From Wikipedia, the free encyclopedia
Lactoperoxidase is a peroxidase enzyme found in milk. This enzyme has antimicrobial and antioxidant properties. It is able to form reactive bromine and iodine species, resulting in natural organobromine and organoiodine substances, and can therefore be categorised as a haloperoxidase. It is fairly heat resistant and was widely used as an indicator of overpasteurization of milk.
[edit] Structure
Freshly isolated and purified samples of goat lactoperioxidase (LPO) were saturated with ammonium iodide and crystallized using 20% polyethylene glycol 3350 in a hanging drop vapor diffusion setup. The structure has been determined using X-ray crystallographic method. Goat LPO consists of a single polypeptide chain of 595 amino acid residues and folds into an oval-shaped structure. The structure contains 20 well-defined alpha-helices of varying lengths including a helix, H(2a), unique to LPO, and two short antiparallel beta-strands.
[edit] References
- ^ PDB 2r5l; Singh, A.K., Singh, N., Sharma, S., Kaur, P., Srinivasan, A., Singh, T.P. (September 2007). "Crystal structure of lactoperoxidase at 2.4A resolution". J. Mol. Biol. 376 (1): 1060–1075. doi:10.2210/pdb2r5l/pdb. PMID 18191143.
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