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Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.
The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the cofactor. This residue is highly conserved as aspartate in malate dehydrogenases, except i...
Tallennettuna:
| Päätekijät: | , , , , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
1995
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1136396/ https://ncbi.nlm.nih.gov/pubmed/7832772 |
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