Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme

Journal of Biological Chemistry

Volumn 286, Issue 42, 2011, Pages 37011-37022

  Dhindwal, Sonali ^a   Patil, Dipak N ^a   Mohammadi, Mahmood ^b   Sylvestre, Michel ^b   Tomar, Shailly ^a   Kumar, Pravindra ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY ROORKEE   (India)

^b INRS INSTITUT ARMAND FRAPPIER   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

APO-STATE; BINARY COMPLEXES; BIOCHEMICAL DATA; BIOCHEMICAL STUDIES; CATABOLIC PATHWAY; CONFORMATION CHANGE; CONFORMATIONAL CHANGE; INTERMEDIATE STATE; LIGAND BINDING; LOOP STRUCTURE; MOLECULAR BASIS; MOLECULAR DOCKING; REDUCTASE ENZYMES; SUBSTRATE BINDING; SUBSTRATE SPECIFICITY; TERNARY COMPLEX; TERNARY STRUCTURE;

CRYSTAL STRUCTURE; ENZYMES; LIGANDS; METABOLISM; METABOLITES;

SUBSTRATES;

2,4,4' TRICHLOROBIPHENYL DERIVATIVE; 2,6 DICHLOROBIPHENYL DERIVATIVE; 3,3' DICHLOROBIPHENYL DERIVATIVE; ACYL COENZYME A DEHYDROGENASE; APOENZYME; BACTERIAL ENZYME; BIPHENYL DEHYDROGENASE; BIPHENYL DERIVATIVE; META CHLOROBIPHENYL DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE 2,3 DIHYDROXYBIPHENYL; NICOTINAMIDE ADENINE DINUCLEOTIDE 4,4' DIHYDROXYBIPHENYL; ORTHO CHLOROBIPHENYL DERIVATIVE; PARA CHLOROBIPHENYL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BIOCHEMISTRY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GRAM NEGATIVE BACTERIUM; LIGAND BINDING; MOLECULAR BIOLOGY; MOLECULAR DOCKING; NONHUMAN; PANDORAEA PNOMENUSA; PRIORITY JOURNAL;

BACTERIAL PROTEINS; BURKHOLDERIACEAE; CHLOROPHENOLS; CRYSTALLOGRAPHY, X-RAY; LIGANDS; OXIDOREDUCTASES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

PANDORAEA PNOMENUSA;

EID: 80054688021     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.291013     Document Type: Article

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