Lactoperoxidase

From Proteopedia

Function Lactoperoxidase (LPO) catalyzes the oxidation of thiocyanate, bromide and iodide using hydrogen peroxide. LPO is the second most abundant enzyme in milk. Heme is the cofactor of LPO. LPO contains a strongly-chelated calcium ion[1]. Relevance The short-lived oxidized intermediates of the LPO reaction serve as potent bactericidal agents[2]. LPO is used as an antimicrobial agent in milk and its products, in cosmetics, toothpaste and ophthalmic solutions. Structural highlights The peroxidation of thiocyanate catalyzed by LPO occurs at the heme cavity site[3]. Water molecules shown as red spheres. Whole active site.

spinqualitylabelsall models Glycosylated bovine lactoferrin containing heme complex with thiocyanate, I- (purple) and Ca+2 (green) ions (PDB entry 3eri) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of lactoperoxidase

Updated on 26-March-2024

Lactoperoxidase binary complex

2pt3 - bPLO + phosphate - bovine

2nqx, 5b72 – bPLO + I

7dlq – bPLO + H2O2

2r5l – gLPO + I – goat

3nak – gLPO + formate

6ky7, 7c73, 7c74, 7c75, 7d52, 7dao, 7de5, 7dmr – yPLO + Ca - yak

7c74 - yLPO + Cl

6l32, 6l42, 7d52, 6l5g, 7c75 - yLPO + Zn

6lqw, 7y3u – yPLO + H2O2

7c73 – yPLO + phosphoserine

Lactoperoxidase ternary complex

2ips, 3eri, 3gc1, 6a4y, 6lco, 6m7e, 7dn7 – bLPO + SCN + I

2qrb – bLPO + SCN + Cl

3bxi – bLPO + SCN + nitrate

4pnx - bPLO + bromomethane + I

2pum – bPLO + catechol + I

3krq – bLPO + amino-triazole + I

6kmk – bPLO + H2O2 + phosphoserine

7dlq, 7dn6 – bPLO + H2O2 + I

2z5z – wbPLO + F + I – water buffalo

2o86 – wbPLO + nitrate + I

3erh - wbLPO + SCN + I

7de5 - yLPO + SCN + I

2ojv – gPLO + CN + I

3n8f - gLPO + SCN + nitrate

5ff1 - gLPO + methimazole + nitrate

5hpw - gLPO + propyl-thiouracil + nitrate

3niu – gLPO + diethylene glycol + phosphate

3rke - gPLO + inhibitor + I

2ikc – sLPO + carbonate + formate – sheep

7ve3 - sLPO + hypoiodite + I

Lactoperoxidase quaternary complex

3gcj, 2qpk - bPLO + salicylhydroxamic acid + SCN + I

3gck - bPLO + benzylhydroxamic acid + SCN + I

3uba, 4gm7 - bPLO + hydroxycinnamic acid + SCN + I

3gcl, 2qqt - bPLO + aspirin + SCN + I

3i6n - bPLO + isoniazid + SCN + I

4ksz - bPLO + cystein + SCN + I

5wv3 - bPLO + oxidosulfanyl-methanamine + Br + I

7dlq - bPLO + Br + Cl + SCN + I

7wyj - bPLO + indomethacin + SCN + I

3py4, 6m7e - bPLO + paracetamol + SCN + I

7dn6 - bPLO + phenyliso-SCN + SCN + I

7dn7 - bPLO + nitro-phenoxymethanesulfonanilide+ SCN + I

8y9x, 4njb, 6lco - bPLO + pyridine derivative + SCN + I

3r4x, 5zgs - bPLO + pyrazine derivative + SCN + I

3r5o - bPLO + methoxyphenol + SCN + I

3tgy - bPLO + ascorbate + SCN + I

3v6q - bPLO + CO + SCN + I

6l9t - bLPO + Zn + OSCN + I

5gls - bLPO + butyl-triazole + SCN + I

5gh0 - bLPO + mercaptoimidazole + nitrate + carbonate

2gjm - wbPLO + carbonate + SCN + I

3faq – wbLPO + CN + SCN + I

3fnl - wbPLO + salicylhydroxamic acid + SCN + I

4y55 - wbLPO + rhodanide + SCN + I

2e9e – gPLO + nitrate + carbonate + SCN + CN

2efb – gPLO + phosphate + carbonate + SCN + CN

3qf1 - gPLO + piperazine + SCN + I

8ing - gPLO + acrylonitrile + SCN + I

4msf, 4oek - gPLO + phenol derivative+ SCN + I

2eha – gPLO + formate + carbonate + SCN

3r55, 6lf7 - gPLO + pyrazine derivative + SCN + I

3sxv - gPLO + amitrole + SCN + I

4qjq - gPLO + octopamine + SCN + I

6lf7 - gPLO + hypocyanite + SCN + H2O2 + I

7ve3 - sPLO +tetrahydrofuran + SCN + I

6ky7, 6l2j – yPLO + H2O2 + phosphoserine + SCN + I

References

1. ↑ Gerson C, Sabater J, Scuri M, Torbati A, Coffey R, Abraham JW, Lauredo I, Forteza R, Wanner A, Salathe M, Abraham WM, Conner GE. The lactoperoxidase system functions in bacterial clearance of airways. Am J Respir Cell Mol Biol. 2000 Jun;22(6):665-71. PMID:10837362
2. ↑ Gerson C, Sabater J, Scuri M, Torbati A, Coffey R, Abraham JW, Lauredo I, Forteza R, Wanner A, Salathe M, Abraham WM, Conner GE. The lactoperoxidase system functions in bacterial clearance of airways. Am J Respir Cell Mol Biol. 2000 Jun;22(6):665-71. PMID:10837362
3. ↑ Sheikh IA, Singh AK, Singh N, Sinha M, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S, Singh TP. Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution. J Biol Chem. 2009 May 29;284(22):14849-56. Epub 2009 Apr 1. PMID:19339248 doi:10.1074/jbc.M807644200