Protein ETHE1, mitochondrial, also known as "ethylmalonic encephalopathy 1 protein" and "per sulfide dioxygenase", is aprotein that in humans is encoded by theETHE1gene located on chromosome 19.[5]
This gene encodes a protein that is expressed mainly in the gastrointestinal tract, but also in several other tissues such as the liver and the thyroid.[5]
The ETHE1 protein is thought to localize primarily to themitochondrial matrix[6][7] and functions as asulfur dioxygenase. Sulfur deoxygenates are proteins that function insulfur metabolism. The ETHE1 protein is thought to catalyze the following reaction:
Mutations in ETHE1gene are thought to causeethylmalonic encephalopathy,[7][9] a rareinborn error of metabolism. Patients carrying ETHE1 mutations have been found to exhibit lower activity of ETHE1 and affinity for the ETHE1 substrate.[8] Mouse models of Ethe1 genetic ablation likewise exhibited reduced sulfide dioxygenase catabolism and cranial features of ethylmalonic encephalopathy.[6] Decrease in sulfide dioxygenase activity results in abnormalcatabolism ofhydrogen sulfide, a gas-phase signaling molecule in the central nervous system,[8] whose accumulation is thought to inhibitcytochrome c oxidase activity in therespiratory chain of themitochondrion.[6] However, other metabolic pathways may also be involved that could exert a modulatory effect onhydrogen sulfide toxicity.[10]
^abcdTiranti V, Viscomi C, Hildebrandt T, Di Meo I, Mineri R, Tiveron C, Levitt MD, Prelle A, Fagiolari G, Rimoldi M, Zeviani M (2009). "Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy".Nat. Med.15 (2):200–5.doi:10.1038/nm.1907.hdl:11577/3321438.PMID19136963.S2CID5970257.
^Barth M, Ottolenghi C, Hubert L, Chrétien D, Serre V, Gobin S, Romano S, Vassault A, Sefiani A, Ricquier D, Boddaert N, Brivet M, de Keyzer Y, Munnich A, Duran M, Rabier D, Valayannopoulos V, de Lonlay P (2010). "Multiple sources of metabolic disturbance in ETHE1-related ethylmalonic encephalopathy".J. Inherit. Metab. Dis.33 (Suppl 3): S443–53.doi:10.1007/s10545-010-9227-y.PMID20978941.S2CID29056515.
^Higashitsuji H, Higashitsuji H, Nagao T, Nonoguchi K, Fujii S, Itoh K, Fujita J (Oct 2002). "A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis".Cancer Cell.2 (4):335–46.doi:10.1016/S1535-6108(02)00152-6.hdl:2433/148468.PMID12398897.
McCoy JG, Bingman CA, Bitto E, Holdorf MM, Makaroff CA, Phillips GN (Sep 2006). "Structure of an ETHE1-like protein from Arabidopsis thaliana".Acta Crystallographica Section D.62 (Pt 9):964–70.Bibcode:2006AcCrD..62..964M.doi:10.1107/S0907444906020592.PMID16929096.
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (Jan 2006)."The LIFEdb database in 2006".Nucleic Acids Research.34 (Database issue): D415-8.doi:10.1093/nar/gkj139.PMC1347501.PMID16381901.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID16189514.S2CID4427026.
Higashitsuji H, Higashitsuji H, Nagao T, Nonoguchi K, Fujii S, Itoh K, Fujita J (Oct 2002). "A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis".Cancer Cell.2 (4):335–46.doi:10.1016/S1535-6108(02)00152-6.hdl:2433/148468.PMID12398897.
