Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.

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 vi...

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Main Authors: Clifton, I, McDonough, M, Ehrismann, D, Kershaw, N, Granatino, N, Schofield, C
Format: Journal article
Language:English
Published: 2006
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author Clifton, I
McDonough, M
Ehrismann, D
Kershaw, N
Granatino, N
Schofield, C
author_facet Clifton, I
McDonough, M
Ehrismann, D
Kershaw, N
Granatino, N
Schofield, C
author_sort Clifton, I
collection OXFORD
description 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 beta-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.
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spelling oxford-uuid:594c90c9-7b90-4c99-bf11-722964c8309e2022-03-26T17:08:57ZStructural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:594c90c9-7b90-4c99-bf11-722964c8309eEnglishSymplectic Elements at Oxford2006Clifton, IMcDonough, MEhrismann, DKershaw, NGranatino, NSchofield, CMononuclear 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 beta-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.
spellingShingle Clifton, I
McDonough, M
Ehrismann, D
Kershaw, N
Granatino, N
Schofield, C
Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title_full Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title_fullStr Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title_full_unstemmed Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title_short Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
title_sort structural studies on 2 oxoglutarate oxygenases and related double stranded beta helix fold proteins
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