Biology:Aminopeptidase S

From HandWiki
Short description: Class of enzymes
Aminopeptidase S
Identifiers
EC number3.4.11.24
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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. "Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme". European Journal of Biochemistry 183 (2): 471–7. August 1989. doi:10.1111/j.1432-1033.1989.tb14952.x. PMID 2503378. 
  2. "Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution". European Journal of Biochemistry 212 (1): 107–12. February 1993. doi:10.1111/j.1432-1033.1993.tb17639.x. PMID 8444149. 
  3. "Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica". Applied Microbiology and Biotechnology 70 (5): 541–7. May 2006. doi:10.1007/s00253-005-0105-8. PMID 16080009. 
  4. "Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus". FEBS Letters 571 (1–3): 192–6. July 2004. doi:10.1016/j.febslet.2004.07.001. PMID 15280041. 
  5. "Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 A resolution". Acta Crystallographica Section D 56 (Pt 5): 551–8. May 2000. doi:10.1107/s0907444900002420. PMID 10771423. 

External links