Entry
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
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
MYB : 102254475(ACY3) 102254790
NPR : 108791080 108797385(ACY3)
RTEM : 120909172(ACY3) 120926705
DRE : 436619(acy3.2) 791456(acy3.1)
SRX : 107714473 107719252 107746091 107746117 107757064
SANH : 107657988 107676738 107703715 107703856
SGH : 107570819 107570825 107571911 107572870 107575636
CCAR : 109045324 109065132 109065133 109112463(acy3)
CAUA : 113044079 113044751 113062648 113084557 113084558
CGIB : 127949056 127949057 128020508
PTET : 122342326 122342355
LROH : 127159455 127165008 127165036
OMC : 131543402 131549411 131549601
PPRM : 120480155 120489148
MAMB : 125264089 125271860 125271861(acy3.2)
CIDE : 127510440 127510448 127516661
MASI : 127443795 127445050
PHYP : 113524540 113545754
SMEO : 124381101 124381703
AMEX : 103024465 103026039
CMAO : 118804195 118816901
CHAR : 105902167 105912884
TNG : GSTEN00011466G001 GSTEN00033497G001
TBEN : 117481706 117488050
PGEO : 117447460 117447506 117464103
GACU : 117537755 117552773
EMAC : 134864629 134876134
PLEP : 121942252 121961819
SLUC : 116034328 116049044
ECRA : 117934689 117955546
PFLV : 114545402 114568528
PPUG : 119218282 119222729
CLUM : 117738085 117747626 117747627 117747628 117747629 117747630 117747631
PSWI : 130189671 130211905
MSAM : 119898960 119913073
SCHU : 122870550 122872968
ALAT : 119020527 119027849
OML : 112156043 112157362(acy3.2)
CSAI : 133420069 133434752
PRET : 103466257 103480428
PFOR : 103137475 103137811 103137813 103148456
PLAI : 106948229 106948230 106949604 106958436
PMEI : 106919317 106931340
GAF : 122819991 122829907(acy3.2)
PPRL : 129354913 129366906
CTUL : 119796250 119799302
ALIM : 106517035 106525346
AOCE : 111567147 111583230
SSEN : 122767038 122770931
HHIP : 117751997 117766206
SMAU : 118286733 118312048
SLAL : 111670415 111673487
PTAO : 133472969 133477223
BPEC : 110159468 110165380
MALB : 109961401 109974273
BSPL : 114857624 114865726
SASA : 100194544(acy3) 106577455 106609950(ACY3)
STRU : 115183052 115191931 115202117
OTW : 112231784 112261060 112261397
OMY : 110497470 110531924 110534382
OGO : 124001891 124008767 124012125
ONE : 115137305 115138221 115145856
OKI : 109894170 109901108 109906771
OKE : 118362944 118369290 118395404
SALP : 111958486 111962015 112072352
SNH : 120030135 120034913 120052833
CCLU : 121550400 121554417
AANG : 118227937 118231297
PSPA : 121302115 121320145
PSEX : 120538191 120538192
SMIN : v1.2.033226.t1(symbB.v1.2.033226.t1) v1.2.039538.t1(symbB.v1.2.039538.t1)
EHX : EMIHUDRAFT_252071 EMIHUDRAFT_44278 EMIHUDRAFT_44328 EMIHUDRAFT_75471
MVZ : myaer102_17080 myaer102_36990
» show all
Taxonomy
Reference
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
Sequence
Reference
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
Sequence
Reference
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
Reference
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
Sequence
Reference
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
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 3.5.1.114