Literature summary for 1.4.1.1 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 .

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Protein Variants

Protein Variants	Comment	Organism
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
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
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

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQB1	-	-
Mycobacterium tuberculosis H37Rv	P9WQB1	-	-

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Release 2023.1 (January 2023)