Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases: Binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2:7 å resolution

Journal of Biological Chemistry

Volumn 285, Issue 2, 2010, Pages 1569-1576

  Singh, Amit K ^a   Kumar, Ramasamy P ^a   Pandey, Nisha ^a   Sinha, Nagendra ^a   Sinha, Mau ^a   Bhushan, Asha ^a   Kaur, Punit ^a   Sharma, Sujata ^a   Singh, Tej P ^a  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROPERTIES; BINDING STUDIES; CATALASE-PEROXIDASE; DISSOCIATION CONSTANT; ENZYME ASSAYS; HEME PEROXIDASE; HYDROPHOBIC INTERACTIONS; ISONICOTINOYL RADICAL; LACTOPEROXIDASE; MODE OF BINDING; MYCOBACTERIUM TUBERCULOSIS; NITROGEN FORM; PRODRUGS; PROTEIN SURFACE; PYRROLE RING; STRUCTURE DETERMINATION; SUBSTRATE-BINDING SITES; WATER MOLECULE;

ATOMS; BINDING ENERGY; COMPLEXATION; DISSOCIATION; HEMOGLOBIN; HYDRAZINE; HYDROGEN; HYDROGEN BONDS; HYDROPHOBICITY; MAMMALS; PLANTS (BOTANY); PORPHYRINS;

CRYSTAL STRUCTURE;

ARGININE; CARBON; CATALASE PEROXIDASE; GLUTAMIC ACID; GLYCINE; HEME; HEME PEROXIDASE; HISTIDINE; HYDROGEN; HYDROGEN PEROXIDE; IRON; ISONIAZID; LACTOPEROXIDASE; NITROBLUE TETRAZOLIUM; NITROGEN; PEROXIDASE; PHENYLALANINE; PYRROLE; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING SITE; CHEMICAL INTERACTION; CONTROLLED STUDY; COW; CRYSTAL STRUCTURE; DIFFUSION; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROPHOBICITY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ANTITUBERCULAR AGENTS; BACTERIAL PROTEINS; BINDING SITES; CATTLE; HEME; HYDROGEN BONDING; HYDROPHOBICITY; ISONIAZID; LACTOPEROXIDASE; MYCOBACTERIUM TUBERCULOSIS; PEROXIDASES; PRODRUGS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

BOVINAE; MAMMALIA; MYCOBACTERIUM TUBERCULOSIS;

EID: 74049108181     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.060327     Document Type: Article

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