Biology:Physarolisin

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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 (EC 3.4.21.103, Dictyostelium discoideum aspartic proteinase, Dictyostelium discoideum aspartic proteinase E, Physarum flavicomum aspartic proteinase, Physarum polycephalum acid proteinase, Physarum aspartic proteinase, physaropepsin) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Milk clotting activity. Preferential cleavage of Gly8-Ser in B chain of insulin most rapidly, followed by Leu11!Val, Cys(SO3H)19-Gly and Phe24-Phe.

This enzyme belongs in peptidase family S53.

References

  1. "Purification and some properties of an intracellular acid (carboxyl) proteinase from differentiating haploid cells of Physarum flavicomum". Exp. Mycol. 6: 161–170. 1982. doi:10.1016/0147-5975(82)90090-1. 
  2. "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: 311–315. 1984. doi:10.1247/csf.9.311. 
  3. "Purification and characterization of two acid proteinases from Dictyostelium discoideum". J. Gen. Microbiol. 130: 123–134. 1984. doi:10.1099/00221287-130-1-123. 
  4. "Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases". Acta Biochimica Polonica 50 (1): 81–102. 2003. PMID 12673349. http://www.actabp.pl/pdf/1_2003/81.pdf. 
  5. "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. February 2003. doi:10.1016/s0006-291x(03)00083-4. PMID 12589815. 

External links