Arginyl aminopeptidase
| Aminopeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifier | |||||||||
| EC number | 3.4.11.6 | ||||||||
| CAS registration number | 9073-92-1 | ||||||||
| Database | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structure | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Arginyl aminopeptidase (Arginyl aminopeptidase) or aminopeptidase B(Aminopeptidase B, EC 3.4.11.6) are enzymes [1]; [2] [3] [4] [5] [6]. I catalyze the following chemical reactions.
- P1' rank is isolated from oligopeptide with arginine of the N-terminus and lysine at time except proline. In addition, I act on arginine of allyl amide and lysine.
This enzyme derived from a mammalian organization is activated by a chloride ion and a low-concentrated thiol compound.
Source
- ^ Gainer, H., Russell, J.T. and Loh, Y.P. (1984). "An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine fromβ-lipotropin(60-65)." FEBS Lett. 175 (1): 135-139. doi: 10.1016/0014-5793(84) 80,586-4. PMID 6434344.
- ^ Belhacène, N., Mari, B., Rossi, B. and Auberger, P. (1993). "Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation." Eur. J. Immunol. 23: 1948-1955. doi: 10.1002/eji.1830230833. PMID 8344358.
- ^ Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D. and Cohen, P. (1995). "Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules." Mol. Cell. Endocrinol. 110 (1-2): 149-160. doi: 10.1016/0303-7207(95)03529-g. PMID 7672445.
- ^ Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S. and Harada, M. (1996). "Molecular cloning and expression of rat liver aminopeptidase B." J. Biol. Chem. 271 (48): 30731-30735. doi: 10.1074/jbc.271.48.30731. PMID 8940051.
- ^ Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N. and Cohen, P. (1997). "Aminopeptidase B from the rat testis is a bifunctional enzyme structually related to leukotriene-A4 hydrolase." Proc. Natl. Acad. Sci. USA 94 (7): 2963-2968. doi: 10.1073/pnas.94.7.2963. PMID 9096329.
- ^ Orning, L., Gierse, J.K. and Fitzpatrick, F.A. (1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity." J. Biol. Chem. 269 (15): 11,269-11,267. PMID 8157657.
Outside link
- Aminopeptidase B - the US National Library of Medicine Medical Subject Headings (MeSH)
This article is taken from the Japanese Wikipedia Arginyl aminopeptidase
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