Some details of the reaction mechanism of glucoamylase from Aspergillus niger - Kinetic and structural studies on Trp52→Phe and Trp317→Phe mutants

European Journal of Biochemistry

Volumn 250, Issue 3, 1997, Pages 638-645

  Christensen, Trine ^a,b   Stoffer, Bjarne B ^a   Svensson, Birte ^b   Christensen, Ulla ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b CARLSBERG LABORATORY   (Denmark)

Author keywords

Binding reaction models; Glucoamylase; Mutation of Trp52 and of Trp317; Presteady state kinetics

Indexed keywords

GLUCAN 1,4 ALPHA GLUCOSIDASE;

ARTICLE; ASPERGILLUS NIGER; CATALYST; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; MUTANT; NONHUMAN; PRIORITY JOURNAL;

ASPERGILLUS NIGER;

EID: 0031574082     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00638.x     Document Type: Article

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