Studies on the Mechanism of the Enzymatic Action of Taka-amylase-A
- 1 October 1963
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 54 (4) , 328-333
- https://doi.org/10.1093/oxfordjournals.jbchem.a127794
Abstract
Taka-amylase A could not hydrolyze phenyl monoacetyl-alpha-maltoside (O-alpha-D-glucopyranosyl-(l[forward arrow]4)-phenyl-6-O-acetyl-alpha-D-glucopyranoside). The monoacetyl derivative did not inhibit hydrolysis of phenyl alpha-maltoside by taka-amylase A. Hydroxyl group at the C-6 position is essential for forming the enzyme-substrate complex.Keywords
This publication has 2 references indexed in Scilit:
- Studies on Taka-amylase AThe Journal of Biochemistry, 1961
- Studies on Taka-Asmylase AThe Journal of Biochemistry, 1959