The Role of a Tyrosine Residue of Bacterial Liquefying α-Amylase in the Enzymatic Hydrolysis of Linear Substrates as Studied by Chemical Modification with Acetic Anhydride*
- 1 July 1974
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 76 (1) , 7-13
- https://doi.org/10.1093/oxfordjournals.jbchem.a130561
Abstract
A tyrosine residue of liquefying α-amylase [EC 3.2.1.1] from B. subtilis was acetyl-ated with acetic anhydride and the effect of the modification on the rate of enzyme reaction was studied with a series of maltooligosaccharides. It was found that the acetylation of a tyrosine residue leads to partial loss of enzyme activity and that the effect does not depend appreciably on the degree of polymerization (n) of the linear substrates in the range n=3˜7 and 760. The results are consistent with the supposition that the modified tyrosine residue is located at a subsite near the catalytic site and is involved in the productive binding of all the substrates studied.Keywords
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