期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 100, 期 4, 页码 644-669出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2006.01.024
关键词
cupin; double stranded beta-helix; DSBH; iron coordination; JmjC; metallo-enzyme; non-heme iron; 2-oxoglutarate; oxygenase; protein structure
资金
- Biotechnology and Biological Sciences Research Council [B18672, BBS/B/07683] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [B18672, BBS/B/07683] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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.
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