Streptopain

Streptopain
Identifiers
EC number 3.4.22.10
CAS number 9025-51-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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'

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

References

  1. Elliott, S.D.; Liu, T.-Y. (1970). "Streptococcal proteinase". Methods Enzymol. 19: 252–261. doi:10.1016/0076-6879(70)19019-7.
  2. Liu, T.-Y.; Elliott, S.D. (1971). "Streptococcal proteinase". In Boyer, P.D. The Enzymes (3rd ed.). New York: Academic Press. pp. 609–647.
  3. Tai, J. (1976). "Y., Kortt, A.A., Liu, T.-Y. and Elliott, S.D. Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain". J. Biol. Chem. 251: 1955–1959. PMID 1270417.
  4. Lo, S.-S.; Fraser, B.A.; Liu, T.-Y. (1984). "The mixed disulphide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis". J. Biol. Chem. 259: 11041–11045. PMID 6381494.
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