Hidrolaza masno kiselinskih amida
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| Hidrolaza masno kiselinskih amida | |
|---|---|
| |
| Hidrolaza masno kiselinskih amida (FAAH) dimer je prikazan sa kovalentnim inhibitorom (MAFP, žuto) vezanim za aktivno mesto. | |
| Identifikatori | |
| Simbol | FAAH |
| Entrez | 2166 |
| Hugo | 3553 |
| OMIM | 602935 |
| PDB | 1MT5 |
| RefSek | NM_001441 |
| UniProt | O00519 |
| Drugi podaci | |
| EC broj | 3.5.1.- |
| Lokus | Hrom. 1 p35-p34 |
Hidrolaza masno kiselinskih amida (EC 3.5.1.99, FAAH, oleamidna hidrolaza, anandamidna amidohidrolaza) je član enzimske familije serinskih hidrolaza. Kod čoveka je ova hidrolaza kodirana FAAH genom. FAAH je kloniran 1996 Ben Kravat et al. na Skripsovom Istraživačkom Institutu (engl. The Scripps Research Institut).[1][2][3] FAAH kristalna struktura je bila rešena u istoj laboratoriji 2002.[3]
Funkcija[uredi | uredi kod]
FAAH je integralna membranska hidrolaza sa jednim N-terminalnim transmembranskim domenom. In vitro, FAAH ima esterazno i amidazno dejstvo.[4] In vivo, FAAH je principalni katabolički enzim za klasu bioaktivnih lipida poznatih kao amidi masnih kiselina (FAA). Članovi FAA familije su:
- Anandamid (N-arahidonoole tanolamin), endokanabinoid[5]
- Drugi N-aciletanolamini, kao što tu N-oleoiletanolamin i N-palmitoiletanolamin[6]
Vidi još[uredi | uredi kod]
Literatura[uredi | uredi kod]
- ↑ Cravatt BF, Giang DK, Mayfield SP, Boger DL, Lerner RA, Gilula NB (November 1996). „Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides”. Nature 384 (6604): 83–7. DOI:10.1038/384083a0. PMID 8900284.
- ↑ Giang DK, Cravatt BF (March 1997). „Molecular characterization of human and mouse fatty acid amide hydrolases”. Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2238–42. DOI:10.1073/pnas.94.6.2238. PMC 20071. PMID 9122178.
- ↑ 3,0 3,1 Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (2002). „Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling”. Science 298 (5599): 1793–6. DOI:10.1126/science.1076535. PMID 12459591. Greška u referenci: Nevaljana oznaka
<ref>; naziv "pmid12459591" je zadan više puta s različitim sadržajem - ↑ Patricelli MP, Cravatt BF (October 1999). „Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism”. Biochemistry 38 (43): 14125–30. DOI:10.1021/bi991876p. PMID 10571985.
- ↑ Cravatt BF, Demarest K, Patricelli MP, Bracey MH, Giang DK, Martin BR, Lichtman AH (July 2001). „Supersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolase”. Proc. Natl. Acad. Sci. U.S.A. 98 (16): 9371–6. DOI:10.1073/pnas.161191698. PMC 55427. PMID 11470906.
- ↑ Saghatelian A, Trauger SA, Want EJ, Hawkins EG, Siuzdak G, Cravatt BF (November 2004). „Assignment of endogenous substrates to enzymes by global metabolite profiling”. Biochemistry 43 (45): 14332–9. DOI:10.1021/bi0480335. PMID 15533037.
- ↑ Cravatt BF, Prospero-Garcia O, Siuzdak G, Gilula NB, Henriksen SJ, Boger DL, Lerner RA (June 1995). „Chemical characterization of a family of brain lipids that induce sleep”. Science (journal) 268 (5216): 1506–9. PMID 7770779.
- ↑ Saghatelian A, McKinney MK, Bandell M, Patapoutian A, Cravatt BF (August 2006). „A FAAH-regulated class of N-acyl taurines that activates TRP ion channels”. Biochemistry 45 (30): 9007–15. DOI:10.1021/bi0608008. PMID 16866345.