Structure and kinetics of phosphonopyruvate hydrolase from Voriovorax sp. Pal2: New insight into the divergence of catalysis within the pep mutase/isocitrate lyase superfamily

Biochemistry

Volumn 45, Issue 38, 2006, Pages 11491-11504

  Chen, Celia C H ^a   Han, Ying ^b   Niu, Weiling ^b   Kulakova, Anna N ^d   Howard, Andrew ^c   Quinn, John P ^d   Dunaway Mariano, Debra ^b   Herzberg, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b UNIVERSITY OF NEW MEXICO   (United States)

^c ILLINOIS INSTITUTE OF TECHNOLOGY   (United States)

^d QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYME INHIBITION; ENZYME KINETICS; ESCHERICHIA COLI; PH EFFECTS; RATE CONSTANTS;

GEL FILTRATION; PHOSPHONOPYRUVATE HYDROLASE; SUPERFAMILY; VORIOVORAX SP.;

ENZYMES;

BACTERIAL ENZYME; DIMER; ENZYME INHIBITOR; HYDROLASE; ISOCITRATE LYASE; MAGNESIUM ION; MONOMER; MUTASE; OXALIC ACID; PHOSPHOENOLPYRUVATE; PHOSPHOENOLPYRUVATE MUTASE; PHOSPHONOPYRUVATE HYDROLASE; PYRUVIC ACID DERIVATIVE; RECOMBINANT ENZYME; SULFOPYRUVATE; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITOR COMPLEX; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GEL FILTRATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN QUATERNARY STRUCTURE; SOIL MICROFLORA; STEADY STATE; STRUCTURE ANALYSIS; VARIOVORAX;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROLASES; ISOCITRATE LYASE; KINETICS; MOLECULAR SEQUENCE DATA; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASES (PHOSPHOMUTASES); PROTEIN STRUCTURE, SECONDARY; PROTEOBACTERIA; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; VARIOVORAX SP. PAL2;

EID: 33749010624     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061208l     Document Type: Article

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