Category:Human 2OG oxygenases

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Human Alpha-ketoglutarate-dependent hydroxylases are involved in a wide range of biological and medicinal processes.[1][2] Enzymes of the family of Fe(II) and 2OG-dependent oxygenases couple the oxidation of their prime substrate to that of 2OG. Structurally, they share a common double-stranded beta-helix (DSBH) fold and coordinate Fe(II) by a conserved HXD/E...H triad.[3]

  1. ^ Hausinger RP (January–February 2004). "Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes". Crit. Rev. Biochem. Mol. Biol. 39 (1): 21–68. doi:10.1080/10409230490440541. PMID 15121720.
  2. ^ Loenarz, C.; Schofield, C. J. (2008). "Expanding chemical biology of 2-oxoglutarate oxygenases". Nat Chem Biol. 4 (3): 152–156. doi:10.1038/nchembio0308-152. PMID 18277970.
  3. ^ Clifton, I. J.; McDonough, M. A.; Ehrismann, D.; Kershaw, N. J.; Granatino, N.; Schofield, C. J. (2006). "Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins". J Inorg Biochem. 100 (4): 644–669. doi:10.1016/j.jinorgbio.2006.01.024. PMID 16513174.

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