Analysis of the key active subsites of glycoside hydrolase 13 family members

Carbohydrate Research

Volumn 345, Issue 7, 2010, Pages 893-898

  Kumar, Vikash ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Amylases; Conformation change; Distance matrix; Glycoside hydrolase family 13; Structure based sequence alignment; Substrate recognition

Indexed keywords

CONFORMATION CHANGE; DISTANCE MATRICES; GLYCOSIDE HYDROLASES; SEQUENCE ALIGNMENTS; STRUCTURE-BASED; SUBSTRATE RECOGNITION;

ALIGNMENT; AMINO ACIDS; BINDING ENERGY; CATALYSTS; ENZYMES; HYDROGEN BONDS; ORGANIC ACIDS; PHOSPHATASES; SUGARS;

SUBSTRATES;

AMYLASE; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; CYCLOMALTODEXTRINASE; GLYCOSIDASE; NEOPULLULANASE; POLYSACCHARIDE; PULLULANASE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME STRUCTURE; ENZYME SYNTHESIS; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; GLYCOSIDE HYDROLASES; HUMANS; HYDROGEN BONDING; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLVENTS;

EID: 77950595950     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carres.2010.02.007     Document Type: Article

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