KEGG   ENZYME: 3.4.24.61Help
Entry
EC 3.4.24.61                Enzyme                                 

Name
nardilysin;
N-arginine dibasic convertase;
NRD-convertase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of polypeptides, preferably at -Xaa!Arg-Lys-, and less commonly at -Arg!Arg-Xaa-, in which Xaa is not Arg or Lys
Comment
Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family)
History
EC 3.4.24.61 created 1995
Orthology
K01411  
nardilysin
Genes
HSA: 
4898(NRDC)
PTR: 
456852(NRDC)
PPS: 
100988880(NRDC)
GGO: 
101131269(NRD1)
PON: 
100452780(NRDC)
NLE: 
100601344(NRDC)
MCC: 
106998623(NRDC)
MCF: 
102123458(NRDC)
CSAB: 
103224822(NRDC)
RRO: 
104667840(NRDC)
CJC: 
100398602(NRDC)
SBQ: 
MMU: 
230598(Nrd1)
RNO: 
25499(Nrdc)
CGE: 
100752575(Nrdc)
NGI: 
103730258(Nrdc)
HGL: 
101716146(Nrdc)
OCU: 
100358011(NRDC)
TUP: 
102500973(NRDC)
CFA: 
475354(NRDC)
AML: 
100480818(NRDC)
UMR: 
103670723(NRDC)
FCA: 
101088678(NRDC)
PTG: 
102958230(NRDC)
BTA: 
511254(NRDC)
BOM: 
102275032(NRDC)
PHD: 
102330606(NRDC)
CHX: 
102168408(NRDC)
OAS: 
101111671(NRDC)
SSC: 
100514906(NRDC)
CFR: 
102510363(NRDC)
BACU: 
103015976(NRDC)
LVE: 
103070846(NRDC)
ECB: 
100050978(NRDC)
MYB: 
102253301(NRDC)
MYD: 
102760071(NRDC)
PALE: 
102880364(NRDC)
LAV: 
100656401(NRDC)
MDO: 
100011053(NRDC)
SHR: 
100924924(NRDC)
OAA: 
100078629(NRDC)
GGA: 
424635(NRDC)
MGP: 
100540908(NRDC)
CJO: 
107317638(NRDC)
APLA: 
TGU: 
100220278(NRDC)
GFR: 
102041804(NRDC)
FAB: 
101806826(NRDC)
PHI: 
102102617(NRDC)
CCW: 
104695202(NRDC)
FPG: 
101917899(NRDC)
FCH: 
102059699(NRDC)
CLV: 
102084824(NRDC)
AAM: 
ASN: 
AMJ: 
PSS: 
CMY: 
102932297(Nardilysin) 102942086(NRDC)
ACS: 
PBI: 
GJA: 
XLA: 
108714316(nrdc.L) 108715597(nrdc.S)
XTR: 
100489182(nrdc)
DRE: 
565850(nrd1a)
TRU: 
TNG: 
MZE: 
OLA: 
XMA: 
SASA: 
LCM: 
102357193(NRDC)
CMK: 
103182811(nrdc)
BFO: 
SPU: 
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD15963(Dsim_GD15963) Dsimw501_GD17647(Dsim_GD17647)
DWI: 
DYA: 
Dyak_GE17590(dyak_GLEANR_18907) Dyak_GE19720(dyak_GLEANR_3580) Dyak_GE23250(dyak_GLEANR_7039)
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
552055(NRD1)
BIM: 
BTER: 
SOC: 
AEC: 
HST: 
105191362(Nardilysin)
CFO: 
105254177(Nardilysin)
NVI: 
TCA: 
BMOR: 
DPL: 
PXY: 
API: 
PHU: 
DPX: 
ISC: 
HRO: 
LGI: 
CRG: 
105319154(Nardilysin)
OBI: 
NVE: 
ADF: 
HMG: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
EGR: 
GMX: 
PVU: 
VRA: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj0g3v0009849.1(Lj0g3v0009849.1) Lj0g3v0009859.1(Lj0g3v0009859.1) Lj4g3v1983560.1(Lj4g3v1983560.1) Lj6g3v0315180.1(Lj6g3v0315180.1) Lj6g3v0315180.2(Lj6g3v0315180.2)
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0013s15070g(POPTRDRAFT_571877)
VVI: 
SLY: 
SPEN: 
SOT: 
SIND: 
BVG: 
NNU: 
OSA: 
DOSA: 
Os03t0336300-01(Os03g0336300)
OBR: 
BDI: 
ATS: 
SBI: 
SORBI_01g036110(SORBIDRAFT_01g036110)
ZMA: 
103639163(GRMZM2G084525)
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
VCN: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
CSL: 
CVR: 
APRO: 
MBR: 
SRE: 
SMIN: 
v1.2.017618.t1(symbB.v1.2.017618.t1)
PTI: 
TPS: 
PIF: 
PSOJ: 
SPAR: 
EHX: 
 » show all
Taxonomy
Reference
1  [PMID:3897221]
  Authors
Gomez S, Gluschankof P, Morel A, Cohen P.
  Title
The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes.
  Journal
J. Biol. Chem. 260 (1985) 10541-5.
Reference
2  [PMID:2885328]
  Authors
Gluschankof P, Gomez S, Morel A, Cohen P.
  Title
Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex.
  Journal
J. Biol. Chem. 262 (1987) 9615-20.
Reference
3  [PMID:8294457]
  Authors
Chesneau V, Pierotti AR, Barre N, Creminon C, Tougard C, Cohen P.
  Title
Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues.
  Journal
J. Biol. Chem. 269 (1994) 2056-61.
Reference
4  [PMID:8016118]
  Authors
Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P.
  Title
N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 6078-82.
  Sequence
[rno:25499]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
292850-69-2

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