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Literature summary extracted from

  • Ling, B.; Bi, S.; Sun, M.; Jing, Z.; Li, X.; Zhang, R.
    Molecular dynamics simulations of mutated Mycobacterium tuberculosis L-alanine dehydrogenase to illuminate the role of key residues (2014), J. Mol. Graph. Model., 50, 61-70 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.1 D270N upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity Mycobacterium tuberculosis
1.4.1.1 D270N/H96A the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity Mycobacterium tuberculosis
1.4.1.1 H96A upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.1 Mycobacterium tuberculosis P9WQB1
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1.4.1.1 Mycobacterium tuberculosis H37Rv P9WQB1
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