Malate dehydrogenase, anticooperative NADH, and L-malate binding in ternary complexes with supernatant pig heart enzyme
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00686a031
Reference27 articles.
1. The binding of oxidized coenzymes by glutamate dehydrogenase and the effects of glutarate and purine nucleotides
2. Malate dehydrogenase, circular dichroism difference spectra of porcine heart mitochondrial and supernatant enzymes, binary enzyme-coenzyme, and ternary enzyme-coenzyme-substrate analog complexes.
3. Dehydrogenase-reduced coenzyme difference spectra, their resolution, and relation to the stereospecificity of hydrogen transfer
4. Kinetic studies on pig heart cytoplasmic malate dehydrogenase.
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5. Characterization of an Essential Histidine Residue in Thermophilic Malate Dehydrogenase;The Journal of Biochemistry;1986
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