Coenzyme Binding and Co-operativity in d-Glyceraldehyde 3-Phosphate Dehydrogenase
Author:
Affiliation:
1. 1M.R.C. Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, U.K.
2. 2M.R.C. Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, U.K.
Publisher
Portland Press Ltd.
Subject
Biochemistry
Link
https://portlandpress.com/biochemsoctrans/article-pdf/5/3/647/553185/bst0050647.pdf
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2. Affinity Labeling of Glyceraldehyde-3-phosphate Dehydrogenase from Sturgeon and Bacillus stearothermophilus by 3-Chloroacetylpyridine-adenine Dinucleotide;European Journal of Biochemistry;2005-03-03
3. Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus;Journal of Molecular Biology;1988-10
4. Structural and Functional Aspects of Domain Motions in Proteins;Critical Reviews in Biochemistry;1984-01
5. NAD+ analogue binding to glyceraldehyde-3-phosphate dehydrogenase;European Journal of Biochemistry;1983-12
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