KEGG   ENZYME: 3.4.11.3Help
Entry
EC 3.4.11.3                 Enzyme                                 

Name
cystinyl aminopeptidase;
cystyl-aminopeptidase;
oxytocinase;
cystine aminopeptidase;
L-cystine aminopeptidase;
oxytocin peptidase;
vasopresssinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aminopeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of an N-terminal amino acid, Cys!Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however [4]
Comment
A zinc-containing sialoglycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family)
History
EC 3.4.11.3 created 1972
Orthology
K01257  
cystinyl aminopeptidase
Genes
HSA: 
4012(LNPEP)
PTR: 
461960(LNPEP)
PPS: 
100975663(LNPEP)
GGO: 
PON: 
100439455(LNPEP)
NLE: 
100603383(LNPEP)
MCC: 
703949(LNPEP)
MCF: 
102115644(LNPEP)
CJC: 
100391174(LNPEP)
MMU: 
240028(Lnpep)
RNO: 
CGE: 
100759698(Lnpep)
NGI: 
103732022(Lnpep)
HGL: 
101709446(Lnpep)
OCU: 
100353022(LNPEP)
TUP: 
102474416(LNPEP)
CFA: 
488896(LNPEP)
AML: 
100473699(LNPEP)
UMR: 
103672209(LNPEP)
FCA: 
101083321(LNPEP)
PTG: 
102969445(LNPEP)
BTA: 
521633(LNPEP)
BOM: 
102267303(LNPEP)
PHD: 
102319089(LNPEP)
CHX: 
102186394(LNPEP)
OAS: 
101102729(LNPEP)
SSC: 
100125826(LNPEP)
CFR: 
102509485(LNPEP)
BACU: 
103014830(LNPEP)
LVE: 
103071064(LNPEP)
ECB: 
100073222(LNPEP)
MYB: 
102260924(LNPEP)
MYD: 
102768292(LNPEP)
PALE: 
102892183(LNPEP)
MDO: 
100015080(LNPEP)
SHR: 
100925233(LNPEP)
OAA: 
100081694(LNPEP)
GGA: 
427279(LNPEP)
APLA: 
TGU: 
FAB: 
101815820(LNPEP)
PHI: 
102109326(LNPEP)
FPG: 
101921722(LNPEP)
FCH: 
102053784(LNPEP)
CLV: 
102089254(LNPEP)
ASN: 
102376681(LNPEP)
AMJ: 
102559536(LNPEP)
PSS: 
CMY: 
102930761(LNPEP)
ACS: 
100565555(lnpep)
PBI: 
103049159(LNPEP)
XLA: 
495293(lnpep)
XTR: 
100216271(lnpep)
DRE: 
322814(lnpep)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102360095(LNPEP)
CMK: 
103178390(lnpep)
HRO: 
 » show all
Taxonomy
Reference
1  [PMID:6041057]
  Authors
Sjoholm I.
  Title
Biochemical studies on oxytocin and oxytocinase.
  Journal
Acta. Pharm. Suec. 4 (1967) 81-96.
Reference
2  [PMID:4292447]
  Authors
Sjoholm I, Yman L.
  Title
Degradation of oxytocin, lysine-vasopressin, angiotensin II and angiotensin-II-amide by oxytocinase (cystine aminopeptidase).
  Journal
Acta. Pharm. Suec. 4 (1967) 65-76.
Reference
3  [PMID:5421622]
  Authors
Yman L.
  Title
Studies on human serum aminopeptidases. Some properties of oxytocinase, human serum aminopeptidase A and leucine aminopeptidase and their purification from retroplacental serum.
  Journal
Acta. Pharm. Suec. 7 (1970) 75-86.
Reference
4
  Authors
Sakura, H., Lin, T.Y., Doi, M., Mizutani, S. and Kawashima, Y.
  Title
Purification and properties of oxytocinase, a metalloenzyme.
  Journal
Biochem. Int. 2 (1981) 173-179.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9031-41-8

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