Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme

Biochemistry

Volumn 44, Issue 25, 2005, Pages 9022-9033

  Katsemi, Vicky ^a,c   Lücke, Christian ^a,d   Koepke, Juergen ^b   Löhr, Frank ^a   Maurer, Steffen ^a   Fritzsch, Günter ^b   Rüterjans, Heinz ^a  

^a GOETHE UNIVERSITY   (Germany)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^c HELLENIC PASTEUR INSTITUTE   (Greece)

^d MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; ENZYMES; HYDROLYSIS; MOLECULAR STRUCTURE; MUTAGENESIS; REACTION KINETICS; SUBSTRATES;

LIGANDS; MUTANTS; SUBSTRATE BINDING SITES; WILD-TYPE ENZYMES;

ENZYME KINETICS;

CALCIUM; DIISOPROPYLFLUOROPHOSPHATASE; HISTIDINE; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; CALCIUM BINDING; CONTROLLED STUDY; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROLYSIS; HYDROPHOBICITY; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM; SITE DIRECTED MUTAGENESIS; SQUID; WILD TYPE;

ANIMALS; ASPARAGINE; BINDING SITES; CALCIUM; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLLUSCA; MUTATION; PHOSPHORIC TRIESTER HYDROLASES; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

LOLIGO VULGARIS;

EID: 21944455433     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0500675     Document Type: Article

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