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

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^ 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.

^ 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.

^ 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. S2CID 25238513.

^ 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. S2CID 22847360.

^ 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. 56 (Pt 5): 551–8. doi:10.1107/s0907444900002420. PMID 10771423.

External links

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Aminopeptidase+S at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O
3.4.13	Dipeptidase 1 2 3
3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II
3.4.15	Angiotensin-converting enzyme
3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase
3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II
Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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