KEGG   ENZYME: 3.4.17.22Help
Entry
EC 3.4.17.22                Enzyme                                 

Name
metallocarboxypeptidase D;
carboxypeptidase D (cattle, human, mouse, rat);
gp180 (duck)
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
BRITE hierarchy
Reaction(IUBMB)
Releases C-terminal Arg and Lys from polypeptides
Comment
Activated by Co2+; inhibited by guanidinoethylmercaptosuccinic acid. Large molecule (180 kDa) because of presence of three copies of metallopeptidase domain. The product of the silver gene (Drosophila) is similar. A zinc metallopeptidase in peptidase family M14 (carboxypeptidase A family)
History
EC 3.4.17.22 created 1997
Orthology
K07752  carboxypeptidase D
Genes
HSA: 1362(CPD)
PTR: 454557(CPD)
PPS: 100977539(CPD)
GGO: 101128462(CPD)
PON: 100436717(CPD)
NLE: 100581363 100597052(CPD)
MCC: 712407(CPD)
MCF: 102135486(CPD)
CSAB: 103242665(CPD)
RRO: 104665980(CPD)
RBB: 108517294(CPD)
CJC: 100394725(CPD)
SBQ: 101034539(CPD)
MMU: 12874(Cpd)
RNO: 25306(Cpd)
CGE: 100757331(Cpd)
NGI: 103730489(Cpd)
HGL: 101707145(Cpd)
CCAN: 109695996(Cpd)
OCU: 100339843(CPD)
TUP: 102482407(CPD)
CFA: 480636(CPD)
AML: 100476363(CPD)
UMR: 103667395(CPD)
ORO: 101378469(CPD)
FCA: 101081771(CPD)
PTG: 102964772(CPD)
AJU: 106968721(CPD)
BTA: 532189(CPD)
BOM: 102274420(CPD)
BIU: 109573746(CPD)
PHD: 102328282(CPD)
CHX: 102173329(CPD)
OAS: 101122802(CPD)
SSC: 100517495(CPD)
CFR: 102509584(CPD)
CDK: 105088145(CPD)
BACU: 103018688(CPD)
LVE: 103069178 103070181(CPD)
OOR: 101288119(CPD)
ECB: 100072234(CPD)
EPZ: 103555366(CPD)
EAI: 106822001(CPD)
MYB: 102248065(CPD)
MYD: 102770691(CPD)
HAI: 109386883(CPD)
RSS: 109451348(CPD)
PALE: 102882023(CPD)
LAV: 100656143(CPD)
TMU: 101345198
MDO: 100015882(CPD)
SHR: 100923705(CPD)
OAA: 100078830(CPD)
GGA: 417590(CPD)
MGP: 100545345(CPD)
CJO: 107322671(CPD)
APLA: 101802114(CPD)
ACYG: 106045786(CPD)
TGU: 100219416(CPD)
GFR: 102042306(CPD)
FAB: 101810441(CPD)
PHI: 102109483(CPD)
PMAJ: 107212948(CPD)
CCW: 104691182(CPD)
FPG: 101913850(CPD)
FCH: 102048834(CPD)
CLV: 102093976(CPD)
EGZ: 104121866(CPD)
ASN: 102370437(CPD)
AMJ: 102566010(CPD)
PSS: 102462593(CPD)
CMY: 102937712(CPD)
CPIC: 101930837(CPD)
ACS: 103282844
PVT: 110084275(CPD)
PBI: 103063983(CPD)
GJA: 107119558(CPD)
XTR: 100135269(cpd) 101730225(cpd)
NPR: 108800486(CPD)
DRE: 563008(cpda)
IPU: 108277877(cpd) 108279099
AMEX: 103034353(cpd) 103045613
TRU: 101064552(cpd)
LCO: 104922855(cpd)
NCC: 104943195(cpd)
MZE: 101482580(cpd)
OLA: 101173725(cpd)
XMA: 102218419(cpd)
PRET: 103474532(cpd)
NFU: 107380397(cpd)
CSEM: 103378079(cpd)
LCF: 108890362(cpd)
HCQ: 109525484(cpd)
BPEC: 110174241(cpd)
ELS: 105007417(cpd)
SFM: 108932207(cpd)
LCM: 102351860(CPD)
CMK: 103183365(cpd)
CIN: 100180843
SPU: 593440
APLC: 110980715
SKO: 100372562
DME: Dmel_CG4122(svr)
DSI: Dsimw501_GD16509(Dsim_GD16509)
MDE: 101900836
AAG: 23687919
AME: 724816
BIM: 100749957
BTER: 100651403
SOC: 105199087
AEC: 105152604
ACEP: 105617236
PBAR: 105433737
HST: 105184921
CFO: 105251427
LHU: 105668319
PGC: 109863141
NVI: 100122498
TCA: 655207
DPA: 109540038
NVL: 108563176
BMOR: 101735927
PRAP: 110997051
DNX: 107164754
ZNE: 110826868
TUT: 107369162
CEL: CELE_F59A3.1(cpd-1)
CBR: CBG12487
BMY: Bm1_48550
TSP: Tsp_00258
MYI: 110446872
OBI: 106880679
LAK: 106176567
SHX: MS3_09839
AQU: 100636145
TCC: 18592698
GHI: 107957516
VRA: 106772299
VAR: 108326385
CCAJ: 109805851
CAM: 101510794
LJA: Lj5g3v1914090.1(Lj5g3v1914090.1)
LANG: 109335576
PMUM: 103336220
PAVI: 110760284
ZJU: 107421610
CSV: 101220508
CMO: 103496589
CMAX: 111487230
CMOS: 111458783
CPEP: 111796924
JCU: 105635478
POP: 7469245
VVI: 100249088
SPEN: 107018317
NSY: 104240271
NTO: 104087394
OEU: 111393795
HAN: 110917190
LSV: 111875971
DCR: 108218697
SOE: 110792166
ZMA: 100278138(si606046e06) 100303788 109939978
PDA: 103709752
DCT: 110114804
MNG: MNEG_3741
DFA: DFA_04675
BMX: BMS_2471
WIN: WPG_1411
IAL: IALB_1057
CACI: CLOAM1811
 » show all
Taxonomy
Reference
1  [PMID:9525948]
  Authors
Eng FJ, Novikova EG, Kuroki K, Ganem D, Fricker LD.
  Title
gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity.
  Journal
J Biol Chem 273:8382-8 (1998)
DOI:10.1074/jbc.273.14.8382
  Sequence
[apla:101802114]
Reference
2  [PMID:7559630]
  Authors
Song L, Fricker LD.
  Title
Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary.
  Journal
J Biol Chem 270:25007-13 (1995)
DOI:10.1074/jbc.270.42.25007
Reference
3  [PMID:8910535]
  Authors
Song L, Fricker LD.
  Title
Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D.
  Journal
J Biol Chem 271:28884-9 (1996)
DOI:10.1074/jbc.271.46.28884
Other DBs
ExplorEnz - The Enzyme Database: 3.4.17.22
IUBMB Enzyme Nomenclature: 3.4.17.22
ExPASy - ENZYME nomenclature database: 3.4.17.22
BRENDA, the Enzyme Database: 3.4.17.22
CAS: 153967-26-1

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