ETFA
Electron-transfer-flavoprotein, alpha polypeptide (glutaric aciduria II), also known as ETFA, is a protein which in humans is encoded by the ETFA gene.[1]
ETFA participates in catalyzing the initial step of the mitochondrial fatty acid beta oxidation. It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. Defects in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.[1]
References
Further reading
- Frerman FE (1988). “Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase”. Biochem. Soc. Trans. 16 (3): 416–8. PMID 3053288.
- Freneaux E, Sheffield VC, Molin L, et al. (1992). “Glutaric acidemia type II. Heterogeneity in beta-oxidation flux, polypeptide synthesis, and complementary DNA mutations in the alpha subunit of electron transfer flavoprotein in eight patients”. J. Clin. Invest. 90 (5): 1679–86. doi:10.1172/JCI116040. PMC 443224. PMID 1430199.
- Indo Y, Glassberg R, Yokota I, Tanaka K (1991). “Molecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II–and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstable mature protein in a patient”. Am. J. Hum. Genet. 49 (3): 575–80. PMC 1683153. PMID 1882842.
- Finocchiaro G, Ito M, Ikeda Y, Tanaka K (1988). “Molecular cloning and nucleotide sequence of cDNAs encoding the alpha-subunit of human electron transfer flavoprotein”. J. Biol. Chem. 263 (30): 15773–80. PMID 3170610.
- White RA, Dowler LL, Angeloni SV, Koeller DM (1996). “Assignment of Etfdh, Etfb, and Etfa to chromosomes 3, 7, and 13: the mouse homologs of genes responsible for glutaric acidemia type II in human”. Genomics. 33 (1): 131–4. doi:10.1006/geno.1996.0170. PMID 8617498.
- Roberts DL, Frerman FE, Kim JJ (1997). “Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution”. Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14355–60. doi:10.1073/pnas.93.25.14355. PMC 26136. PMID 8962055.
- Bross P, Pedersen P, Winter V, et al. (1999). “A polymorphic variant in the human electron transfer flavoprotein alpha-chain (alpha-T171) displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with mild childhood presentation”. Mol. Genet. Metab. 67 (2): 138–47. doi:10.1006/mgme.1999.2856. PMID 10356313.
- Jones M, Talfournier F, Bobrov A, et al. (2002). “Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein”. J. Biol. Chem. 277 (10): 8457–65. doi:10.1074/jbc.M111105200. PMID 11756429.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Olsen RK, Andresen BS, Christensen E, et al. (2003). “Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation deficiency”. Hum. Mutat. 22 (1): 12–23. doi:10.1002/humu.10226. PMID 12815589.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). “Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes”. Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Schiff M, Froissart R, Olsen RK, et al. (2006). “Electron transfer flavoprotein deficiency: functional and molecular aspects”. Mol. Genet. Metab. 88 (2): 153–8. doi:10.1016/j.ymgme.2006.01.009. PMID 16510302.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Chiong MA, Sim KG, Carpenter K, et al. (2007). “Transient multiple acyl-CoA dehydrogenation deficiency in a newborn female caused by maternal riboflavin deficiency”. Mol. Genet. Metab. 92 (1–2): 109–14. doi:10.1016/j.ymgme.2007.06.017. PMID 17689999.
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