1.1.1.23: histidinol dehydrogenase
This is an abbreviated version!
For detailed information about histidinol dehydrogenase, go to the full flat file.
Reaction
Synonyms
11412251, BN980_GECA03s06082g, BsHDH, GcHDH, HDH, HIS4 protein, HisD, histidinol dehydrogenase, HLDase, L-histidinol dehydrogenase
ECTree
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General Information
General Information on EC 1.1.1.23 - histidinol dehydrogenase
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malfunction
metabolism
physiological function
additional information
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enzyme inhibition leads to inhibition of intracellular bacterial growth in macrophage infection of the facultative intracellular pathogen
malfunction
a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication
malfunction
growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells
malfunction
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a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication
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malfunction
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growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells
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histidinol dehydrogenase mediates the final step in the histidine biosynthetic pathway
metabolism
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L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
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
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
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
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
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
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
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
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
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
metabolism
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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
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metabolism
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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
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metabolism
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L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
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metabolism
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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
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the enzyme is essential for intramacrophagic replication
physiological function
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role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development. The enzyme is essential for infection of the host cell
physiological function
the enzyme is essential for Mycobacterium tuberculosis survival in vitro
physiological function
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role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development. The enzyme is essential for infection of the host cell
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physiological function
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the enzyme is essential for Mycobacterium tuberculosis survival in vitro
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physiological function
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role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
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physiological function
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role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
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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
additional information
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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
additional information
MtHisD is a bifunctional four-electron dehydrogenase enzyme that catalyzes two subsequent reactions, the oxidation of L-Hol and the reduction of two NAD+ molecules,23 with the formation of two intermediaries, L-histidinaldehyde and L-histidindiol. L-histidinaldehyde is very unstable at neutral pH when not bound to HisD
additional information
residues Glu326 and His327 are directly involved in catalysis, the first participating in acid-base catalysis and the second activating a water molecule, active site structure, overview
additional information
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two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer, molecular homology modeling
additional information
two identical active sites, one in each subunit of the dimer, residues His261 and His326 are involved in proton transfers during catalysis
additional information
two identical active sites, one in each subunit of the dimer. The dimer layout resulting in an active site displays a domain swapping between the monomers and allows a complete mapping of the Zn2+ and substrate binding by the involved residues
additional information
two identical active sites, one in each subunit of the dimer. Two histidine residues are critical for the activity, both amino acids are zinc ligands
additional information
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two identical active sites, one in each subunit of the dimer
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additional information
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MtHisD is a bifunctional four-electron dehydrogenase enzyme that catalyzes two subsequent reactions, the oxidation of L-Hol and the reduction of two NAD+ molecules,23 with the formation of two intermediaries, L-histidinaldehyde and L-histidindiol. L-histidinaldehyde is very unstable at neutral pH when not bound to HisD
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additional information
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two identical active sites, one in each subunit of the dimer, molecular homology modeling
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additional information
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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
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additional information
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two identical active sites, one in each subunit of the dimer
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additional information
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residues Glu326 and His327 are directly involved in catalysis, the first participating in acid-base catalysis and the second activating a water molecule, active site structure, overview
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