KEGG   ENZYME: 3.5.1.14Help
Entry
EC 3.5.1.14                 Enzyme                                 

Name
N-acyl-aliphatic-L-amino acid amidohydrolase;
aminoacylase 1;
aminoacylase I;
dehydropeptidase II;
histozyme;
hippuricase;
benzamidase;
acylase I;
hippurase;
amido acid deacylase;
L-aminoacylase;
acylase;
aminoacylase;
L-amino-acid acylase;
alpha-N-acylaminoacid hydrolase;
long acyl amidoacylase;
short acyl amidoacylase;
ACY1 (gene name);
N-acyl-L-amino-acid amidohydrolase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)
Reaction(IUBMB)
(1) an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate [RN:R01263];
(2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate [RN:R10553]
Reaction(KEGG)
Substrate
N-acyl-aliphatic-L-amino acid;
H2O [CPD:C00001];
N-acetyl-L-cysteine-S-conjugate
Product
aliphatic L-amino acid;
carboxylate [CPD:C00060];
L-cysteine-S-conjugate;
acetate [CPD:C00033]
Comment
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
History
EC 3.5.1.14 created 1965, modified 2013
Pathway
Arginine and proline metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K14677  
aminoacylase
Genes
HSA: 
95(ACY1)
PTR: 
460414(ACY1)
PPS: 
100989711(ACY1)
GGO: 
PON: 
100171519(ACY1)
NLE: 
100603023(ACY1)
MCC: 
698851(ABHD14A)
MCF: 
CJC: 
100386117(ACY1)
MMU: 
109652(Acy1)
RNO: 
300981(Acy1)
CGE: 
100765707(Acy1)
NGI: 
103747435(Acy1)
HGL: 
101696409(Acy1)
OCU: 
100344479(ACY1)
TUP: 
CFA: 
476602(ACY1)
AML: 
UMR: 
103675074(ACY1)
FCA: 
101101118(ACY1)
PTG: 
102948715(ACY1)
BTA: 
768058(ACY1)
BOM: 
102274671(ACY1)
PHD: 
102335491(ACY1)
CHX: 
102173979(ACY1)
OAS: 
101113801(ACY1)
SSC: 
396930(ACY1)
CFR: 
102512036(ACY1)
BACU: 
103005903(ACY1)
LVE: 
103082569(ACY1)
ECB: 
100060631(ACY1)
MYB: 
102263075(ACY1)
MYD: 
102753333(ACY1)
PALE: 
102885238(ACY1)
MDO: 
SHR: 
OAA: 
100075293(ACY1)
GGA: 
100858836(ACY1)
MGP: 
APLA: 
101803141(ACY1)
TGU: 
100219242(ACY1)
FAB: 
101809806(ACY1)
PHI: 
102107169(ACY1)
FPG: 
101918277(ACY1)
FCH: 
102057393(ACY1)
CLV: 
102085226(ACY1)
ASN: 
AMJ: 
PSS: 
102455304(ACY1)
CMY: 
ACS: 
100567123(acy1)
PBI: 
103050622(ACY1)
XLA: 
446741(acy1.1)
XTR: 
496883(acy1.1)
DRE: 
393970(acy1)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102363836(ACY1)
CMK: 
103176752(acy1)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
408969(GB12125)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
CEL: 
CELE_C10C5.5(C10C5.5)
CBR: 
LOA: 
TSP: 
HRO: 
LGI: 
SMM: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os06t0210200-01(Os06g0210200) Os08t0511900-01(Os08g0511900)
OBR: 
BDI: 
SBI: 
SORBI_07g027550(SORBIDRAFT_07g027550)
ZMA: 
SITA: 
PDA: 
ATR: 
s00022p00154990(AMTR_s00022p00154990) s00157p00058420(AMTR_s00157p00058420) s00157p00064680(AMTR_s00157p00064680) s00351p00009890(AMTR_s00351p00009890)
SMO: 
PPP: 
CME: 
GSL: 
CCP: 
MBR: 
DDI: 
DPP: 
DFA: 
DFA_03140(acy1)
ACAN: 
PTI: 
TPS: 
PIF: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:14927637]
  Authors
BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP.
  Title
Specificity of amino acid acylases.
  Journal
J. Biol. Chem. 194 (1952) 455-70.
Reference
2  [PMID:13061423]
  Authors
FONES WS, LEE M.
  Title
Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase.
  Journal
J. Biol. Chem. 201 (1953) 847-56.
Reference
3  [PMID:3355856]
  Authors
Henseling J, Rohm KH
  Title
Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters.
  Journal
Biochim. Biophys. Acta. 959 (1988) 370-7.
Reference
4  [PMID:2318199]
  Authors
Heese D, Berger S, Rohm KH
  Title
Nuclear magnetic relaxation studies of the role of the metal ion in Mn2(+)-substituted aminoacylase I.
  Journal
Eur. J. Biochem. 188 (1990) 175-80.
Reference
5  [PMID:7662111]
  Authors
Palm GJ, Rohm KH
  Title
Aminoacylase I from porcine kidney: identification and characterization of two major protein domains.
  Journal
J. Protein. Chem. 14 (1995) 233-40.
Reference
6  [PMID:9671543]
  Authors
Uttamsingh V, Keller DA, Anders MW
  Title
Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines.
  Journal
Chem. Res. Toxicol. 11 (1998) 800-9.
Reference
7  [PMID:10727768]
  Authors
Lindner H, Hopfner S, Tafler-Naumann M, Miko M, Konrad L, Rohm KH
  Title
The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney.
  Journal
Biochimie. 82 (2000) 129-37.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9012-37-7

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