Thermodynamics of binding of heterobidentate ligands consisting of spacer-connected acarbose and β-cyclodextrin to the catalytic and starch- binding domains of glucoamylase from Aspergillus niger shows that the catalytic and starch-binding sites are in close proximity in space

Biochemistry

Volumn 37, Issue 29, 1998, Pages 10446-10452

  Sigurskjold, Bent W ^a   Christensen, Trine ^a   Payre, Nathalie ^b   Cottaz, Sylvain ^b   Driguez, Hugues ^b   Svensson, Birte ^c  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b CENTRE DE RECHERCHES SUR LES MACROMOLÉCULES VÉGÉTALES CERMAV CNRS   (France)

^c CARLSBERG LABORATORY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ACARBOSE; BETA CYCLODEXTRIN; GLUCAN 1,4 ALPHA GLUCOSIDASE; STARCH;

ARTICLE; ASPERGILLUS NIGER; BINDING SITE; CARBOHYDRATE METABOLISM; LIGAND BINDING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; THERMODYNAMICS;

ACARBOSE; ARGININE; ASPERGILLUS NIGER; BETA-CYCLODEXTRINS; BINDING SITES; CALORIMETRY; CATALYSIS; CYCLODEXTRINS; ENZYME INHIBITORS; GLUCAN 1,4-ALPHA-GLUCOSIDASE; HYDROGEN BONDING; LIGANDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; STARCH; THERMODYNAMICS; TRISACCHARIDES;

ASPERGILLUS NIGER;

EID: 0032555254     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9807310     Document Type: Article

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