| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10763933 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Abstract
⺠Human PHYHD1A has the double-stranded β-helix fold and Fe(II) and cosubstrate binding residues characteristic of the 2-oxoglutarate dependent oxygenases. ⺠Human PHYHD1A catalyzes the conversion of 2-oxoglutarate to succinate and CO2 in an iron-dependent manner. ⺠The PHYHD1 B and C isoforms are likely not active as 2OG oxygenases. ⺠PHYHD1 does not catalyze the hydroxylation of phytanoyl-CoA unlike its closest homologue PAHX.
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Authors
Zhihong Zhang, Grazyna T. Kochan, Stanley S. Ng, Kathryn L. Kavanagh, Udo Oppermann, Christopher J. Schofield, Michael A. McDonough,