| Aminopeptidase S | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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+.
- ^ 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.
- Aminopeptidase+S at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Aminopeptidase S | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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+.
- ^ 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.
- Aminopeptidase+S at the U.S. National Library of Medicine Medical Subject Headings (MeSH)