Sedolisin

The sedolisin (MEROPS S53) family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.[1]

S8/S53 domain
Structure of pseudomonalisin (PDB: 1GA6​)
Identifiers
SymbolPeptidase_S8
PfamPF00082
InterProIPR000209
PROSITEPDOC00125
CATH1GA6
SCOP21GA6 / SCOPe / SUPFAM
CDDcd07477

Their optimal pH is around 3. Most members of the family are produced as a precursor protein with N-terminal (InterPro: IPR015366) and sometimes C-terminal peptides that need to be cleaved off.[2]

Family members

Sedolisin
Sedolisin
Identifiers
EC number3.4.21.100
CAS number848318-58-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Sedolisin (P42790, pseudomonapepsin, sedolysin) is a serine protease. It is secreted by Pseudomonas sp. 101. It performs hydrolysis of the B chain of insulin at -Glu13-Ala-, -Leu15-Tyr- and -Phe25-Tyr-, and angiotensin I at -Tyr4-Ile-. A good synthetic substrate is Lys-Pro-Ile-Glu-Phe-Phe(NO2)-Arg-Leu.[3][4][5][6]

Xanthomonalisin
Xanthomonalisin
Identifiers
EC number3.4.21.101
CAS number113356-29-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Xanthomonalisin (Q60106) is found in Xanthomonas bacteria. It cleaves caesin and clots milk.[7][8]

Physarolisin
Physarolisin
Identifiers
EC number3.4.21.103
CAS number94949-28-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Physarolisin (Q8MZS4, physaropepsin) is a milk-clotting enzyme. It shows preferential cleavage of Gly8-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-Gly and Phe24-Phe.[9][10][11][12][13]

It is special in that it is cold-adapted. It was discovered in the slime mold Physarum flavicomum. Similar proteins (InterPro: IPR017001) are also found in archaea.[14]

References
  1. "Family S53: Summary". MEROPS - the Peptidase Database.
  2. Oda, K (January 2012). "New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases". Journal of Biochemistry. 151 (1): 13–25. doi:10.1093/jb/mvr129. PMID 22016395.
  3. Oda K, Sugitani M, Fukuhara K, Murao S (March 1987). "Purification and properties of a pepstatin-insensitive carboxyl proteinase from a gram-negative bacterium". Biochimica et Biophysica Acta (BBA) - General Subjects. 923 (3): 463–9. doi:10.1016/0304-4165(87)90055-9. PMID 3548827.
  4. Oda K, Nakatani H, Dunn BM (April 1992). "Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1120 (2): 208–14. doi:10.1016/0167-4838(92)90272-f. PMID 1562589.
  5. Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K (May 2001). "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes". Nature Structural Biology. 8 (5): 442–6. doi:10.1038/87610. PMID 11323721.
  6. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases" (PDF). Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
  7. Oda K, Nakazima T, Terashita T, Suzuki KI, Murao S (1987). "Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium". Agric. Biol. Chem. 51 (11): 3073–3080. doi:10.1271/bbb1961.51.3073.
  8. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases" (PDF). Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
  9. Henney HR, Tavana G (1982). "Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum". Exp. Mycol. 6: 161–170. doi:10.1016/0147-5975(82)90090-1.
  10. Murakami-Murofushi K, Hiratsuka A, Ohta J (1984). "A novel acid protease from haploid amoebae of Physarum polycephalum, and its changes during mating and subsequent differentiation into diploid plasmodia". Cell Struct. Funct. 9 (3): 311–315. doi:10.1247/csf.9.311.
  11. North MJ, Whyte A (1984). "Purification and characterization of two acid proteinases from Dictyostelium discoideum". J. Gen. Microbiol. 130: 123–134. doi:10.1099/00221287-130-1-123.
  12. Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K (2003). "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases" (PDF). Acta Biochimica Polonica. 50 (1): 81–102. doi:10.18388/abp.2003_3716. PMID 12673349.
  13. Nishii W, Ueki T, Miyashita R, Kojima M, Kim YT, Sasaki N, Murakami-Murofushi K, Takahashi K (February 2003). "Structural and enzymatic characterization of physarolisin (formerly physaropepsin) proves that it is a unique serine-carboxyl proteinase". Biochemical and Biophysical Research Communications. 301 (4): 1023–9. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815.
  14. Nishii, W; Kuriyama, H; Takahashi, K (10 July 2003). "The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II". FEBS Letters. 546 (2–3): 340–4. doi:10.1016/S0014-5793(03)00621-5. PMID 12832065.
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