Specificity of sweet-almond alpha-galactosidase.
1. The specificity of purified sweet-almond alpha-galactosidase has been investigated with 17 substrates. 2. Some of them exhibited inhibition at high substrate concentrations but others did not. Both substrate types were bound and hydrolysed at the same site on the enzyme. 3. The enzyme is specific for alpha-d-galactosides and beta-l-arabinosides. It did not hydrolyse beta-d-galactosides or alpha-d-glucosides. 4. Among galactosides the order of decreasing rates of enzymic hydrolysis was: aryl alpha-galactosides; sugars; alkyl alpha-galactosides. 5. All substituents in the aryl moiety of aryl alpha-galactosides enhanced V(max.), the electron-releasing (-sigma) groups being more effective than the electron-withdrawing (+sigma) groups. The substituent groups did not alter K(m) appreciably. 6. Implications of these results are discussed from a mechanistic viewpoint.
D002384:Catalysis; D004187:Disaccharides / Q000378:metabolism*; D005696:Galactosidases / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism*; D006600:Hexosephosphates; D007700:Kinetics; D009596:Nitrophenols; D009754:Nuts; D009844:Oligosaccharides / Q000378:metabolism*
D004187:Disaccharides; D006027:Glycosides; D006600:Hexosephosphates; D009596:Nitrophenols; D009844:Oligosaccharides; D005696:Galactosidases