Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA hydroxylase.

Journal article

Phytanoyl-CoA hydroxylase (PAHX) catalyzes an important step in the metabolism of the fatty acid side chain of chlorophyll. PHYHD1 exists in three isoforms and is the closest human homologue of PAHX. We show that like PAHX, the PHYHD1A but likely not the PHYHD1B/C isoforms, is a functional Fe(II) and 2-oxoglutarate (2OG) dependent oxygenase. Crystallographic and biochemical analyses reveal that PHYHD1A has the double-stranded β-helix fold and Fe(II) and cosubstrate binding residues characteri...

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Authors: Zhang, Z; Kochan, G; Ng, S; Kavanagh, K; Oppermann, U

• Publication status: Published
• Journal: Biochemical and biophysical research communications
• Volume: 408
• Issue: 4
• Pages: 553-558
• Publication date: 2011-05-01
• DOI: 10.1016/j.bbrc.2011.04.059
• EISSN: 1090-2104
• ISSN: 0006-291X
• Language: English
• Keywords: Humans; Crystallography, X-Ray; Mixed Function Oxygenases; Protein Structure, Secondary; Oxygenases; Iron; Phosphorylation; Protein Processing, Post-Translational