Characterization of Ruminococcus albus cellodextrin phosphorylase and identification of a key phenylalanine residue for acceptor specificity and affinity to the phosphate group

FEBS Journal

Volumn 280, Issue 18, 2013, Pages 4463-4473

  Sawano, Tatsuya ^a   Saburi, Wataru ^a   Hamura, Ken ^a   Matsui, Hirokazu ^a   Mori, Haruhide ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

acceptor binding site; cellodextrin phosphorylase; glycoside hydrolase family 94; phosphate binding site; substrate specificity

Indexed keywords

BACTERIAL ENZYME; BETA 1,4 MANNOBIOSE; BETA 1,4 XYLOBIOSE; CARBOHYDRATE DERIVATIVE; CELLOBIITOL; CELLODEXTRIN PHOSPHORYLASE; CELLOHEXAOSE; CELLOPENTAOSE; CELLOTRIOSE; GLUCOSE 1 PHOSPHATE; GLUTAMINE; GLYCOSIDASE; HISTIDINE; LAMINARIBIOSE; MUTANT PROTEIN; N,N' DIACETYLCHITOBIOSE PHOSPHORYLASE; OLIGOSACCHARIDE; PHENYLALANINE; PHOSPHATE; SOPHOROSE; TYROSINE; UNCLASSIFIED DRUG; VALINE; BACTERIAL PROTEIN; CELLOBIOSE; CELLODEXTRIN; CELLULOSE; DEXTRIN; DRUG DERIVATIVE; GLUCOSYLTRANSFERASE; MALTOPENTAOSE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOHYDRATE SYNTHESIS; CATALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME RELEASE; ENZYME STRUCTURE; NONHUMAN; PHOSPHOROLYSIS; PRIORITY JOURNAL; RUMINOCOCCUS ALBUS; WILD TYPE; ACCEPTOR BINDING SITE; CHEMISTRY; CLASSIFICATION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; GLYCOSIDE HYDROLASE FAMILY 94; HYDROLYSIS; KINETICS; METABOLISM; MUTATION; PHOSPHATE BINDING SITE; PHYLOGENY; RUMINOCOCCUS; THERMODYNAMICS;

RUMINOCOCCUS ALBUS;

ACCEPTOR BINDING SITE; CELLODEXTRIN PHOSPHORYLASE; GLYCOSIDE HYDROLASE FAMILY 94; PHOSPHATE BINDING SITE; SUBSTRATE SPECIFICITY;

BACTERIAL PROTEINS; CELLOBIOSE; CELLULOSE; DEXTRINS; ESCHERICHIA COLI; GLUCOSYLTRANSFERASES; HYDROLYSIS; KINETICS; MUTATION; OLIGOSACCHARIDES; PHENYLALANINE; PHYLOGENY; RECOMBINANT PROTEINS; RUMINOCOCCUS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 84883457467     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12408     Document Type: Article

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