KEGG   ENZYME: 3.4.19.1Help
Entry
EC 3.4.19.1                 Enzyme                                 

Name
acylaminoacyl-peptidase;
acylamino-acid-releasing enzyme;
N-acylpeptide hydrolase;
N-formylmethionine (fMet) aminopeptidase;
alpha-N-acylpeptide hydrolase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Omega peptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Comment
Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family).
History
EC 3.4.19.1 created 1978 as EC 3.4.14.3, transferred 1981 to EC 3.4.19.1
Orthology
K01303  
acylaminoacyl-peptidase
Genes
HSA: 
327(APEH)
PTR: 
460376(APEH)
PPS: 
100985786(APEH)
GGO: 
101141597(APEH)
PON: 
100435231(APEH)
MCC: 
705948(APEH)
MCF: 
102122091(APEH)
MMU: 
235606(Apeh)
RNO: 
24206(Apeh)
CGE: 
100761732(Apeh)
HGL: 
101715825(Apeh)
TUP: 
102483690(APEH)
CFA: 
476622(APEH)
AML: 
100475477(APEH)
FCA: 
101085867(APEH)
PTG: 
102959601(APEH)
BTA: 
514666(APEH)
BOM: 
102269347(APEH)
PHD: 
102339268(APEH)
CHX: 
102177845(APEH)
OAS: 
101103273(APEH)
SSC: 
396961(APEH)
CFR: 
102505664(APEH)
BACU: 
103017766(APEH)
LVE: 
103078029(APEH)
ECB: 
100053100(APEH)
MYB: 
102261178(APEH)
MYD: 
102768766(APEH)
PALE: 
102893074(APEH)
MDO: 
100027962(APEH)
SHR: 
100934071(APEH)
OAA: 
100091478(APEH)
GGA: 
MGP: 
TGU: 
FAB: 
PHI: 
FPG: 
FCH: 
CLV: 
102097899(APEH)
ASN: 
102378133(APEH)
AMJ: 
102565732(APEH)
PSS: 
102451421(APEH)
CMY: 
102935556(APEH)
ACS: 
100567769(apeh)
PBI: 
XTR: 
100491896(apeh)
DRE: 
321028(apeh) 678599(si:dkey-16c7.3)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
AME: 
727648(GB19295)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
CBG11649(Cbr-dpf-5)
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
MTR: 
CAM: 
FVE: 
CSV: 
RCU: 
POP: 
POPTR_0008s16030g(POPTRDRAFT_657231)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os10t0415800-01(Os10g0415800)
OBR: 
BDI: 
SBI: 
SORBI_01g021960(SORBIDRAFT_01g021960)
ZMA: 
100281428(cl9977_1) 100285393(pco091746)
SITA: 
ATR: 
s00002p00268330(AMTR_s00002p00268330)
SMO: 
PPP: 
CRE: 
VCN: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
LBC: 
MPR: 
CCI: 
SCM: 
PGR: 
DDI: 
DPP: 
DFA: 
DFA_09138(apeh)
CPV: 
CHO: 
TGO: 
TET: 
PTM: 
PTI: 
TPS: 
PIF: 
GTT: 
NGR: 
TVA: 
ILO: 
PHA: 
BRA: 
CCS: 
BCE: 
BCL: 
OIH: 
GKA: 
GTN: 
LDB: 
LBR: 
ACE: 
FNU: 
SRU: 
TTH: 
APE: 
SMR: 
HBU: 
PAS: 
 » show all
Taxonomy
Reference
1  [PMID:1137989]
  Authors
Tsunasawa S, Narita K, Ogata K.
  Title
Purification and properties of acylamino acid-releasing enzyme from rat liver.
  Journal
J. Biochem. (Tokyo). 77 (1975) 89-102.
Reference
2  [PMID:477668]
  Authors
Unger T, Nagelschmidt M, Struck H.
  Title
N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification and some properties.
  Journal
Eur. J. Biochem. 97 (1979) 205-11.
Reference
3  [PMID:3305492]
  Authors
Kobayashi K, Smith JA.
  Title
Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction.
  Journal
J. Biol. Chem. 262 (1987) 11435-45.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
73562-30-8

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