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Information on EC 3.5.1.4 - amidase and Organism(s) Mus musculus and UniProt Accession Q9D7V9

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.4 amidase
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This record set is specific for:
Mus musculus
UNIPROT: Q9D7V9 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
amidase, deaminase, acylase, acetamidase, amide hydrolase, acid transferase, n-acylethanolamine acid amidase, n-acylethanolamine-hydrolyzing acid amidase, atfaah, acylamidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-acylethanolaminehydrolyzing acid amidase
-
acid transferase
-
-
-
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acylamidase
-
-
-
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acylase
-
-
-
-
amide hydrolase
-
-
-
-
amide transferase
-
-
-
-
amidohydrolase
-
-
-
-
deaminase
-
-
-
-
ester transferase
-
-
-
-
FAAH
-
-
fatty acid amide hydrolase
-
-
fatty acid amide hydrolase 1
-
N-acetylaminohydrolase
-
-
-
-
Wide spectrum amidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic acid amide
-
-
-
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transfer of amide group
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-
-
-
transfer of acyl group
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acylamide amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9012-56-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
anandamide + H2O
arachidonic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: N-palmitoylethanolamine, N-oleoylethanolamine, anandamide
-
-
?
N-oleoylethanolamine + H2O
oleic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: N-palmitoylethanolamine, N-oleoylethanolamine, anandamide
-
-
?
N-palmitoylethanolamine + H2O
palmitic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: N-palmitoylethanolamine, N-oleoylethanolamine, anandamide
-
-
?
2-arachidonoylglycerol + H2O
?
show the reaction diagram
-
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: anandamide, N-oleoylethanolamine, N-palmitoylethanolamine
-
-
?
N-oleoylethanolamine + H2O
oleic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: anandamide, N-oleoylethanolamine, N-palmitoylethanolamine
-
-
?
N-palmitoylethanolamine + H2O
palmitic acid + ethanolamine
show the reaction diagram
substrates in order of decreasing activity: anandamide, N-oleoylethanolamine, N-palmitoylethanolamine
-
-
?
additional information
?
-
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
additional information
?
-
-
FAAH is a key regulator in the development of ethanol dependence
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-(cyclohexylcarbonyl)pentadecylamine
-
3'-{[(E)-(cyclohexylimino)(hydroxy)methyl]oxy}biphenyl-3-carboximidic acid
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the inhibitor markedly increases the preference for ethanol. The inhibitor specifically acts through FAAH
DNA containing thymine glycol
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
activates
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAAA_MOUSE
362
1
40075
Swiss-Prot
other Location (Reliability: 3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
down-regulated state of FAAH - through its effects on CB1 and opioid receptor in the brain reward circuitry - promotes ethanol drinking behavior. Manipulation of the FAAH activity might represent a novel therapeutic target for the treatment of ethanol dependence
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsuboi, K.; Takezaki, N.; Ueda, N.
The N-acylethanolamine-hydrolyzing acid amidase (NAAA)
Chem. Biodivers.
4
1914-1925
2007
Homo sapiens (O00519), Homo sapiens (Q02083), Homo sapiens, Mus musculus (O08914), Mus musculus (Q9D7V9), Mus musculus, Rattus norvegicus (P97612), Rattus norvegicus (Q5KTC7), Sus scrofa (Q9TUI8)
Manually annotated by BRENDA team
Vinod, K.Y.; Sanguino, E.; Yalamanchili, R.; Manzanares, J.; Hungund, B.L.
Manipulation of fatty acid amide hydrolase functional activity alters sensitivity and dependence to ethanol
J. Neurochem.
104
233-243
2008
Mus musculus
Manually annotated by BRENDA team