Identification of the conserved spatial position of key active-site atoms in glycoside hydrolase 13 family members

Carbohydrate Research

Volumn 345, Issue 11, 2010, Pages 1564-1569

  Kumar, Vikash ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Amylases; Conserved position; Glycoside hydrolase family 13; Hydrolytic water; Ligand interactions; Substrate recognition

Indexed keywords

, INHIBITOR; 3D STRUCTURE; ATOMIC LEVELS; CARBOXYL GROUPS; CATALYTIC TRIAD; CHEMICAL NATURE; COMPUTATIONAL STUDIES; GLYCOSIDE HYDROLASES; PROTON DONORS; SPATIAL ARRANGEMENTS; SPATIAL POSITIONS; SUBSITES; SUBSTRATE RECOGNITION; WATER LIGANDS; WATER OXYGEN ATOMS;

AMINO ACIDS; HYDROGEN BONDS; LIGANDS; ORGANIC ACIDS; OXYGEN; SUBSTRATES; SUGARS;

ATOMS;

AMINO ACID; ASPARTIC ACID; GLUTAMINE; GLYCOSIDASE; GLYCOSIDE HYDROLASE 13; HYDROGEN; OXYGEN; UNCLASSIFIED DRUG; WATER; GLUCOSE;

ARTICLE; ATOM; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROLYSIS; PRIORITY JOURNAL; RECOGNITION; ANIMAL; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; HUMAN; METABOLISM; NUCLEOTIDE SEQUENCE;

ANIMALS; CATALYTIC DOMAIN; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; GLUCOSE; GLYCOSIDE HYDROLASES; HUMANS; MODELS, MOLECULAR;

EID: 77953872498     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carres.2010.04.027     Document Type: Article

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