EC Number   |
General Information |
Reference |
|---|
   1.1.1.23 | malfunction |
a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication |
-, 741455 |
| 1.1.1.23 | malfunction |
enzyme inhibition leads to inhibition of intracellular bacterial growth in macrophage infection of the facultative intracellular pathogen |
723322 |
| 1.1.1.23 | malfunction |
growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells |
-, 741455 |
| 1.1.1.23 | metabolism |
histidinol dehydrogenase mediates the final step in the histidine biosynthetic pathway |
711417 |
| 1.1.1.23 | metabolism |
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis |
-, 741455 |
| 1.1.1.23 | metabolism |
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis. In the pathogen's bacterial biosynthesis of His is crucial for intracellular growth, the vacuole-borne pathogens have no access to this amino acid produced by the host cell |
-, 741455 |
| 1.1.1.23 | metabolism |
reaction mechanism: a proton is withdrawn from the histidinol O atom by Nepsilon of His368 (Base 1) that becomes double-protonated, and one hydride is abstracted by the first NAD+ molecule, and histidinaldehyde is formed. The used NADH dissociates and is replaced by the second NAD+ molecule. A water molecule is activated by Glu367 (Base 2) and performs a nucleophilic attack on the reactive carbon, forming a new C-O bond. Simultaneously, the histidinaldehyde oxygen withdraws the proton back from Nepsilon of His368, resulting in the formation of a gem-diol histidinaldehyde hydrate. In the next step, His368 abstracts a proton from one of the hydroxyl groups of histidinaldehyde hydrate, whereas the second NAD+ removes hydride from the reactive carbon, producing His |
762423 |
| 1.1.1.23 | metabolism |
the enzyme catalyzes the last step in histidine biosynthesis |
723322 |
| 1.1.1.23 | metabolism |
the enzyme is involved in the histidine biosynthesis pathway catalyzing catalyzes the last two steps in the histidine biosynthesis pathway, namely the sequential NAD+-dependent oxidations of L-histidinol to L-histidinaldehyde and subsequently to L-histidine |
-, 740116 |
| 1.1.1.23 | more |
molecular homology model building, overview. His336 plays a critical role in both catalysis and L-Hol binding to MtHisD, Tyr129, Tyr223 and His335 residues make contacts with the substrates in the MtHisD enzyme active site, three-dimensional model analysis, overview |
-, 721426 |
