Structural analysis of the α-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism

Acta Crystallographica Section D: Biological Crystallography

Volumn 71, Issue , 2015, Pages 1382-1391

  Shen, Xing ^a,b   Saburi, Wataru ^b   Gai, Zuoqi ^b   Kato, Koji ^b   Ojima Kato, Teruyo ^c   Yu, Jian ^b   Komoda, Keisuke ^b   Kido, Yusuke ^b   Matsui, Hirokazu ^b   Mori, Haruhide ^b   Yao, Min ^b,d  

^a SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

^b HOKKAIDO UNIVERSITY   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

^d ZHENGZHOU UNIVERSITY   (China)

Author keywords

glucosyl enzyme intermediate; glycoside hydrolase family 13; Halomonas sp. H11; reaction mechanism; substrate specificity; glucosidase

Indexed keywords

HALOMONAS;

ALPHA GLUCOSIDASE;

AMINO ACID SEQUENCE; CATALYSIS; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

ALPHA-GLUCOSIDASES; AMINO ACID SEQUENCE; CATALYSIS; CRYSTALLIZATION; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84931038861     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S139900471500721X     Document Type: Article

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