Some properties of trehalase from Phycomyces blakesleeanus.
Trehalase (alpha, alpha-trehalase glucohydrolase EC 3.2.1.28) from Phycomyces spores occurs in two different forms which are convertible in vivo: a form with low activity found in dormant spores and an active form after breaking the dormancy. Between the two forms no difference in molecular weight and electrophoretic mobility can be detected. The molecular weight is estimated by gel filtration at about 210 000. The relation between substrate concentration and trehalase activity follows the Michaelis-Menten equation (K-m plus or minus 55 mM) in activated spores whereas in dormant spores trehalase shows a different substrate binding, indicating a negative cooperative effect. They differ further in thermostability and in sensitivity to inhibition by ATP. Other nucleosidephosphates have no inhibiting effect. Heating the spores at different temperatures between 38 and 44 degrees C results in a partial breaking of dormancy of the spore population and a corresponding partial activation of trehalase. This suggests a close connection between breaking dormancy and trehalase activation.
D002850:Chromatography, Gel; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D005658:Fungi / Q000201:enzymology*; D006358:Hot Temperature; D007700:Kinetics; D010800:Phycomyces / Q000201:enzymology*; D012265:Ribonucleotides / Q000494:pharmacology; D013172:Spores, Fungal / Q000201:enzymology; D013997:Time Factors; D014198:Trehalase / Q000302:isolation & purification / Q000378:metabolism*
D012265:Ribonucleotides; D014198:Trehalase