Steric course of the hydrolysis of alpha,alpha-trehalose and alpha-D-glucosyl fluoride catalyzed by pig kidney trehalase.
We are unable to confirm the report of Labat et al.3 that pig kidney trehalase hydrolyzes alpha,alpha-trehalose to form solely alpha-D-glucose. Highly purified trehalase from pig renal cortex was found, in reactions monitored by 1H-n.m.r. spectra, to hydrolyze alpha,alpha-trehalose with the formation of both alpha- and beta-D-glucose. That the beta anomer constitutes the enzymically mobilized glucosyl residue is indicated by the further finding that beta-D-glucose is the product formed on hydrolysis of alpha-D-glucosyl fluoride by the enzyme. Present results show the stereochemical behavior of pig kidney trehalase in hydrolyzing alpha,alpha-trehalose to be indistinguishable from that reported by ourselves and others for trehalase preparations from a range of biological sources including rabbit renal cortex.
Nakano
M
M
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461.
Brewer
C F
CF
Kasumi
T
T
Hehre
E J
EJ
D000818:Animals; D004187:Disaccharides; D005947:Glucose / Q000031:analogs & derivatives*; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D013237:Stereoisomerism; D013552:Swine; D014198:Trehalase / Q000378:metabolism*; D014199:Trehalose
D004187:Disaccharides; C030364:glucosyl fluoride; D014199:Trehalose; D014198:Trehalase; D005947:Glucose