KEGG   ENZYME: 3.5.1.114Help
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
BRITE hierarchy
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)
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)
CJC: 
103796426(ACY3)
SBQ: 
101028900(ACY3)
MMU: 
71670(Acy3)
RNO: 
293653(Acy3)
CGE: 
100763612(Acy3)
NGI: 
HGL: 
101725542(Acy3)
TUP: 
102503277(ACY3)
FCA: 
101083207(ACY3)
PTG: 
102970090(ACY3)
BACU: 
103009750(ACY3)
LVE: 
103079001(ACY3)
MYB: 
MYD: 
102764000(ACY3)
HAI: 
109384127(ACY3)
PALE: 
102895489(ACY3)
LAV: 
100668205(ACY3)
MDO: 
100013740(ACY3)
SHR: 
100933605(ACY3)
ASN: 
102373930(ACY3)
AMJ: 
102567904(ACY3)
PSS: 
102461093(ACY3)
CMY: 
CPIC: 
101949865(ACY3)
ACS: 
100558126(acy3)
PBI: 
103058598(ACY3)
XLA: 
779340(acy3.L)
XTR: 
595015(acy3)
DRE: 
436619(acy3.2) 791456(acy3.1)
IPU: 
TRU: 
TNG: 
LCO: 
MZE: 
OLA: 
XMA: 
SASA: 
LCM: 
AAF: 
EHX: 
 » show all
Taxonomy
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 (2004) C848-56.
  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 (2007) 43-50.
  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 (2009) 1049-57.
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 (2010) 17962-7.
  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 (2012) 303-14.
  Sequence
[rno:293653]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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