Serin protease
| Serine endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Struktur kristal kimotripsin sapi. 1CBW. | |||||||||
| Pengidentifikasi | |||||||||
| Nomor EC | 3.4.21.- | ||||||||
| Basis data | |||||||||
| IntEnz | tinjauan IntEnz | ||||||||
| BRENDA | entri BRENDA | ||||||||
| ExPASy | tinjauan NiceZyme | ||||||||
| KEGG | entri KEGG | ||||||||
| MetaCyc | jalur metabolik | ||||||||
| PRIAM | profil | ||||||||
| Struktur PDB | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Serin protease (atau serin endopeptidase) kelompok enzim-enzim yang membelah ikatan peptida pada protein. Serin berperan sebagai asam amino nukleofilik.[1] Serin protease ditemukan dalam jumlah yang cukup baik pada organisme eukariota maupun prokariota. Serin protease terdiri atas dua kategori besar berdasarkan strukturnya yaitu struktur seperti kimotripsin (seperti tripsin) atau seperti subtilisin[2]
Klasifikasi
Sistem klasifikasi protease MEROPS memiliki 16 superfamili (tahun 2013) yang tiap superfamili terdiri dari banyak famili. Setiap superfamili menggunakan dyad dalam ikatan protein yang berbeda sehingga menyebabkan evolusi konvergen mekanisme katalitik.
Untuk superfamili P terdiri dari gabungan kelas famili nukleofil campuran. Superfamili S adalah serin protease murni.
| Protein superfamili | Famili | Contoh |
|---|---|---|
| SB | S8, S53 | Subtilisin (Bacillus licheniformis) |
| SC | S9, S10, S15, S28, S33, S37 | Prolil oligopeptidase (Sus scrofa) |
| SE | S11, S12, S13 | D-Ala-D-Ala peptidase C (Escherichia coli) |
| SF | S24, S26 | Signal peptidase I (Escherichia coli) |
| SH | S21, S73, S77, S78, S80 | Sitomegalovirus (herpesvirus 5) |
| SJ | S16, S50, S69 | Lon-A peptidase (Escherichia coli) |
| SK | S14, S41, S49 | Clp protease (Escherichia coli) |
| SO | S74 | K1F endosialidase CIMCD (Enterobacteria phage K1F) |
| SP | S59 | Nucleoporin 145 (Homo sapiens) |
| SR | S60 | Lactoferin (Homo sapiens) |
| SS | S66 | Murein tetrapeptidase LD-karboksipeptidase (Pseudomonas aeruginosa) |
| ST | S54 | Rhomboid-1 (Drosophila melanogaster) |
| PA | S1, S3, S6, S7, S29, S30, S31, S32, S39, S46, S55, S64, S65, S75 |
Kimotripsin A (Bos taurus) |
| PB | S45, S63 | Penicillin G asilase precursor (Escherichia coli) |
| PC | S51 | Dipeptidase E (Escherichia coli) |
| PE | P1 | DmpA aminopeptidase (Ochrobactrum anthropi) |
| None | S48, S62, S68, S71, S72, S79, S81 |
Referensi
- ^ Hedstrom, L. (Dec 2002). "Serine protease mechanism and specificity". Chem Rev. 102 (12): 4501–24. doi:10.1021/cr000033x. PMID 12475199.
- ^ Madala PK, Tyndall JD, Nall T, Fairlie DP (Jun 2010). "Update 1 of: Proteases universally recognize beta strands in their active sites". Chem Rev. 110 (6): PR1–31. doi:10.1021/cr900368a. PMID 20377171.
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