Aminopeptidase B - Misplaced Pages

Aminopeptidase B (EC 3.4.11.6, arylamidase II, arginine aminopeptidase, arginyl aminopeptidase, Cl—activated arginine aminopeptidase, cytosol aminopeptidase IV, L-arginine aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction

Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys

This enzyme from mammalian tissues is activated by chloride ions and low concentrations of thiol compounds.

An inhibitor is bestatin (ubenimex).

References

Gainer H, Russell JT, Loh YP (September 1984). "An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65". FEBS Letters. 175 (1): 135–9. doi:10.1016/0014-5793(84)80586-4. PMID 6434344.
Belhacene N, Mari B, Rossi B, Auberger P (August 1993). "Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation". European Journal of Immunology. 23 (8): 1948–55. doi:10.1002/eji.1830230833. PMID 8344358. S2CID 855382.
Cadel S, Pierotti AR, Foulon T, Créminon C, Barré N, Segrétain D, Cohen P (April 1995). "Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules". Molecular and Cellular Endocrinology. 110 (1–2): 149–60. doi:10.1016/0303-7207(95)03529-g. PMID 7672445. S2CID 6951437.
Fukasawa KM, Fukasawa K, Kanai M, Fujii S, Harada M (November 1996). "Molecular cloning and expression of rat liver aminopeptidase B". The Journal of Biological Chemistry. 271 (48): 30731–5. doi:10.1074/jbc.271.48.30731. PMID 8940051.
Cadel S, Foulon T, Viron A, Balogh A, Midol-Monnet S, Noël N, Cohen P (April 1997). "Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase". Proceedings of the National Academy of Sciences of the United States of America. 94 (7): 2963–8. Bibcode:1997PNAS...94.2963C. doi:10.1073/pnas.94.7.2963. PMC 20305. PMID 9096329.
Orning L, Gierse JK, Fitzpatrick FA (April 1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity". The Journal of Biological Chemistry. 269 (15): 11269–73. doi:10.1016/S0021-9258(19)78120-4. PMID 8157657.

External links

Aminopeptidase+B 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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Biology

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EC 3.4.11