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Subsite Structure of Rhizopus niveus Glucoamylase, Estimated with the Binding Parameters for Maltooligosaccharides
Author(s) -
Ohnishi Masatake
Publication year - 1990
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.19900420807
Subject(s) - rhizopus , hydrolysis , chemistry , cleavage (geology) , substrate (aquarium) , stereochemistry , affinities , enzyme kinetics , enzyme , biochemistry , active site , biology , fermentation , paleontology , ecology , fracture (geology)
Based on K d and K i for maltosaccarides G n (n = 1 ± 7) and on a specified mode of their binding, the intrinsic affinities A 1 , A 2 , –, A i at subsites i (i = 1 ± 5), were tried to estimate for glucoamylase from Rhizopus niveus . Previously, we have evaluated the apparent values A i using K m and k 0 on the enzyme‐catalyzed hydrolysis for G n , where A 1 is nearly 0 kcal/mol. Thus A 1 , which was found here 3.3 kcal/mol, may be cancelled out with the heat, which is consumed for the hydrolytic cleavage of a substrate glucosyl bond.