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A p p e a r a n c e
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A p p e a r a n c e
F r o m W i k i p e d i a , t h e f r e e e n c y c l o p e d i a
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 .[1] [2] [3] [4] [5] [6] 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
[ edit ]
^ 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
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t
e
Activity
Regulation
Classification
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Types
R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Aminopeptidase_B&oldid=1172339831 "
C a t e g o r y :
● E C 3 . 4 . 1 1
H i d d e n c a t e g o r i e s :
● A r t i c l e s w i t h s h o r t d e s c r i p t i o n
● S h o r t d e s c r i p t i o n m a t c h e s W i k i d a t a
● T h i s p a g e w a s l a s t e d i t e d o n 2 6 A u g u s t 2 0 2 3 , a t 1 3 : 0 8 ( U T C ) .
● T e x t i s a v a i l a b l e u n d e r t h e C r e a t i v e C o m m o n s A t t r i b u t i o n - S h a r e A l i k e L i c e n s e 4 . 0 ;
a d d i t i o n a l t e r m s m a y a p p l y . B y u s i n g t h i s s i t e , y o u a g r e e t o t h e T e r m s o f U s e a n d P r i v a c y P o l i c y . W i k i p e d i a ® i s a r e g i s t e r e d t r a d e m a r k o f t h e W i k i m e d i a F o u n d a t i o n , I n c . , a n o n - p r o f i t o r g a n i z a t i o n .
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