Subsite affinities of Aspergillus niger glucoamylase II determined with p-nitrophenylmaltooligosaccharides.
Kinetic parameters were obtained for glucoamylase catalysed hydrolysis of substrates of an alpha-(1,4)-maltooligosaccharide series and of a p-nitro-phenyl-alpha-maltooligosaccharide series. p-Nitrophenyl substrates of chain length 11 and 17 were synthesized in 97% and 95% purity, respectively, to test the significance of binding at remote subsites. The affinities of the subsites > 4 are demonstrated to be insignificant. The subsite binding contributions for D-glucopyranosyl and for p-nitrophenyl residues were calculated.
Ermer
J
J
Abteilung Enzymologie, Martin-Luther-Universität Halle/Wittenberg.
Rose
K
K
Hübner
G
G
Schellenberger
A
A
D001234:Aspergillus niger / Q000201:enzymology*; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D009596:Nitrophenols / Q000378:metabolism; D009844:Oligosaccharides / Q000138:chemical synthesis / Q000378:metabolism*; D013379:Substrate Specificity
D009596:Nitrophenols; D009844:Oligosaccharides; C021705:maltooligosaccharides; D005087:Glucan 1,4-alpha-Glucosidase; D005947:Glucose