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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Bibliographic Details
Main Authors: Singh, Amit K., Singh, Nagendra, Sinha, Mau, Bhushan, Asha, Kaur, Punit, Srinivasan, Alagiri, Sharma, Sujata, Singh, Tej P.
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2009
Subjects:
Enzyme Catalysis and Regulation
Online Access: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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