Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation

Journal of Biological Chemistry

Volumn 284, Issue 25, 2009, Pages 17216-17226

  Podzelinska, Kateryna ^a   He, Shu Mei ^a   Wathier, Matthew ^a   Yakunin, Alexander ^b   Proudfoot, Michael ^b   Hove Jensen, Bjarne ^c   Zechel, David L ^a   Jia, Zongchao ^a  

^a QUEEN S UNIVERSITY   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; CYCLIC NUCLEOTIDE; ENDONUCLEASES; HISTIDINE RESIDUES; HYDROLASE; INORGANIC PHOSPHATES; LACTAMASE; ORGANOPHOSPHONATES; PHOSPHODIESTERASE; PHOSPHODIESTERASE ACTIVITY; PHOSPHONATE; SEQUENCE HOMOLOGY; STRUCTURAL MOTIFS; THREE-DIMENSIONAL STRUCTURE;

BINDING ENERGY; BINDING SITES; CATALYSTS; ENZYME ACTIVITY; ENZYMES; MANGANESE; MANGANESE COMPOUNDS; METAL IONS; NUCLEIC ACIDS; NUCLEOTIDES; PHOSPHORUS; PHOTODEGRADATION; RNA; X RAY CRYSTALLOGRAPHY; ZINC;

SUBSTRATES;

2',3' CYCLIC NUCLEOTIDE; 4 NITROPHENYLPHOSPHATASE; CARBON PHOSPHORUS LYASE; CYCLIC NUCLEOTIDE; CYSTEINE; ENDONUCLEASE; HISTIDINE; LYASE; MANGANESE; METAL ION; NITROGEN; PROTEIN PHNP; PYRROLOQUINOLINEQUINONE; TRANSFER RNA; TRNASE Z ENDONUCLEASE; UNCLASSIFIED DRUG; ZINC ION;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PRIORITY JOURNAL; PROTEIN DEGRADATION; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; LYASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PHOSPHONIC ACIDS; PHOSPHORIC DIESTER HYDROLASES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; ZINC;

EID: 67650523967     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M808392200     Document Type: Article

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