Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii. Evidence for High Structural Similarity with the Lipoyl Domain of the Pyruvate Dehydrogenase Complex
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.148_c.x/fullpdf
Reference50 articles.
1. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
2. Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
3. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
4. Toward complete 1H NMR spectra in proteins
5. Three-dimensional Structure of the Lipoyl domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex
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1. Role of Lipoyl Domains in the Function and Regulation of Mammalian Pyruvate Dehydrogenase Complex;Oxidative Stress and Disease;2008-03-17
2. Reaction Mechanism for Mammalian Pyruvate Dehydrogenase Using Natural Lipoyl Domain Substrates;Archives of Biochemistry and Biophysics;2001-02
3. Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex;Journal of Molecular Biology;2001-01
4. Specificity Determinants for the Pyruvate Dehydrogenase Component Reaction Mapped with Mutated and Prosthetic Group Modified Lipoyl Domains;Journal of Biological Chemistry;2000-05
5. Structure and selectivity in post-translational modification: attaching the biotinyl–lysine and lipoyl–lysine swinging arms in multifunctional enzymes;The EMBO Journal;1999-05-17
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