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Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.

Abstract:

Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes including the hydroxylation of proline and lysine residues during the post-translational modification of collagen. 2-OG oxygenases commonly require ascorbate for full activity. In the vitamin C deficient disease, scurvy, reduced activity of 2-OG oxygenases results in impaired formation of collagen. Here we report the crystal structure of bacterial proline 3-hydroxylase from Stre...

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Publication status:
Published

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Authors


Clifton, IJ More by this author
Baldwin, JE More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
European journal of biochemistry / FEBS
Volume:
268
Issue:
24
Pages:
6625-6636
Publication date:
2001-12-05
DOI:
EISSN:
1432-1033
ISSN:
0014-2956
URN:
uuid:2aaa71f5-41f7-43dc-8aee-5ff7f86c60d8
Source identifiers:
32007
Local pid:
pubs:32007

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