Photoaffinity labelling of the 2-oxoglutarate binding site of prolyl 4-hydroxylase with 5-azidopyridine-2-carboxylic acid
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference23 articles.
1. A stereochemical concept for the catalytic mechanism of prolylhydroxylase
2. α-Ketoglutarate dependent dioxygenases: A mechanism for prolyl hydroxylase action
3. Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction
4. Mechanism of the Prolyl Hydroxylase Reaction. 1. Role of Co-substrates
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1. 5-Azido-2-aminopyridine, a New Nitrene/Nitrenium Ion Photoaffinity Labeling Agent That Exhibits Reversible Intersystem Crossing between Singlet and Triplet Nitrenes;Journal of the American Chemical Society;2013-12-13
2. Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4-Hydroxylases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Chemical reagents in photoaffinity labeling;Tetrahedron;1995-11
4. Procollagen-proline dioxygenase;Enzyme Handbook;1994
5. Interaction of prolyl 4-hydroxylase with synthetic peptide substrates. A conformational model for collagen proline hydroxylation.;Journal of Biological Chemistry;1991-02
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