Entry
Name
N-(long-chain-acyl)ethanolamine deacylase;
NAAA (gene name);
N-acylethanolamine amidohydrolase;
acylethanolamine amidase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
N-(long-chain-acyl)ethanolamine amidohydrolase
Reaction(IUBMB)
N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine [RN:
R02041 ]
Reaction(KEGG)
Substrate
N-(long-chain-acyl)ethanolamine [CPD:
C04080 ];
H2O [CPD:
C00001 ]
Product
long-chain carboxylate [CPD:
C00347 ];
ethanolamine [CPD:
C00189 ]
Comment
This lysosomal enzyme acts best on palmitoyl ethanolamide, with lower activity on other N-(long-chain-acyl)ethanolamines. It is only active at acidic pH. Unlike EC
3.5.1.99 , fatty acid amide hydrolase, it does not act on primary amides such as oleamide, and has only a marginal activity with anandamide. The enzyme is translated as an inactive proenzyme, followed by autocatalytic cleavage into two subunits that reassociate to form an active heterodimeric complex.
History
EC 3.5.1.60 created 1989, modified 2019
Orthology
K13720 N-(long-chain-acyl)ethanolamine deacylase
Genes
MDO : 100024418 100024438(NAAA)
GAS : 123251099(NAAA) 123252185
PCW : 110209778(NAAA) 110209855
PRAF : 128421503 128421504
XLA : 379721(naaal.L) 447407(naaa.L)
XTR : 105945457 448239(naaa)
RTEM : 120916545 120916550
MUO : 115458875 115461084(NAAA)
SANH : 107699746 107703218
CCAR : 109056132 109087861 109091043 109096511
CAUA : 113049647 113080901
CGIB : 127958216 127998243
SMEO : 124380789 124380790
PRET : 103465513 103465514
PFOR : 103147313 103147343
PLAI : 106963034 106963035
PMEI : 106928993 106929004
PPRL : 129358208 129358209
CVG : 107082339 107095639(naaa)
CTUL : 119786643 119790775
GMU : 124856925 124856926 124857233
SASA : 106585383 106585736
PKI : 111839351 111839373 111839374
ARUT : 117408605 117963630
SCLV : 120339486 120342616 120343018 120343494 120343495
SKO : 102805521 102805630 102808278
CEL : CELE_Y55D5A.3(Y55D5A.3)
LGI : LOTGIDRAFT_169146 LOTGIDRAFT_84289
PVUL : 126827845 126828231
GAE : 121369748 121370541 121372582 121377994
MMER : 123551808 123551809
RPHI : 132720535 132724057
AQU : 100632037 100638703 100641855 105315877
MPP : MICPUCDRAFT_19562(JGI:MicpuC2_19562)
MBR : MONBRDRAFT_1488 MONBRDRAFT_5578
SRE : PTSG_05656 PTSG_05669
TET : TTHERM_00213580 TTHERM_00657610
PTM : GSPATT00004243001 GSPATT00004244001 GSPATT00006883001 GSPATT00028435001 GSPATT00035774001 GSPATT00035775001
SMIN : v1.2.000929.t1(symbB.v1.2.000929.t1) v1.2.007250.t1(symbB.v1.2.007250.t1)
» show all
Taxonomy
Reference
Authors
Ueda N, Yamanaka K, Yamamoto S
Title
Purification and characterization of an acid amidase selective for N-palmitoylethanolamine, a putative endogenous anti-inflammatory substance.
Journal
Reference
Authors
Ueda N, Yamanaka K, Terasawa Y, Yamamoto S
Title
An acid amidase hydrolyzing anandamide as an endogenous ligand for cannabinoid receptors.
Journal
Reference
Authors
West JM, Zvonok N, Whitten KM, Wood JT, Makriyannis A
Title
Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase.
Journal
Reference
Authors
Zhao LY, Tsuboi K, Okamoto Y, Nagahata S, Ueda N
Title
Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.60
ExPASy - ENZYME nomenclature database: 3.5.1.60