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Literature summary for 3.5.1.99 extracted from

  • Patricelli, M.P.; Lashuel, H.A.; Giang, D.K.; Kelly, J.W.; Cravatt, B.F.
    Comparative characterization of wild type and transmembrane domain-deleted fatty acid amide hydrolase identification of the transmembrane domain as a site for oligomerization (1998), Biochemistry, 37, 15177-15187.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain, expression in COS-7 cells and in Escherichia coli Rattus norvegicus

General Stability

General Stability Organism
100 mM Na2CO3 incubation (30 min at 4°C and pH 11.0) destroys the catalytic activity of both wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain derived from transfected COS-7 cells, whereas the native liver-isolated FAAH is stable to this treatment Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
oleamide pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain Rattus norvegicus
0.023
-
oleamide pH 9.0, recombinantly expressed wild-type enzyme Rattus norvegicus
0.031
-
oleamide pH 9.0, rat liver FAAH Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein Rattus norvegicus 16020
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinantly expressed wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oleamide + H2O
-
Rattus norvegicus oleic acid + NH3
-
?

Subunits

Subunits Comment Organism
oligomer wild-type FAAH behaves as a larger oligomer than FAAH protein lacking the N-terminal transmembrane domain. Presence of SDS-resistant oligomers for wild-type FAAH, but not for FAAH protein lacking the N-terminal transmembrane domain. Self-association through the transmembrane domain is demonstrated Rattus norvegicus

Synonyms

Synonyms Comment Organism
FAAH
-
Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.3
-
oleamide pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain Rattus norvegicus
7.1
-
oleamide pH 9.0, recombinantly expressed wild-type enzyme Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
native and recombinant enzymes Rattus norvegicus