Relationship of sequence and structure to specificity in the α-amylase family of enzymes

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1546, Issue 1, 2001, Pages 1-20

  MacGregor, E Ann ^a   Janeček, Štefan ^b   Svensson, Birte ^c  

^a UNIVERSITY OF MANITOBA   (Canada)

^b INSTITUTE OF CHEMISTRY   (Slovakia)

^c CARLSBERG LABORATORY   (Denmark)

Author keywords

1,4 Glucoside bond; 1,6 Glucoside bond; Amylase family; Glycoside hydrolase family 13; Glycoside hydrolase family 70; Glycoside hydrolase family 77; Sequence motif; Specificity

Indexed keywords

AMYLASE; ASPARTIC ACID; GLUCOSIDE; GLUTAMIC ACID; GLYCOSIDASE; HISTIDINE; HYDROLASE; TRANSFERASE;

AMINO ACID SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; GENETIC ENGINEERING; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CARBOHYDRATE SEQUENCE; CATALYSIS; CONSENSUS SEQUENCE; GLYCOSIDE HYDROLASES; HUMANS; MODELS, CHEMICAL; MODELS, MOLECULAR; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0035831255     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00302-2     Document Type: Review

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