The fully conserved Asp residue in conserved sequence region I of the α-amylase family is crucial for the catalytic site architecture and activity

FEBS Letters

Volumn 541, Issue 1-3, 2003, Pages 47-51

  Leemhuis, Hans ^a   Rozeboom, Henriëtte J ^a   Dijkstra, Bauke W ^a   Dijkhuizen, Lubbert ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

CGTase; Cyclodextrin glycosyltransferase; Glycoside hydrolase; Structure; Amylase

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; AMYLASE; ARGININE; ASPARTIC ACID; CARBOXYLIC ACID; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; ISOAMYLASE; OLIGO 1,6 GLUCOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STRUCTURE; ENZYME SYNTHESIS; HYDROGEN BOND; INFORMATION PROCESSING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN INTERACTION; STRUCTURE ANALYSIS;

EID: 0344406252     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00286-2     Document Type: Article

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