SUBSITE AFFINITIES OF ASPERGILLUS-NIGER GLUCOAMYLASE-II DETERMINED WITH P-NITROPHENYLMALTOOLIGOSACCHARIDES

被引：18

作者：

ERMER, J ^{[1
]}

ROSE, K ^{[1
]}

HUBNER, G ^{[1
]}

SCHELLENBERGER, A ^{[1
]}

机构：

[1] MARTIN LUTHER UNIV,INST BIOCHEM,ENZYMOL ABT,WEINBERWEG 16A,PSF 8,O-4010 HALLE,GERMANY

来源：

BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1993年 / 374卷 / 02期

关键词：

GLUCOAMYLASE-II; P-NITROPHENYLMALTOOLIGOSACCHARIDE; KINETICS; SUBSITE STRUCTURE;

D O I：

10.1515/bchm3.1993.374.1-6.123

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Kinetic parameters were obtained for glucoamylase catalysed hydrolysis of substrates of an alpha-(1,4)-maltooligosaccharide series and of a p-nitrophenyl-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.

引用

页码：123 / 128

页数：6

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