Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases

Proceedings of the National Academy of Sciences of the United States of America

Volumn 92, Issue 15, 1995, Pages 7090-7094

  Henrissat, Bernard ^a   Callebaut, Isabelle ^b   Fabrega, Sylvie ^c   Lehn, Pierre ^c   Mornon, Jean Paul ^b   Davies, Gideon ^d  

^a CENTRE DE RECHERCHES SUR LES MACROMOLÉCULES VÉGÉTALES CERMAV CNRS   (France)

^b UNIVERSITÉ PIERRE ET MARIE CURIE   (France)

^c HÔPITAL ROBERT DEBRÉ   (France)

^d UNIVERSITY OF YORK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAN 1,4 ALPHA GLUCOSIDASE; GLYCOSIDASE; THIOGLUCOSIDASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; EVOLUTION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; CLUSTER ANALYSIS; COMPARATIVE STUDY; CONSERVED SEQUENCE; DATABASES, FACTUAL; EVOLUTION; GLYCOSIDE HYDROLASES; LYSOSOMES; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T;

EID: 0029166485     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.15.7090     Document Type: Article

References (32)