Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.1.60 - N-(long-chain-acyl)ethanolamine deacylase and Organism(s) Oryctolagus cuniculus and UniProt Accession G1T7U7

for references in articles please use BRENDA:EC3.5.1.60
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Oryctolagus cuniculus
UNIPROT: G1T7U7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hnaaa, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acylethanolamine acid amidase
-
amidase, acylethanolamine
-
-
-
-
N-acylethanolamine amidohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-(long-chain-acyl)ethanolamine amidohydrolase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
99283-61-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-palmitoylethanolamide + H2O
palmitate + ethanolamine
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-palmitoylethanolamide + H2O
palmitate + ethanolamine
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-cyclohexylbutyl-N-[(S)-2-oxoazetidin-3-yl]carbamate
ARN726, enzyme-binding structure analysis. Nucleophilic attack on the carbonyl carbon of the strained beta-lactam moiety by the Cys126 side chain
additional information
NAAA inhibitors block the substrate-binding site
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
N-acylethanolamine acid amidase is expressed at high levels in immune cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
proposed membrane interactions via hydrophobic helices alpha3 and alpha6
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure analysis of the enzme in complex with myristate, substrate binding structure, overview. The enzyme must disrupt the membrane to reach its embedded substrate, and helices alpha3 and alpha6 are likely candidates for this function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAAA_RABIT
358
0
39877
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
enzyme NAAA adopts an alphabetabetaalpha-fold with a helical alpha-subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
self-proteolysis exposes the NAAA active site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme C116A mutant in complex with inhibitors ARN726, ARN19702, and with substrate myristate, and in presence of Triton X-100, X-ray diffraction structure determination and analysis at 2.7 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Spodoptera frugiperda Sf9 insect cells by nickel affinity chromatography, gel filtration, and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of enzyme NAAA in Spodoptera frugiperda Sf9 insect cells via baculovirus transfection method, the enzyme is secreted. The endogenous signal peptide is replaced by the melittin signal peptide MKFLVNVALVFMVVYISYIYA followed by a His6-tag DRHHHHHHKL. Construct encompasses residues 31-359 of NAAA of mouse enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gorelik, A.; Gebai, A.; Illes, K.; Piomelli, D.; Nagar, B.
Molecular mechanism of activation of the immunoregulatory amidase NAAA
Proc. Natl. Acad. Sci. USA
115
E10032-E10040
2018
Cavia porcellus (H0VCJ6), Homo sapiens (Q02083), Mus musculus (Q9D7V9), Oryctolagus cuniculus (G1T7U7)
Manually annotated by BRENDA team