کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1317649 | 976558 | 2006 | 26 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins](/preview/png/1317649.png)
Mononuclear non-heme ferrous iron dependent oxygenases and oxidases constitute an extended enzyme family that catalyze a wide range of oxidation reactions. The largest known sub-group employs 2-oxoglutarate as a cosubstrate and catalysis by these and closely related enzymes is proposed to proceed via a ferryl intermediate coordinated to the active site via a conserved HXD/E … H motif. Crystallographic studies on the 2-oxoglutarate oxygenases and related enzymes have revealed a common double-stranded β-helix core fold that supports the residues coordinating the iron. This fold is common to proteins of the cupin and the JmjC transcription factor families. The crystallographic studies on 2-oxoglutarate oxygenases and closely related enzymes are reviewed and compared with other metallo-enzymes/related proteins containing a double-stranded β-helix fold. Proposals regarding the suitability of the active sites and folds of the 2-oxoglutarate oxygenases to catalyze reactions involving reactive oxidizing species are described.
Journal: Journal of Inorganic Biochemistry - Volume 100, Issue 4, April 2006, Pages 644–669