KEGG   ENZYME: 3.4.17.20
Entry
EC 3.4.17.20                Enzyme                                 

Name
carboxypeptidase U;
arginine carboxypeptidase;
carboxypeptidase R;
plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes);
thrombin-activatable fibrinolysis inhibitor
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
Reaction(IUBMB)
Release of C-terminal Arg and Lys from a polypeptide
Comment
Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family)
History
EC 3.4.17.20 created 1997
Orthology
K01300  carboxypeptidase B2
Genes
HSA: 1361(CPB2)
PTR: 452582(CPB2)
PPS: 100993828(CPB2)
GGO: 101153798(CPB2)
PON: 100452501(CPB2)
NLE: 100582393(CPB2)
MCC: 703317(CPB2)
MCF: 102132600(CPB2)
CSAB: 103214382(CPB2)
RRO: 104658149(CPB2)
RBB: 108528946(CPB2)
CJC: 100411115(CPB2)
SBQ: 101041667(CPB2)
MMU: 56373(Cpb2)
MCAL: 110309374(Cpb2)
MPAH: 110325644(Cpb2)
RNO: 113936(Cpb2)
MUN: 110547470(Cpb2)
CGE: 100754304(Cpb2)
NGI: 103726752(Cpb2)
HGL: 101712343(Cpb2)
CCAN: 109698557(Cpb2)
OCU: 100341346(CPB2)
TUP: 102473098(CPB2)
CFA: 608910(CPB2)
VVP: 112933941(CPB2)
AML: 100482734(CPB2)
UMR: 103677685(CPB2)
UAH: 113251347(CPB2)
ORO: 101370239(CPB2)
ELK: 111147094
FCA: 101082116(CPB2)
PTG: 102952076(CPB2)
PPAD: 109265929(CPB2)
AJU: 106972009(CPB2)
BTA: 508222(CPB2)
BOM: 102285531(CPB2)
BIU: 109566696(CPB2)
BBUB: 102390937(CPB2)
CHX: 102181135(CPB2)
OAS: 101112329(CPB2)
SSC: 100155038(CPB2)
CFR: 102509764(CPB2)
CDK: 105089749(CPB2)
BACU: 103010017(CPB2)
LVE: 103075780(CPB2)
OOR: 101269719(CPB2)
DLE: 111175334(CPB2)
PCAD: 102985818(CPB2)
ECB: 100058534(CPB2)
EPZ: 103548935(CPB2)
EAI: 106829669(CPB2)
MYB: 102250791(CPB2)
MYD: 102755974(CPB2)
MNA: 107542259(CPB2)
HAI: 109391288(CPB2)
DRO: 112310676(CPB2)
PALE: 102878653(CPB2)
RAY: 107505990(CPB2)
MJV: 108407588(CPB2)
MDO: 100016398(CPB2)
SHR: 100928968(CPB2)
PCW: 110197346(CPB2)
OAA: 100083738(CPB2)
GGA: 418851(CPB2)
MGP: 100545409(CPB2)
CJO: 107308136(CPB2)
NMEL: 110387568(CPB2)
APLA: 101791007(CPB2)
ACYG: 106035057(CPB2)
TGU: 100229153(CPB2)
LSR: 110469572(CPB2)
SCAN: 103827416(CPB2)
GFR: 102041508(CPB2)
FAB: 101808771(CPB2)
PHI: 102107395(CPB2)
PMAJ: 107199992(CPB2)
CCAE: 111937540(CPB2)
CCW: 104689980(CPB2)
ETL: 114059887(CPB2)
FPG: 101919154(CPB2)
FCH: 102052809(CPB2)
CLV: 102085489(CPB2)
EGZ: 104131617(CPB2)
NNI: 104010961(CPB2)
ACUN: 113481749(CPB2)
PADL: 103915914(CPB2)
AAM: 106489197(CPB2)
ASN: 102376487(CPB2)
AMJ: 102562517(CPB2)
PSS: 102448472(CPB2)
CMY: 102946625(CPB2)
CPIC: 101933938(CPB2)
ACS: 100567959(cpb2)
PVT: 110076120(CPB2)
PBI: 103051972(CPB2)
PMUR: 107289863(CPB2)
PMUA: 114593624(CPB2)
GJA: 107110254(CPB2)
XLA: 108708528(cpb2.L) 108709798(cpb2.S)
XTR: 595005(cpb2)
NPR: 108794281(CPB2)
DRE: 100000935(cpb2)
SRX: 107707839(cpb2)
SANH: 107654270(cpb2)
SGH: 107588824(cpb2)
CCAR: 109067316(cpb2)
IPU: 108258492(cpb2)
PHYP: 113537361(cpb2)
AMEX: 103039184(cpb2)
EEE: 113585022(cpb2)
TRU: 101063870(cpb2)
LCO: 104937555(cpb2)
NCC: 104941379
ONL: 100699903
OLA: 101175299(cpb2)
XMA: 102234292(cpb2)
XCO: 114138216(cpb2)
PRET: 103475539(cpo)
CVG: 107093726(cpb2)
NFU: 107381108(cpb2)
KMR: 108246710(cpb2)
ALIM: 106529640(cpb2)
AOCE: 111580792(cpb2)
CSEM: 103389881(cpb2)
POV: 109643485
LCF: 108872994(cpb2)
SDU: 111238723(cpb2)
SLAL: 111644417(cpb2)
HCQ: 109520860(cpb2)
BPEC: 110168983(cpb2)
SASA: 106574315(cpb2) 106575090(cpo)
SALP: 111953182 111953547(cpb2)
ELS: 105023706(cpo)
PKI: 111860687
LCM: 102355283(CPB2)
CMK: 103177537(cpb2)
RTP: 109917215
AAG: 5572629
MDL: 103577483
EPA: 110245430
SPIS: 111335355
 » show all
Reference
1  [PMID:1939207]
  Authors
Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D.
  Title
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.
  Journal
J Biol Chem 266:21833-8 (1991)
  Sequence
[hsa:1361]
Reference
2  [PMID:8130654]
  Authors
Shinohara T, Sakurada C, Suzuki T, Takeuchi O, Campbell W, Ikeda S, Okada N, Okada H.
  Title
Pro-carboxypeptidase R cleaves bradykinin following activation.
  Journal
Int Arch Allergy Immunol 103:400-4 (1994)
DOI:10.1159/000236661
Reference
3  [PMID:8195249]
  Authors
Wang W, Hendriks DF, Scharpe SS.
  Title
Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen.
  Journal
J Biol Chem 269:15937-44 (1994)
Reference
4  [PMID:7727441]
  Authors
Tan AK, Eaton DL.
  Title
Activation and characterization of procarboxypeptidase B from human plasma.
  Journal
Biochemistry 34:5811-6 (1995)
DOI:10.1021/bi00017a012
Reference
5  [PMID:8916945]
  Authors
Broze GJ Jr, Higuchi DA.
  Title
Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma.
  Journal
Blood 88:3815-23 (1996)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.17.20
IUBMB Enzyme Nomenclature: 3.4.17.20
ExPASy - ENZYME nomenclature database: 3.4.17.20
BRENDA, the Enzyme Database: 3.4.17.20
CAS: 156621-18-0
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