
Glycogen synthesis by amylosucrase from Neisseria perflava
Author(s) -
Colin R. MacKenzie,
Kenneth G. Johnson,
I. McDonald
Publication year - 1977
Publication title -
canadian journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.635
H-Index - 94
eISSN - 1480-3275
pISSN - 0008-4166
DOI - 10.1139/m77-196
Subject(s) - biochemistry , chemistry , enzyme , levansucrase , glucan , fructose , polysaccharide , glycosyltransferase , sucrose , glucosyltransferases , glucosyltransferase , moiety , stereochemistry , biology , bacillus subtilis , bacteria , genetics
Amylosucrase (sucrose:1,4-alpha-D-glucan 4-alpha-glucosyltransferase; EC 2.4.1.4) which mediates the transfer of the glucosyl moiety of sucrose to a growing alpha-1,4-glucan chain is a constitutive enzyme of Neisseria perflava. The products of enzymic action are insoluble glycogenlike polysaccharides and fructose, the latter being a competitive inhibitor of the enzyme (Ki=20 mM). The enzyme is extremely stable and appears to bind very tightly to its polymerized product. Properties of product-bound enzyme reflect those of the native complex.