (280 kDa trehalase) exists mostly as a cryptic enzyme whose activity can be postranslationally activated by cAMP-dependent phosphorylation. The enzyme activity of the 280 kDa trehalase is strongly inhibited by Zn2+ and markedly enhanced in the presence of Ca2+ and Mn2+. The activation by these cations, contrariwise to that induced by ATP and cAMP, does not imply a covalent modification of the 280 kDa enzyme. Several parameters have been determined for both enzymes. The 280 kDa enzyme has the properties shown by the so-called regulatory trehalases whereas the 500 kDa enzyme presents characteristics of a nonregulatory type of trehalase.
Argüelles
J C
JC
Departamento de Microbiologia, Facultad de Biologia, Universidad de Murcia, Spain.
Gacto
M
M
D000255:Adenosine Triphosphate / Q000494:pharmacology; D002175:Candida / Q000201:enzymology*; D002412:Cations / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D000242:Cyclic AMP / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D014198:Trehalase / Q000302:isolation & purification* / Q000378:metabolism
D002412:Cations; D005656:Fungal Proteins; D007527:Isoenzymes; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D014198:Trehalase