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 [CPD:C02882];
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
ec00220  Arginine biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01130  Biosynthesis of antibiotics
Orthology
K14677  aminoacylase
Genes
HSA: 100526760(ABHD14A-ACY1) 95(ACY1)
PTR: 460414(ACY1)
PPS: 100989711(ACY1)
GGO: 101146240(ACY1)
PON: 100171519(ACY1)
NLE: 100603023(ACY1)
MCC: 698851(ACY1)
MCF: 101867505
CSAB: 103227712(ACY1)
RRO: 104663721(ACY1)
RBB: 108525587
CJC: 100386117(ACY1)
SBQ: 101027476(ACY1)
MMU: 109652(Acy1)
RNO: 300981(Acy1)
CGE: 100765707(Acy1)
NGI: 103747435(Acy1)
HGL: 101696409(Acy1)
CCAN: 109685975(Acy1)
OCU: 100344479(ACY1)
TUP: 102503256(ACY1)
CFA: 476602(ACY1)
AML: 100479661(ACY1)
UMR: 103675074(ACY1)
ORO: 101372032(ACY1)
PTG: 102948715(ACY1)
AJU: 106987018(ACY1)
BTA: 768058(ACY1)
BOM: 102274671(ACY1)
BIU: 109576040(ACY1)
PHD: 102335491(ACY1)
CHX: 102173979(ACY1)
OAS: 101113801(ACY1)
SSC: 396930(ACY1)
CFR: 102512036(ACY1)
CDK: 105093821(ACY1)
BACU: 103005903(ACY1)
LVE: 103082569(ACY1)
OOR: 101286870(ACY1)
ECB: 100060631(ACY1)
EPZ: 103546483(ACY1)
EAI: 106821753(ACY1)
MYB: 102263075(ACY1)
MYD: 102753333(ACY1)
HAI: 109375828(ACY1)
RSS: 109459082
PALE: 102885238(ACY1)
LAV: 100663232
TMU: 101349746
MDO: 100031141(ACY1)
SHR: 100934680(ACY1)
OAA: 100075293(ACY1)
GGA: 100858836(ACY1)
MGP: 100550404(ACY1)
CJO: 107319637(ACY1)
APLA: 101803141(ACY1)
ACYG: 106042853(ACY1)
TGU: 100219242(ACY1)
GFR: 102033439(ACY1)
FAB: 101809806(ACY1)
PHI: 102107169(ACY1)
PMAJ: 107210075
CCAE: 111935148(ACY1)
CCW: 104683245
FPG: 101918277(ACY1)
FCH: 102057393(ACY1)
CLV: 102085226
EGZ: 104126741(ACY1)
AAM: 106487065(ACY1)
ASN: 102369149(ACY1)
AMJ: 102566953(ACY1)
PSS: 102455304(ACY1)
CMY: 102938259
CPIC: 101950834(ACY1)
ACS: 100567123(acy1)
PVT: 110084475(ACY1)
PBI: 103050622(ACY1)
GJA: 107115931(ACY1)
XLA: 399011(acy1.2.L) 446741(acy1.1.S)
XTR: 100494699 101735201 108647469(acy1) 496883(acy1.1)
NPR: 108793445
DRE: 103909643 393970(acy1)
CCAR: 109047323
IPU: 108254950(acy1)
AMEX: 103031539(acy1)
TRU: 101072726(acy1)
LCO: 104931347(acy1)
NCC: 104967510(acy1)
MZE: 101471948(acy1)
OLA: 101160548(acy1)
XMA: 102227096(acy1)
PRET: 103464610(acy1)
NFU: 107385138(acy1)
KMR: 108247369(acy1)
CSEM: 103385797(acy1) 103399583
LCF: 108889386(acy1)
SDU: 111222940(acy1)
HCQ: 109522261(acy1)
BPEC: 110168627(acy1)
MALB: 109952383(acy1)
SASA: 100194932(acy1)
ELS: 105028113(acy1)
SFM: 108933832(acy1)
LCM: 102363836(ACY1)
CMK: 103176752(acy1)
APLC: 110984341
DME: Dmel_CG6465(CG6465) Dmel_CG6726(CG6726) Dmel_CG6738(CG6738)
DSI: Dsimw501_GD20716(Dsim_GD20716) Dsimw501_GD20717(Dsim_GD20717) Dsimw501_GD20996(Dsim_GD20996) Dsimw501_GD20998(Dsim_GD20998) Dsimw501_GD20999(Dsim_GD20999) Dsimw501_GD21000(Dsim_GD21000) Dsimw501_GD21001(Dsim_GD21001)
AAG: 5574529
AME: 408969
BIM: 100746427
BTER: 100645222
SOC: 105207857
AEC: 105154436
ACEP: 105621043
PBAR: 105428375
LHU: 105669821
PGC: 109860040
NVI: 100114283
MDL: 103571230
DPA: 109540108
CLEC: 106670786
ZNE: 110832721
CEL: CELE_C06A6.4(C06A6.4) CELE_C10C5.3(C10C5.3) CELE_C10C5.4(C10C5.4) CELE_C10C5.5(C10C5.5)
CBR: CBG17687
TSP: Tsp_07914
CRG: 105336810
MYI: 110443347
OBI: 106878078
SHX: MS3_08008
EGL: EGR_04365
ADF: 107353293
AQU: 100634447
ATH: AT1G44820 AT4G38220(AQI)
CPAP: 110821496
EGR: 104419053
CAM: 101489624
LJA: Lj0g3v0037669.1(Lj0g3v0037669.1) Lj0g3v0201079.1(Lj0g3v0201079.1) Lj0g3v0313609.1(Lj0g3v0313609.1) Lj0g3v0313609.2(Lj0g3v0313609.2) Lj0g3v0313609.3(Lj0g3v0313609.3) Lj2g3v1495110.1(Lj2g3v1495110.1)
CSV: 101213747
VVI: 100260562
OEU: 111393386
DOSA: Os06t0210200-01(Os06g0210200) Os08t0511900-01(Os08g0511900)
BDI: 100839108
ATS: 109742087(LOC109742087) 109779347(LOC109779347)
SBI: 8055167
SITA: 101785165
AOF: 109841919
DDI: DDB_G0270562(acy1)
DFA: DFA_03140(acy1)
SMIN: v1.2.025325.t1(symbB.v1.2.025325.t1)
SPAR: SPRG_01415
 » 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 194:455-70 (1952)
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 201:847-56 (1953)
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 959:370-7 (1988)
DOI:10.1016/0005-2760(88)90211-1
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 188:175-80 (1990)
DOI:10.1111/j.1432-1033.1990.tb15385.x
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 14:233-40 (1995)
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 11:800-9 (1998)
DOI:10.1021/tx980018b
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 82:129-37 (2000)
DOI:10.1016/S0300-9084(00)00191-7
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.14
IUBMB Enzyme Nomenclature: 3.5.1.14
ExPASy - ENZYME nomenclature database: 3.5.1.14
BRENDA, the Enzyme Database: 3.5.1.14
CAS: 9012-37-7

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