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| Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins |
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| Author(s): Clifton IJ, McDonough MA, Ehrismann D, Kershaw NJ, Granatino N, Schofield CJ |
| Source: JOURNAL OF INORGANIC BIOCHEMISTRY Volume: 100 Issue: 4 Pages: 644-669 Published: APR 2006 |
| Times Cited: 73 References: 157 |
| Abstract: 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 P-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 beta-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. (c) 2006 Elsevier Inc. All rights reserved. |
| Document Type: Review |
| Language: English |
| Reprint Address: Schofield, CJ (reprint author), Univ Oxford, Oxford Ctr Mol Sci, Mansfield Rd, Oxford OX1 3TA, England |
Addresses:
1. Univ Oxford, Oxford Ctr Mol Sci, Oxford OX1 3TA, England
2. Univ Oxford, Dept Chem, Chem Res Lab, Oxford OX1 3TA, England |
| Publisher: ELSEVIER SCIENCE INC, 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA |
| Subject Category: Biochemistry & Molecular Biology; Chemistry, Inorganic & Nuclear |
| IDS Number: 046RP |
| ISSN: 0162-0134 |
| DOI: 10.1016/j.jinorgbio.2006.01.024 |
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