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1.1.1.23
Structures of Medicago truncatula L-histidinol dehydrogenase show rearrangements required for NAD+ binding and the cofactor positioned to accept a hydride
Medicago truncatula
1.1.1.23
A cysteine residue (cysteine-116) in the histidinol binding site of histidinoldehydrogenase
Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23
Anti-virulence strategy against Brucella suis: synthesis, biological evaluation and molecular modeling of selective histidinol dehydrogenase inhibitors
Brucella suis
1.1.1.23
Binding of histidinal to histidinol dehydrogenase
Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23
Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide
Brucella suis
1.1.1.23
Effect of excess cadmium ion on the metal binding site of cabbage histidinol dehydrogenase studie by 113Cd-NMR spectroscopy
Brassica oleracea
1.1.1.23
Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase
Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23
Histidinol dehydrogenase from salmonella typhimurium and escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group
Escherichia coli
1.1.1.23
Histidinol dehydrogenase from salmonella typhimurium and escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group
Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23
Histidinol dehydrogenase loses its catalytic function through the mutation of His261-Asn due to its inability to ligate the essential Zn
Salmonella enterica subsp. enterica serovar Typhimurium
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