| Animal heme-dependent peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of the human myeloperoxidase-thiocyanate complex.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | An_peroxidase | ||||||||
| Pfam | PF03098 | ||||||||
| InterPro | IPR019791 | ||||||||
| PROSITE | PDOC00394 | ||||||||
| SCOP2 | 1mhl / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 36 | ||||||||
| OPM protein | 1q4g | ||||||||
| CDD | cd05396 | ||||||||
| |||||||||
Animal heme-dependent peroxidases is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin.[2][3][4]
- ^ PDB: 1dnu; Blair-Johnson M, Fiedler T, Fenna R (November 2001). "Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution". Biochemistry. 40 (46): 13990–7. doi:10.1021/bi0111808. PMID 11705390.
- ^ Nelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, Olson PF, Parker CG, Fessler JH (1994). "Peroxidasin: a novel enzyme-matrix protein of Drosophila development". EMBO J. 13 (15): 3438–3447. doi:10.1002/j.1460-2075.1994.tb06649.x. PMC 395246. PMID 8062820.
- ^ Poulos TL, Li H (1994). "Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures". Structure. 2 (6): 461–464. doi:10.1016/S0969-2126(00)00046-0. PMID 7922023.
- ^ Kimura S, Ikeda-Saito M (1988). "Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family". Proteins. 3 (2): 113–120. doi:10.1002/prot.340030206. PMID 2840655. S2CID 29575992.