KEGG   ENZYME: 3.5.1.114
Entry
EC 3.5.1.114                Enzyme                                 

Name
N-acyl-aromatic-L-amino acid amidohydrolase;
aminoacylase 3;
aminoacylase III;
ACY3 (gene name)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
Sysname
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
Reaction(IUBMB)
(1) an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate [RN:R10621];
(2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate [RN:R10553]
Reaction(KEGG)
R10553 R10621
Substrate
N-acyl-aromatic-L-amino acid [CPD:C20735];
H2O [CPD:C00001];
N-acetyl-L-cysteine S-conjugate [CPD:C05727]
Product
aromatic-L-amino acid [CPD:C01021];
carboxylate [CPD:C00060];
L-cysteine S-conjugate [CPD:C05726];
acetate [CPD:C00033]
Comment
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nalpha-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
History
EC 3.5.1.114 created 2013
Orthology
K18458  N-acyl-aromatic-L-amino acid amidohydrolase
Genes
HSA: 91703(ACY3)
PTR: 451373(ACY3)
PPS: 100992485(ACY3)
GGO: 101144518(ACY3)
PON: 100454588(ACY3)
NLE: 100581974(ACY3)
MCC: 711083(ACY3)
MCF: 102123426(ACY3)
RRO: 104664723(ACY3)
RBB: 108518683(ACY3)
CJC: 103796426(ACY3)
SBQ: 101028900(ACY3)
MMU: 71670(Acy3)
MCAL: 110285586(Acy3)
MPAH: 110332220(Acy3)
RNO: 293653(Acy3)
MUN: 110547162(Acy3)
CGE: 100763612(Acy3)
NGI: 103725050
HGL: 101725542(Acy3)
CCAN: 109692320(Acy3)
TUP: 102503277(ACY3)
CFA: 100683126(ACY3)
ORO: 101362499(ACY3)
FCA: 101083207(ACY3)
PTG: 102970090(ACY3)
PPAD: 109246993(ACY3)
BACU: 103009750(ACY3)
LVE: 103079001(ACY3)
OOR: 101270966(ACY3)
DLE: 111184037(ACY3)
PCAD: 102979768
ECB: 102149799(ACY3)
EPZ: 103544301
MYB: 102254475(ACY3) 102254790
MYD: 102764000(ACY3)
MNA: 107537402(ACY3)
HAI: 109384127(ACY3)
DRO: 112317043(ACY3)
PALE: 102895489(ACY3)
RAY: 107503948(ACY3)
LAV: 100668205(ACY3)
MDO: 100013740(ACY3)
SHR: 100933605(ACY3)
PCW: 110195585(ACY3)
OAA: 100680665(ACY3)
ASN: 102373930(ACY3)
AMJ: 102567904(ACY3)
PSS: 102461093(ACY3)
CMY: 102932193
CPIC: 101949865(ACY3)
ACS: 100558126(acy3)
PVT: 110085674(ACY3)
PBI: 103058598(ACY3)
PMUR: 107293628(ACY3)
TSR: 106538901(ACY3)
PMUA: 114602141(ACY3)
XLA: 779340(acy3.L)
XTR: 595015(acy3)
NPR: 108791080 108797385(ACY3)
DRE: 436619(acy3.2) 791456(acy3.1)
OLA: 101159859
CSEM: 103383512
SASA: 100194544(acy3) 106577455 106609950(ACY3)
EPA: 110237552
PDAM: 113674876
SPIS: 111333775
SMIN: v1.2.033226.t1(symbB.v1.2.033226.t1) v1.2.039538.t1(symbB.v1.2.039538.t1)
SPAR: SPRG_00693
VAG: N646_4536
NIS: NIS_0887
LBO: LBWT_610
MAR: MAE_01890
CALH: IJ00_18430
FSC: FSU_0931
 » show all
Reference
1  [PMID:14656720]
  Authors
Pushkin A, Carpenito G, Abuladze N, Newman D, Tsuprun V, Ryazantsev S, Motemoturu S, Sassani P, Solovieva N, Dukkipati R, Kurtz I
  Title
Structural characterization, tissue distribution, and functional expression of murine aminoacylase III.
  Journal
Am J Physiol Cell Physiol 286:C848-56 (2004)
DOI:10.1152/ajpcell.00192.2003
  Sequence
[mmu:71670]
Reference
2  [PMID:17012540]
  Authors
Newman D, Abuladze N, Scholz K, Dekant W, Tsuprun V, Ryazantsev S, Bondar G, Sassani P, Kurtz I, Pushkin A
  Title
Specificity of aminoacylase III-mediated deacetylation of mercapturic acids.
  Journal
Drug Metab Dispos 35:43-50 (2007)
DOI:10.1124/dmd.106.012062
  Sequence
[mmu:71670]
Reference
3  [PMID:19362172]
  Authors
Tsirulnikov K, Abuladze N, Newman D, Ryazantsev S, Wolak T, Magilnick N, Koag MC, Kurtz I, Pushkin A
  Title
Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel.
  Journal
Biochim Biophys Acta 1794:1049-57 (2009)
DOI:10.1016/j.bbapap.2009.03.022
Reference
4  [PMID:20921362]
  Authors
Hsieh JM, Tsirulnikov K, Sawaya MR, Magilnick N, Abuladze N, Kurtz I, Abramson J, Pushkin A
  Title
Structures of aminoacylase 3 in complex with acetylated substrates.
  Journal
Proc Natl Acad Sci U S A 107:17962-7 (2010)
DOI:10.1073/pnas.1006687107
  Sequence
[mmu:71670]
Reference
5  [PMID:22819785]
  Authors
Tsirulnikov K, Abuladze N, Bragin A, Faull K, Cascio D, Damoiseaux R, Schibler MJ, Pushkin A
  Title
Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal.
  Journal
Toxicol Appl Pharmacol 263:303-14 (2012)
DOI:10.1016/j.taap.2012.07.002
  Sequence
[rno:293653]
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.114
IUBMB Enzyme Nomenclature: 3.5.1.114
ExPASy - ENZYME nomenclature database: 3.5.1.114
BRENDA, the Enzyme Database: 3.5.1.114

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