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
Orthology
K14677  aminoacylase
Genes
HSA: 100526760(ABHD14A-ACY1) 95(ACY1)
PTR: 460414(ACY1)
PPS: 100989711(ACY1)
PON: 100171519(ACY1)
NLE: 100603023
MCC: 100425407 698851
MCF: 101867505
CSAB: 103227712(ACY1)
RRO: 104663721 115898588
CJC: 100386117(ACY1)
SBQ: 101027476(ACY1)
MMU: 109652(Acy1)
MCAL: 110301037(Acy1)
MPAH: 110327471
RNO: 300981(Acy1)
MUN: 110550172(Acy1)
CGE: 100765707(Acy1)
NGI: 103747435(Acy1)
HGL: 101696409(Acy1)
CCAN: 109685975(Acy1)
OCU: 100344479(ACY1)
TUP: 102503256(ACY1)
CFA: 476602(ACY1)
VVP: 112910690
AML: 100479661(ACY1)
UMR: 103675074(ACY1)
UAH: 113256935
ORO: 101372032(ACY1)
ELK: 111143997
PTG: 102948715(ACY1)
PPAD: 109247881
AJU: 106987018
BTA: 768058(ACY1)
BOM: 102274671(ACY1)
BIU: 109576040(ACY1)
BBUB: 102408788(ACY1)
CHX: 102173979(ACY1)
OAS: 101113801(ACY1)
SSC: 396930(ACY1)
CFR: 102512036
CDK: 105093821(ACY1)
BACU: 103005903(ACY1)
LVE: 103082569(ACY1)
OOR: 101286870(ACY1)
DLE: 111174327(ACY1)
ECB: 100060631(ACY1)
EPZ: 103546483(ACY1)
EAI: 106821753(ACY1)
MYB: 102263075(ACY1)
MYD: 102753333(ACY1)
MNA: 107540194(ACY1)
HAI: 109375828(ACY1)
DRO: 112309817
PALE: 102885238(ACY1)
RAY: 107504158(ACY1)
MJV: 108388575(ACY1)
LAV: 100663232
TMU: 101349746
MDO: 100031141(ACY1)
SHR: 100934680(ACY1)
PCW: 110217043(ACY1)
OAA: 100075293
GGA: 100858836(ACY1)
MGP: 100550404(ACY1)
CJO: 107319637
NMEL: 110405016(ACY1)
APLA: 101803141
ACYG: 106042853(ACY1)
TGU: 100219242
LSR: 110472111
SCAN: 103824272
GFR: 102033439(ACY1)
FAB: 101809806(ACY1)
PHI: 102107169(ACY1)
PMAJ: 107210075
CCAE: 111935148(ACY1)
CCW: 104683245
ETL: 114058684
FPG: 101918277(ACY1)
FCH: 102057393
CLV: 102085226
EGZ: 104126741(ACY1)
NNI: 104008693(ACY1)
ACUN: 113484690(ACY1)
PADL: 103915051(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)
PMUR: 107291116(ACY1)
TSR: 106557154(ACY1)
PMUA: 114591568(ACY1)
GJA: 107115931(ACY1)
XLA: 399011(acy1.2.L) 446741(acy1.1.S)
XTR: 101735201 496883(acy1.1)
NPR: 108793445
CCAR: 109047323
IPU: 108254950(acy1)
PHYP: 113539457(acy1)
AMEX: 103031539(acy1)
EEE: 113583811(acy1)
TRU: 101072726(acy1)
LCO: 104931347(acy1)
NCC: 104967510(acy1)
MZE: 101471948(acy1)
ONL: 100694810(acy1)
OLA: 101160548(acy1)
XMA: 102227096(acy1)
XCO: 114135714(acy1)
PRET: 103464610(acy1)
CVG: 107102904(acy1)
NFU: 107385138(acy1)
KMR: 108247369(acy1)
ALIM: 106516071(acy1)
AOCE: 111563222(acy1)
CSEM: 103385797(acy1)
POV: 109638451(acy1)
LCF: 108889386(acy1)
SDU: 111222940(acy1)
SLAL: 111660709(acy1)
HCQ: 109522261(acy1)
BPEC: 110168627(acy1)
MALB: 109952383(acy1)
SASA: 100194932(acy1)
SALP: 112070374(acy1)
ELS: 105028113(acy1)
SFM: 108933832(acy1)
PKI: 111860026(acy1)
LCM: 102363836(ACY1)
CMK: 103176752(acy1)
RTP: 109923199(acy1)
APLC: 110984341
DME: Dmel_CG17109(CG17109) Dmel_CG17110(CG17110) Dmel_CG6465(CG6465) Dmel_CG6726(CG6726) Dmel_CG6733(CG6733) 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
CCAL: 108622570
OBB: 114876678
SOC: 105207857
MPHA: 105839002
AEC: 105154436
ACEP: 105621043
PBAR: 105428375
LHU: 105669821
PGC: 109860040
OBO: 105276644
PCF: 106788996
NVI: 100114283
CSOL: 105359781
MDL: 103571230
DPA: 109540108
BTAB: 109043553
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)
TSP: Tsp_07914
PCAN: 112571574
CRG: 105336810
MYI: 110443347
OBI: 106878078
SHX: MS3_08008
EGL: EGR_04365
ADF: 107353293
AMIL: 114947117
PDAM: 113673272
SPIS: 111322407
AQU: 100634447
CAM: 101489624
LJA: Lj0g3v0037669.1(Lj0g3v0037669.1) Lj0g3v0313609.1(Lj0g3v0313609.1) Lj0g3v0313609.2(Lj0g3v0313609.2) Lj0g3v0313609.3(Lj0g3v0313609.3)
CSV: 101213747
OEU: 111393386
DOSA: Os06t0210200-01(Os06g0210200) Os08t0511900-01(Os08g0511900)
ATS: 109742087(LOC109742087) 109779347(LOC109779347)
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)
DOI:10.1007/bf01886764
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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