Marine Rhodobacteraceae l -haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water

FEBS Journal

Volumn 280, Issue 7, 2013, Pages 1664-1680

  Novak, Halina R ^a   Sayer, Christopher ^a   Isupov, Michail N ^a   Paszkiewicz, Konrad ^a   Gotz, Dorothee ^b   Mearns Spragg, Andrew ^b   Littlechild, Jennifer A ^a  

^a UNIVERSITY OF EXETER   (United Kingdom)

^b Aquapharm Biodiscovery Limited   (United Kingdom)

Author keywords

crystal structure; enzyme mechanism; l 2 haloacid dehalogenase; marine bacterium; novel enzyme

Indexed keywords

ARGININE; ASPARAGINASE; ASPARTIC ACID; BACTERIAL PROTEIN; GLUTAMIC ACID; HALOACID; HALOACID DEHALOGENASE; HISTIDINE; UNCLASSIFIED DRUG; WATER;

ARTICLE; CATALYSIS; CATALYST; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTON TRANSPORT; RHODOBACTERACEAE; STRUCTURE ANALYSIS; TEMPERATURE; THERMOSTABILITY;

AMINO ACID SEQUENCE; AQUATIC ORGANISMS; ARGININE; ASPARAGINE; BINDING SITES; CATALYTIC DOMAIN; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESCHERICHIA COLI; GLYCINE; HISTIDINE; HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; RHODOBACTERACEAE; SOLVENTS; SUBSTRATE SPECIFICITY; TEMPERATURE; WATER;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; RHODOBACTERACEAE;

EID: 84875852457     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12177     Document Type: Article

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