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Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.
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- Author(s): Mantri M;Mantri M; Zhang Z; McDonough MA; Schofield CJ
- Source:
The FEBS journal [FEBS J] 2012 May; Vol. 279 (9), pp. 1563-75. Date of Electronic Publication: 2012 Feb 20.
- Publication Type:
Journal Article; Review
- Language:
English
- Additional Information
- Source:
Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1742-4658 (Electronic) Linking ISSN: 1742464X NLM ISO Abbreviation: FEBS J Subsets: MEDLINE
- Publication Information:
Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005-
- Subject Terms:
- Abstract:
Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase).
(© 2012 The Authors Journal compilation © 2012 FEBS.)
- Accession Number:
0 (Ferrous Compounds)
0 (Ketoglutaric Acids)
0 (Repressor Proteins)
EC 1.- (Mixed Function Oxygenases)
EC 1.13.- (Oxygenases)
EC 1.14.11.- (2,4-dichlorophenoxyacetate-alpha-ketoglutarate dioxygenase)
EC 1.14.11.- (HIF1AN protein, human)
EC 1.4.- (Amino Acid Oxidoreductases)
EC 1.4.3.- (1-aminocyclopropane-1-carboxylic acid oxidase)
- Publication Date:
Date Created: 20120119 Date Completed: 20120611 Latest Revision: 20181201
- Publication Date:
20240829
- Accession Number:
10.1111/j.1742-4658.2012.08496.x
- Accession Number:
22251775
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