Divergence of chemical function in the alkaline phosphatase superfamily: Structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase

Biochemistry

Volumn 50, Issue 17, 2011, Pages 3481-3494

  Kim, Alexander ^a   Benning, Matthew M ^b   OkLee, Sang ^a   Quinn, John ^c   Martin, Brian M ^d   Holden, Hazel M ^b   Dunaway Mariano, Debra ^a  

^a UNIVERSITY OF NEW MEXICO   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

^d MSC 1262   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; ALKALINE PHOSPHATASE; BACTERIAL SPECIES; BOND-CLEAVING; CARBON ATOMS; CATALYTIC MECHANISMS; CATALYTIC NUCLEOPHILES; CHEMICAL FUNCTIONS; DEGRADATION PATHWAYS; DIANIONS; ENZYME SUPERFAMILIES; ION SPECIFICITY; LABELING STRATEGY; LEAVING GROUPS; METALLOENZYMES; NATURAL PRODUCTS; ORGANOPHOSPHATE ESTERS; PHOSPHONATES; PHOSPHORUS ATOM; PHOSPHORYL GROUPS; PROTEOBACTERIA; SITE DIRECTED MUTAGENESIS; SITE-DIRECTED MUTATION; X-RAY STRUCTURE; ZINC IONS;

ALKALINITY; BACTERIA; BACTERIOLOGY; BIOINFORMATICS; CARBOXYLATION; ENZYMES; ESTERS; GENES; METAL IONS; NUCLEOPHILES; PHOSPHATASES; PHOSPHORUS; STABILIZATION; ZINC;

HYDROLASES;

ALKALINE PHOSPHATASE; HYDROLASE; NUCLEOTIDE PYROPHOSPHATASE; PHOSPHONOACETIC ACID HYDROLASE; UNCLASSIFIED DRUG;

ARTICLE; BIODEGRADATION; BIOINFORMATICS; BIOSYNTHESIS; CATALYSIS; CHEMICAL BOND; COMPLEX FORMATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEOBACTERIA; SITE DIRECTED MUTAGENESIS;

ALKALINE PHOSPHATASE; BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; CATIONS, DIVALENT; CRYSTALLOGRAPHY, X-RAY; FOSCARNET; HYDROGEN-ION CONCENTRATION; METALS, HEAVY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEOBACTERIA; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); PROTEOBACTERIA;

EID: 79955411030     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200165h     Document Type: Article

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