The X-ray crystallographic structure and specificity profile of HAD superfamily phosphohydrolase BT1666: Comparison of paralogous functions in B. thetaiotaomicron

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 11, 2011, Pages 3099-3107

  Lu, Zhibing ^a   Dunaway Mariano, Debra ^b   Allen, Karen N ^a  

^a USA   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

Author keywords

Bacteroides thetaiotaomicron; BT1666; BT4131; Divergent evolution; Haloalkanoate dehalogenase superfamily; Housekeeping; Phosphatase; Phosphohydrolase; Substrate promiscuity

Indexed keywords

BT1666 PHOSPHATASE; ENZYME; HALOALKANOATE DEHALOGENASE SUPERFAMILY; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BACTEROIDES THETAIOTAOMICRON; BIOINFORMATICS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; METABOLITE; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEADY STATE; X RAY CRYSTALLOGRAPHY;

BACTEROIDES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

BACTEROIDES THETAIOTAOMICRON; BACTEROIDES THETAIOTAOMICRON VPI-5482;

EID: 80054006773     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23137     Document Type: Article

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