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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.1.1.23
762423
Structures of Medicago truncatula L-histidinol dehydrogenase show rearrangements required for NAD+ binding and the cofactor positioned to accept a hydride
Sci. Rep.
7
10476
2017
Medicago truncatula
28874718
1.1.1.23
286326
Site-directed mutagenesis shows that the conserved cysteine residues of histidinol dehydrogensae are not essential for catalysis
J. Biochem.
114
856-861
1993
Brassica oleracea
8138543
1.1.1.23
286325
Histidinol dehydrogenase loses its catalytic function through the mutation of His261-Asn due to its inability to ligate the essential Zn
J. Biochem.
115
22-25
1994
Salmonella enterica subsp. enterica serovar Typhimurium
8188630
1.1.1.23
286334
Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase
Eur. J. Biochem.
118
125-130
1981
Salmonella enterica subsp. enterica serovar Typhimurium
6793363
1.1.1.23
286332
Purification and properties of histidinol dehydrogenase from Escherichia coli B
J. Gen. Microbiol.
128
579-584
1982
Escherichia coli
7042909
1.1.1.23
286331
Binding of histidinal to histidinol dehydrogenase
Eur. J. Biochem.
150
305-308
1985
Salmonella enterica subsp. enterica serovar Typhimurium
3894023
1.1.1.23
286337
Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli
Biochem. J.
165
247-253
1977
Geobacillus stearothermophilus
921748
1.1.1.23
286337
Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli
Biochem. J.
165
247-253
1977
[Bacillus] caldolyticus
921748
1.1.1.23
286337
Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli
Biochem. J.
165
247-253
1977
Bacillus subtilis
921748
1.1.1.23
286337
Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli
Biochem. J.
165
247-253
1977
Sporosarcina psychrophila
921748
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