KEGG   ENZYME: 3.4.11.6Help
Entry
EC 3.4.11.6                 Enzyme                                 

Name
aminopeptidase B;
arylamidase II;
arginine aminopeptidase;
arginyl aminopeptidase;
Cl--activated arginine aminopeptidase;
cytosol aminopeptidase IV;
L-arginine aminopeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aminopeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Comment
Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family) [4,5].
History
EC 3.4.11.6 created 1972, modified 1997
Orthology
K01260  
aminopeptidase B
Genes
HSA: 
6051(RNPEP)
PTR: 
469638(RNPEP)
PPS: 
100974364(RNPEP)
GGO: 
101127560(RNPEP)
PON: 
100456066(RNPEP)
MCC: 
706696(RNPEP)
MCF: 
102146949(RNPEP)
CJC: 
100400846(RNPEP)
MMU: 
215615(Rnpep)
RNO: 
81761(Rnpep)
CGE: 
100755451(Rnpep)
HGL: 
101712935(Rnpep)
TUP: 
102475581(RNPEP)
CFA: 
490236(RNPEP)
AML: 
100471332(RNPEP)
UMR: 
103657779(RNPEP)
FCA: 
101100613(RNPEP)
PTG: 
102952170(RNPEP)
BTA: 
282040(RNPEP)
BOM: 
102286299(RNPEP)
PHD: 
102333014(RNPEP)
CHX: 
102170601(RNPEP)
OAS: 
101114205(RNPEP)
SSC: 
100524577(RNPEP)
CFR: 
102505914(RNPEP)
BACU: 
103013646(RNPEP)
LVE: 
103076101(RNPEP)
ECB: 
100063775(RNPEP)
MYB: 
102246228(RNPEP)
MYD: 
102760506(RNPEP)
MDO: 
100014545(RNPEP)
SHR: 
100923693(RNPEP)
GGA: 
421165(RNPEP)
MGP: 
APLA: 
TGU: 
FAB: 
PHI: 
FPG: 
FCH: 
CLV: 
ASN: 
102369662(RNPEP)
AMJ: 
102562169(RNPEP)
PSS: 
102450932(RNPEP)
CMY: 
102931368(RNPEP)
ACS: 
100554554(rnpep)
PBI: 
103063102(RNPEP)
XLA: 
443974(rnpep-b) 447741(rnpep)
XTR: 
407876(rnpep)
DRE: 
437014(rnpep)
LCM: 
CMK: 
103179129(rnpep)
BFO: 
SPU: 
LGI: 
PIF: 
 » show all
Taxonomy
Reference
1  [PMID:6434344]
  Authors
Gainer H, Russell JT, Loh YP.
  Title
An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65.
  Journal
FEBS. Lett. 175 (1984) 135-9.
Reference
2  [PMID:8344358]
  Authors
Belhacene N, Mari B, Rossi B, Auberger P.
  Title
Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation.
  Journal
Eur. J. Immunol. 23 (1993) 1948-55.
Reference
3  [PMID:7672445]
  Authors
Cadel S, Pierotti AR, Foulon T, Creminon C, Barre N, Segretain D, Cohen P.
  Title
Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules.
  Journal
Mol. Cell. Endocrinol. 110 (1995) 149-60.
Reference
4  [PMID:8940051]
  Authors
Fukasawa KM, Fukasawa K, Kanai M, Fujii S, Harada M.
  Title
Molecular cloning and expression of rat liver aminopeptidase B.
  Journal
J. Biol. Chem. 271 (1996) 30731-5.
  Sequence
[rno:81761]
Reference
5  [PMID:9096329]
  Authors
Cadel S, Foulon T, Viron A, Balogh A, Midol-Monnet S, Noel N, Cohen P.
  Title
Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 2963-8.
  Sequence
[rno:81761]
Reference
6  [PMID:8157657]
  Authors
Orning L, Gierse JK, Fitzpatrick FA.
  Title
The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity.
  Journal
J. Biol. Chem. 269 (1994) 11269-73.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9073-92-1

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