Coenzyme-B12 -dependent enzyme reactions: A spectrophotometric rapid kinetic study of ethanolamine ammonia-lyase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)80018-4/fullpdf
Reference18 articles.
1. Coenzyme B12-dependent enzyme reactions I. Emission mössbauer spectroscopic study of ethanolamine-ammonia lyase a coenzyme B12-dependent enzyme
2. Detection of intermediates during the conversion of propane-1,2-diol to propionaldehyde by glycerol dehydrase, a coenzyme B12-dependent reaction
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1. Magnetic Field Effect Studies Indicate Reduced Geminate Recombination of the Radical Pair in Substrate-Bound Adenosylcobalamin-Dependent Ethanolamine Ammonia Lyase;Journal of the American Chemical Society;2007-11-28
2. The Number of Functional Active Sites per Molecule of the Adenosylcobalamin-Dependent Enzyme, Ethanolamine Ammonia-lyase, as Determined by a Kinetic Method;European Journal of Biochemistry;2005-03-03
3. Theoretical studies of coenzyme B12-dependent carbon-skeleton rearrangements;Theoretical and Computational Chemistry;2001
4. The Chemistry and Enzymology of Cobalamin-dependent Enzymes;Comprehensive Natural Products Chemistry;1999
5. Use of magnetic field effects to study coenzyme B12-dependent reactions;Methods in Enzymology;1997
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