PMID: 1225912Sep 1, 1975

Studies on the substrate specificity of Taka-amylase A. XII. Investigation of the active site of Taka-amylase A by examining the properties of p-phenylazobenzoyl Taka-amylase A

Journal of Biochemistry
K OmichiY Matsushima

Abstract

1. When p-phenylazobenzoyl Taka-amylase A (PhAB-TAA) was incubated at pH 6.5 with hydroxylamine for 3 hr at 20degrees, some of the p-phenylazobenzoyl residues that had been introduced into Taka-amylase A (TAA) [1, 4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1, Aspergillus oryzae] were liberated as a hydroxamic acid, and the activity pattern of PhAB-TAA changed to that of intact TAA. This result suggested that the p-phenylazobenzoyl residues liberated had been bound to the tyrosyl residue located near the active site in the enzyme. 2. The transferase action of TAA or PhAB-TAA was studied using phenyl alpha-maltoside as a substrate and maltotritol as an acceptor. Unlike intact TAA, PhAB-TAA was not able to transfer the maltose residue to maltotritol, and this suggested that the p-phenylazobenzoyl residue was located near one of the aglycone-binding subsites, causing steric hindrance.

Related Concepts

Structure-Activity Relationship
Plasma Protein Binding Capacity
Amylases
Chromatography, Gas-Liquid
Transferase
Benzoate

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