Aminopeptidase S

Aminopeptidase S
Identifiers
EC number 3.4.11.24
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Aminopeptidase S (EC 3.4.11.24, Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues

This enzyme contains two zinc molecules in its active site and is activated by Ca2+.

References

  1. ↑ Spungin A, Blumberg S (August 1989). "Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme". European Journal of Biochemistry. 183 (2): 471–7. doi:10.1111/j.1432-1033.1989.tb14952.x. PMID 2503378.
  2. ↑ Ben-Meir D, Spungin A, Ashkenazi R, Blumberg S (February 1993). "Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution". European Journal of Biochemistry. 212 (1): 107–12. doi:10.1111/j.1432-1033.1993.tb17639.x. PMID 8444149.
  3. ↑ Arima J, Uesugi Y, Iwabuchi M, Hatanaka T (May 2006). "Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica". Applied Microbiology and Biotechnology. 70 (5): 541–7. doi:10.1007/s00253-005-0105-8. PMID 16080009.
  4. ↑ Fundoiano-Hershcovitz Y, Rabinovitch L, Langut Y, Reiland V, Shoham G, Shoham Y (July 2004). "Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus". FEBS Letters. 571 (1–3): 192–6. doi:10.1016/j.febslet.2004.07.001. PMID 15280041.
  5. ↑ Gilboa R, Greenblatt HM, Perach M, Spungin-Bialik A, Lessel U, Wohlfahrt G, Schomburg D, Blumberg S, Shoham G (May 2000). "Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 A resolution". Acta Crystallographica. Section D, Biological Crystallography. 56 (Pt 5): 551–8. doi:10.1107/s0907444900002420. PMID 10771423.
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