Streptopain

Streptopain (EC 3.4.22.10, Streptococcus peptidase A, streptococcal cysteine proteinase, Streptococcus protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Preferential cleavage with hydrophobic residues at P2, P1 and P1'
Streptopain
Identifiers
EC no.3.4.22.10
CAS no.9025-51-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
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NCBIproteins

This enzyme is isolated from the bacterium, group A Streptococcus.

References

  1. Elliott SD, Liu TY (1970). "Streptococcal proteinase". Methods Enzymol. 19: 252–261. doi:10.1016/0076-6879(70)19019-7.
  2. Liu TY, Elliott SD (1971). "Streptococcal proteinase". In Boyer, P.D. (ed.). The Enzymes (3rd ed.). New York: Academic Press. pp. 609–647.
  3. Tai JY, Kortt AA, Liu TY, Elliott SD (April 1976). "Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain". The Journal of Biological Chemistry. 251 (7): 1955–9. PMID 1270417.
  4. Lo SS, Fraser BA, Liu TY (September 1984). "The mixed disulfide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis". The Journal of Biological Chemistry. 259 (17): 11041–5. PMID 6381494.
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