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Sedolisin

May 18, 2024

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
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 edit

Sedolisin edit

Sedolisin
Identifiers
EC no.3.4.21.100
CAS no.848318-58-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 edit

Xanthomonalisin
Identifiers
EC no.3.4.21.101
CAS no.113356-29-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

Physarolisin edit

Physarolisin
Identifiers
EC no.3.4.21.103
CAS no.94949-28-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 edit

  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): 463–469. 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): 208–214. doi:10.1016/0167-4838(92)90272-f. PMID 1562589.
  5. ^ Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, et al. (May 2001). "Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes". Nature Structural Biology. 8 (5): 442–446. doi:10.1038/87610. PMID 11323721. S2CID 16793101.
  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". 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". 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". 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, et al. (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): 1023–1029. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815.
  14. ^ Nishii W, Kuriyama H, Takahashi K (July 2003). "The Physarum polycephalum php gene encodes a unique cold-adapted serine-carboxyl peptidase, physarolisin II". FEBS Letters. 546 (2–3): 340–344. doi:10.1016/S0014-5793(03)00621-5. PMID 12832065. S2CID 19197020.

External links edit

May 18, 2024
sedolisin, sedolisin, merops, family, peptidases, family, serine, proteases, structurally, related, subtilisin, family, well, known, members, this, family, include, sedolisin, pseudomonalisin, found, pseudomonas, bacteria, xanthomonalisin, sedolisin, physaroli. 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 domainStructure of pseudomonalisin PDB 1GA6 IdentifiersSymbolPeptidase S8PfamPF00082InterProIPR000209PROSITEPDOC00125CATH1GA6SCOP21GA6 SCOPe SUPFAMCDDcd07477Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary 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 Contents 1 Family members 1 1 Sedolisin 1 2 Xanthomonalisin 1 3 Physarolisin 2 References 3 External linksFamily members editSedolisin edit SedolisinIdentifiersEC no 3 4 21 100CAS no 848318 58 1DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 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 edit XanthomonalisinIdentifiersEC no 3 4 21 101CAS no 113356 29 9DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Xanthomonalisin Q60106 is found in Xanthomonas bacteria It cleaves caesin and clots milk 7 8 Physarolisin edit PhysarolisinIdentifiersEC no 3 4 21 103CAS no 94949 28 7DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 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 edit Family S53 Summary MEROPS the Peptidase Database 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 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 3 463 469 doi 10 1016 0304 4165 87 90055 9 PMID 3548827 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 2 208 214 doi 10 1016 0167 4838 92 90272 f PMID 1562589 Wlodawer A Li M Dauter Z Gustchina A Uchida K Oyama H et al May 2001 Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin like enzymes Nature Structural Biology 8 5 442 446 doi 10 1038 87610 PMID 11323721 S2CID 16793101 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 Acta Biochimica Polonica 50 1 81 102 doi 10 18388 abp 2003 3716 PMID 12673349 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 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 Acta Biochimica Polonica 50 1 81 102 doi 10 18388 abp 2003 3716 PMID 12673349 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 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 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 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 Acta Biochimica Polonica 50 1 81 102 doi 10 18388 abp 2003 3716 PMID 12673349 Nishii W Ueki T Miyashita R Kojima M Kim YT Sasaki N et al 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 1029 doi 10 1016 s0006 291x 03 00083 4 PMID 12589815 Nishii W Kuriyama H Takahashi K July 2003 The Physarum polycephalum php gene encodes a unique cold adapted serine carboxyl peptidase physarolisin II FEBS Letters 546 2 3 340 344 doi 10 1016 S0014 5793 03 00621 5 PMID 12832065 S2CID 19197020 External links editSedolisin at the U S National Library of Medicine Medical Subject Headings MeSH Physarolisin at the U S National Library of Medicine Medical Subject Headings MeSH Xanthomonalisin at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Sedolisin amp oldid 1172360585, wikipedia, wiki, book, books, library,

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