Energetic and mechanistic studies of glucoamylase using molecular recognition of maltose OH groups coupled with site-directed mutagenesis

Biochemistry

Volumn 39, Issue 29, 2000, Pages 8585-8592

  Sierks, Michael R ^a   Svensson, Birte ^b  

^a UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

^b CARLSBERG LABORATORY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAN 1,4 ALPHA GLUCOSIDASE; MALTOSE;

AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS NIGER; CONFORMATIONAL TRANSITION; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; HYDROGEN BOND; MOLECULAR RECOGNITION; MUTATION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ASPERGILLUS NIGER; BINDING SITES; ENERGY METABOLISM; ENZYME STABILITY; GLUCAN 1,4-ALPHA-GLUCOSIDASE; HYDROGEN BONDING; KINETICS; MALTOSE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ASPERGILLUS NIGER; FELIS CATUS;

EID: 0034713823     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9925219     Document Type: Article

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