Substrate recognition and hydrolysis by a family 50 exo-β-agarase, aga50D, from the marine bacterium Saccharophagus degradans

Journal of Biological Chemistry

Volumn 288, Issue 39, 2013, Pages 28078-28088

  Pluvinage, Benjamin ^a   Hehemann, Jan Hendrik ^a,b   Boraston, Alisdair B ^a  

^a UNIVERSITY OF VICTORIA   (Canada)

^b Massachusetts Institute of Technology Cambridge   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE ARCHITECTURE; CATALYTIC MECHANISMS; GLYCOSIDE HYDROLASES; MARINE BACTERIUM; MICHAELIS COMPLEX; SACCHAROPHAGUS DEGRADANS; STRUCTURAL WORKS; SUBSTRATE RECOGNITION;

ENZYME ACTIVITY; HYDROLYSIS;

SUBSTRATES;

50 EXO BETA AGARASE; AGAROSE; GLYCOSIDASE; OLIGOMER; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME SUBSTRATE; MARINE BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SACCHAROPHAGUS DEGRADANS; STRUCTURE ANALYSIS;

BACTERIAL METABOLISM; CARBOHYDRATE PROCESSING; GLYCOBIOLOGY; GLYCOSIDE HYDROLASES; POLYSACCHARIDE;

ALTEROMONADACEAE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARBOHYDRATE METABOLISM; CATALYSIS; CATALYTIC DOMAIN; GLYCOSIDE HYDROLASES; GLYCOSIDES; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEPHAROSE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84884773798     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.491068     Document Type: Article

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