Binding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACID

The binding and structural studies of bovine lactoperoxidase with three aromatic ligands, acetylsalicylic acid (ASA), salicylhydoxamic acid (SHA), and benzylhydroxamic acid (BHA) show that all the three compounds bind to lactoperoxidase at the substrate binding site on the distal heme side. The bind...

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Autores principales: Singh, Amit K., Singh, Nagendra, Sinha, Mau, Bhushan, Asha, Kaur, Punit, Srinivasan, Alagiri, Sharma, Sujata, Singh, Tej P.
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2009
Materias:
Enzyme Catalysis and Regulation
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC2740456/
https://ncbi.nlm.nih.gov/pubmed/19465478
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.010280
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