Crystal structure of glycoside hydrolase family 127 β-l- arabinofuranosidase from Bifidobacterium longum

Biochemical and Biophysical Research Communications

Volumn 447, Issue 1, 2014, Pages 32-37

  Ito, Tasuku ^a   Saikawa, Kyo ^a   Kim, Seonah ^b   Fujita, Kiyotaka ^c   Ishiwata, Akihiro ^d   Kaeothip, Sophon ^e   Arakawa, Takatoshi ^a   Wakagi, Takayoshi ^a   Beckham, Gregg T ^a,b   Ito, Yukishige ^d,e   Fushinobu, Shinya ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL RENEWABLE ENERGY LABORATORY   (United States)

^c KAGOSHIMA UNIVERSITY   (Japan)

^d RIKEN   (Japan)

^e JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Crystal structure; DUF1680; Human gut bacteria; Plant polysaccharide; Quantum mechanical calculations; Retaining glycoside hydrolase

Indexed keywords

ARABINOFURANOSIDASE; BETA ARABINOFURANOSIDASE; CARBON; CYSTEINE; GLUTAMIC ACID; NUCLEOPHILE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BIFIDOBACTERIUM LONGUM; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; METAL BINDING; NONHUMAN; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DOMAIN; QUANTUM CHEMISTRY; REACTION ANALYSIS;

BACTERIA (MICROORGANISMS); BIFIDOBACTERIUM LONGUM;

CRYSTAL STRUCTURE; DUF1680; HUMAN GUT BACTERIA; PLANT POLYSACCHARIDE; QUANTUM MECHANICAL CALCULATIONS; RETAINING GLYCOSIDE HYDROLASE;

AMINO ACID SEQUENCE; ARABINOSE; BIFIDOBACTERIUM; CATALYTIC DOMAIN; CYSTEINE; GLUTAMIC ACID; GLYCOSIDE HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; QUANTUM THEORY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; ZINC;

EID: 84899484472     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.03.096     Document Type: Article

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