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
K19701  aminopeptidase YwaD
Genes
HSA: 6051(RNPEP)
PTR: 469638(RNPEP)
PPS: 100974364(RNPEP)
GGO: 101127560(RNPEP)
PON: 100456066(RNPEP)
MCC: 706696(RNPEP)
MCF: 102146949(RNPEP)
CSAB: 103230319(RNPEP)
RRO: 104674517(RNPEP)
RBB: 108545095(RNPEP)
CJC: 100400846(RNPEP)
SBQ: 101049218(RNPEP)
MMU: 215615(Rnpep)
RNO: 81761(Rnpep)
CGE: 100755451(Rnpep)
NGI: 103731828(Rnpep)
HGL: 101712935(Rnpep)
CCAN: 109684759(Rnpep)
OCU: 100342982(RNPEP)
TUP: 102475581(RNPEP)
CFA: 490236(RNPEP)
AML: 100471332(RNPEP)
UMR: 103657779(RNPEP)
ORO: 101367496(RNPEP)
FCA: 101100613(RNPEP)
PTG: 102952170(RNPEP)
AJU: 106974256(RNPEP)
BTA: 282040(RNPEP)
BOM: 102286299(RNPEP)
PHD: 102333014(RNPEP)
CHX: 102170601(RNPEP)
OAS: 101114205(RNPEP)
SSC: 100524577(RNPEP)
CFR: 102505914(RNPEP)
CDK: 105103112(RNPEP)
BACU: 103013646(RNPEP)
LVE: 103076101(RNPEP)
OOR: 101290438(RNPEP)
ECB: 100063775(RNPEP)
EPZ: 103567457(RNPEP)
EAI: 106832344(RNPEP)
MYB: 102246228(RNPEP)
MYD: 102760506(RNPEP)
HAI: 109380478(RNPEP)
RSS: 109457769(RNPEP)
LAV: 100673954(RNPEP)
TMU: 101342405
MDO: 100014545(RNPEP)
SHR: 100923693(RNPEP)
OAA: 100093099(RNPEP)
GGA: 421165(RNPEP)
MGP: 100549291(RNPEP)
CJO: 107324639(RNPEP)
APLA: 101802986(RNPEP)
ACYG: 106045854(RNPEP)
TGU: 100224003(RNPEP)
GFR: 102036435(RNPEP)
FAB: 101813510(RNPEP)
PHI: 102112448(RNPEP)
PMAJ: 107214916(RNPEP)
CCW: 104692573(RNPEP)
FPG: 101914529(RNPEP)
FCH: 102048572(RNPEP)
CLV: 102090773(RNPEP)
EGZ: 104122020(RNPEP)
AAM: 106500249(RNPEP)
ASN: 102369662(RNPEP)
AMJ: 102561220(RNPEP)
PSS: 102450932(RNPEP)
CMY: 102931368(RNPEP)
CPIC: 101946561(RNPEP)
ACS: 100554554(rnpep)
PVT: 110073333(RNPEP)
PBI: 103063102(RNPEP)
GJA: 107121706(RNPEP)
XLA: 443974(rnpep.S) 447741(rnpep.L)
XTR: 407876(rnpep)
NPR: 108795716(RNPEP)
DRE: 437014(rnpep)
CCAR: 109098332 109100480(rnpep)
AMEX: 103045130(rnpep)
SASA: 100195514(rnpep)
ELS: 105016934(rnpep)
LCM: 102364673(RNPEP)
CMK: 103179129(rnpep)
SPU: 588993
SKO: 100372225
MYI: 110440307
BSU: BSU38470(ywaD)
BSR: I33_4001
BSL: A7A1_2084
BSH: BSU6051_38470(ywaD)
BSUT: BSUB_04085(ywaD)
BSUL: BSUA_04085(ywaD)
BSUS: Q433_21180
BSS: BSUW23_19060(ywaD)
BST: GYO_4245
BSO: BSNT_10509(ywaD)
BSQ: B657_38470(ywaD)
BSX: C663_3758(ywaD)
BLI: BL03935(ywaD)
BLD: BLi04074(ywaD)
BLH: BaLi_c40830(ywaD)
BAY: RBAM_031250(ywaD)
BAQ: BACAU_3151(ywaD1)
BAMP: B938_16010
BAML: BAM5036_3039(ywaD)
BAMA: RBAU_3260(ywaD)
BAMN: BASU_3041(ywaD)
BAMT: AJ82_17655
BAMY: V529_33860
BAO: BAMF_3251(ywaD)
BAZ: BAMTA208_17260(ywaD)
BQL: LL3_03534(ywaD)
BXH: BAXH7_03525(ywaD)
BAMI: KSO_003505
BAMC: U471_32420
BAMF: U722_16775
BHA: BH3861
BAN: BA_5606
BAR: GBAA_5606
BAT: BAS5208
BAI: BAA_5632
BANT: A16_56160
BANR: A16R_56850
BANS: BAPAT_5374
BANV: DJ46_4254
BCE: BC5359
BCA: BCE_5488
BCQ: BCQ_5199
BCX: BCA_5508
BNC: BCN_5287
BCF: bcf_26900
BCER: BCK_08560
BTL: BALH_4856
BTT: HD73_5768
BTHI: BTK_28440
BTM: MC28_4594
BTG: BTB_c55600(ywaD)
BTW: BF38_1082
BWW: bwei_4420(ywaD)
BMYO: BG05_646
BMYC: DJ92_2450(ywaD)
BMQ: BMQ_2033(ywaD)
BMD: BMD_1989(ywaD)
BMH: BMWSH_3244(ywaD)
BMEG: BG04_4334(amp)
BJS: MY9_3952
BACP: SB24_13125
BACY: QF06_17685
BACL: BS34A_41670(ywaD)
BALM: BsLM_3881
BEO: BEH_16595
BGY: BGLY_4528(ywaD)
JEO: JMA_03500
BPRS: CK3_26930
ACTI: UA75_21805
ACAD: UA74_21325
AHG: AHOG_18820(ywaD)
DMC: btf_974
ABAC: LuPra_01172(ywaD_1)
CHZ: CHSO_2503
LOKI: Lokiarch_24450(ywaD_3)
 » 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 175:135-9 (1984)
DOI:10.1016/0014-5793(84)80586-4
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 23:1948-55 (1993)
DOI:10.1002/eji.1830230833
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 110:149-60 (1995)
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 271:30731-5 (1996)
DOI:10.1074/jbc.271.48.30731
  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 94:2963-8 (1997)
DOI:10.1073/pnas.94.7.2963
  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 269:11269-73 (1994)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.11.6
IUBMB Enzyme Nomenclature: 3.4.11.6
ExPASy - ENZYME nomenclature database: 3.4.11.6
BRENDA, the Enzyme Database: 3.4.11.6
CAS: 9073-92-1

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