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Literature summary extracted from

  • Koehler, S.; Dessolin, J.; Winum, J.
    Inhibitors of histidinol dehydrogenase (2017), Top. Med. Chem., 22, 35-46.
No PubMed abstract available

Application

EC Number Application Comment Organism
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Brucella sp.
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Geotrichum candidum
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Burkholderia pseudomallei
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Brucella suis
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents Brassica oleracea
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents, overview Escherichia coli
1.1.1.23 drug development histidinol dehydrogenase is a target for the development of antimicrobial agents, overview Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.23 gene hisD, overexpression of His-tagged HDH in Escherichia coli Brucella suis
1.1.1.23 gene hisD, recombinant overexpression Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.23 crystal structure determination of HDH in its native state and with several substrates and Zn2+. the NAD+ molecule is crystallized with L-histidinol into the active site. In the apo structure, the Zn2+ coordination is tetrahedral, while it is octahedral in the inhibitor/enzyme complex Escherichia coli
1.1.1.23 only a C366S mutant allows crystallization to proceed, probably forbidding oxidation/reduction of the native enzyme at this position, molecular replacement using the structure of the Escherichia coli enzyme. In the apo structure, the Zn2+ coordination is tetrahedral, while it is octahedral in the inhibitor/enzyme complex Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.23 C366S site-directed mutagenesis Mycobacterium tuberculosis
1.1.1.23 additional information site-directed mutagenesis of hisD, resulting in the replacement of the five His-residues with asparagine or glutamine, causes an important decrease in kcat for His261 and His326 Salmonella enterica subsp. enterica serovar Typhimurium

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.23 (2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
-
 Mycobacterium tuberculosis
1.1.1.23 (3S)-3-amino-1-(4-hydroxyphenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
 Brassica oleracea
1.1.1.23 (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one causes strong in vivo inhibition and growth inhibition Brucella sp.
1.1.1.23 (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
 Mycobacterium tuberculosis
1.1.1.23 (3S)-3-amino-4-(1H-imidazol-4-yl)-1-phenylbutan-2-one
-
 Escherichia coli
1.1.1.23 (3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one causes strong in vivo inhibition and growth inhibition Brucella sp.
1.1.1.23 (3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
-
 Mycobacterium tuberculosis
1.1.1.23 (3S)-3-amino-4-(1H-imidazol-4-yl)butan-2-one
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 (8S)-8-[2-(biphenyl-4-yl)ethanethioyl]-7,8-dihydroimidazo[1,5-c]pyrimidine-5(6H)-thione
-
 Mycobacterium tuberculosis
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Brassica oleracea
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as antimicrobial drugs Brucella sp.
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Brucella suis
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Burkholderia pseudomallei
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Escherichia coli
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Geotrichum candidum
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs. Enzyme inactivation by chelating agents Mycobacterium tuberculosis
1.1.1.23 additional information exploration of enzyme inhibitors for potential application as novel antimicrobial drugs Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.23 additional information
-
 additional information kinetic isotope effects studies with deuterated histidinols on Salmonella typhimurium HDH reveals that the rate constants obtained at pH 9.0 allow kinetic simulations indicating a thermodynamically unfavorable but relatively fast hydride transfer from histidinol, and an irreversible and slower second hydride transfer from a histidinal derivative Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 0.012
-
 L-histidinol pH and temperature not specified in the publication Brucella suis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.23 chloroplast
-
 Brassica oleracea 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Brucella sp.
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Escherichia coli
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Geotrichum candidum
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Burkholderia pseudomallei
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Brucella suis
1.1.1.23 Cd2+ activates, to a higher degree than Zn2+ Brassica oleracea
1.1.1.23 Co2+ activates less than Zn2+ Brucella sp.
1.1.1.23 Co2+ activates less than Zn2+ Escherichia coli
1.1.1.23 Co2+ activates less than Zn2+ Geotrichum candidum
1.1.1.23 Co2+ activates less than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Co2+ activates less than Zn2+ Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 Co2+ activates less than Zn2+ Burkholderia pseudomallei
1.1.1.23 Co2+ activates less than Zn2+ Brucella suis
1.1.1.23 Co2+ activates less than Zn2+ Brassica oleracea
1.1.1.23 Cu2+ activates less than Zn2+ Brucella sp.
1.1.1.23 Cu2+ activates less than Zn2+ Escherichia coli
1.1.1.23 Cu2+ activates less than Zn2+ Geotrichum candidum
1.1.1.23 Cu2+ activates less than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Cu2+ activates less than Zn2+ Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 Cu2+ activates less than Zn2+ Burkholderia pseudomallei
1.1.1.23 Cu2+ activates less than Zn2+ Brucella suis
1.1.1.23 Cu2+ activates less than Zn2+ Brassica oleracea
1.1.1.23 Mg2+ activates less than Zn2+ Brucella sp.
1.1.1.23 Mg2+ activates less than Zn2+ Escherichia coli
1.1.1.23 Mg2+ activates less than Zn2+ Geotrichum candidum
1.1.1.23 Mg2+ activates less than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Mg2+ activates less than Zn2+ Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 Mg2+ activates less than Zn2+ Burkholderia pseudomallei
1.1.1.23 Mg2+ activates less than Zn2+ Brucella suis
1.1.1.23 Mg2+ activates less than Zn2+ Brassica oleracea
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Brucella sp.
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Geotrichum candidum
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Burkholderia pseudomallei
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Brucella suis
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+ Brassica oleracea
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form Escherichia coli
1.1.1.23 Mn2+ activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Brucella sp.
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Escherichia coli
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Geotrichum candidum
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Mycobacterium tuberculosis
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Burkholderia pseudomallei
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Brucella suis
1.1.1.23 additional information the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity Brassica oleracea
1.1.1.23 Ni2+ activates less than Zn2+ Brucella sp.
1.1.1.23 Ni2+ activates less than Zn2+ Escherichia coli
1.1.1.23 Ni2+ activates less than Zn2+ Geotrichum candidum
1.1.1.23 Ni2+ activates less than Zn2+ Mycobacterium tuberculosis
1.1.1.23 Ni2+ activates less than Zn2+ Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 Ni2+ activates less than Zn2+ Burkholderia pseudomallei
1.1.1.23 Ni2+ activates less than Zn2+ Brucella suis
1.1.1.23 Ni2+ activates less than Zn2+ Brassica oleracea
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Brucella sp.
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Escherichia coli
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Geotrichum candidum
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Mycobacterium tuberculosis
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Burkholderia pseudomallei
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Brucella suis
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis Brassica oleracea
1.1.1.23 Zn2+ metalloenzyme containing one Zn2+ cation in each subunit. His261 and His418 are candidates for zinc ion ligands, as affinities for metal ions decrease with substitutions at these residues. Binding structure analysis Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.23 47000
-
 2 * 47000 Brucella sp.
1.1.1.23 47000
-
 2 * 47000 Geotrichum candidum
1.1.1.23 47000
-
 2 * 47000 Mycobacterium tuberculosis
1.1.1.23 47000
-
 2 * 47000 Burkholderia pseudomallei
1.1.1.23 47000
-
 2 * 47000 Brassica oleracea
1.1.1.23 49000
-
-
 Brucella suis
1.1.1.23 52000
-
 2 * 52000, SDS-PAGE Escherichia coli
1.1.1.23 90000
-
 about, gel filtration Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.23 L-histidinol + 2 NAD+ + H2O Brucella sp.
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Escherichia coli
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Geotrichum candidum
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Mycobacterium tuberculosis
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Burkholderia pseudomallei
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Brucella suis
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Brassica oleracea
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Brucella suis 1330
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Mycobacterium tuberculosis H37Rv
-
 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Burkholderia pseudomallei K96243
-
 L-histidine + 2 NADH + 3 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.23 Brassica oleracea P24226 var. capitata
-
1.1.1.23 Brucella sp.
-
-
-
1.1.1.23 Brucella suis Q8G2R2 biovar 1
-
1.1.1.23 Brucella suis 1330 Q8G2R2 biovar 1
-
1.1.1.23 Burkholderia pseudomallei Q63Q86
-
-
1.1.1.23 Burkholderia pseudomallei K96243 Q63Q86
-
-
1.1.1.23 Escherichia coli P06988
-
-
1.1.1.23 Geotrichum candidum A0A0J9X7D2
-
-
1.1.1.23 Mycobacterium tuberculosis P9WNW9
-
-
1.1.1.23 Mycobacterium tuberculosis H37Rv P9WNW9
-
-
1.1.1.23 Salmonella enterica subsp. enterica serovar Typhimurium P10370
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.23 recombinant enzyme by anion exchange chromatography and gel filtration Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Brucella sp.
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Escherichia coli
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Geotrichum candidum
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Mycobacterium tuberculosis
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Salmonella enterica subsp. enterica serovar Typhimurium
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Burkholderia pseudomallei
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Brucella suis
a
1.1.1.23 L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+ the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism Brassica oleracea
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Brucella sp. L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Escherichia coli L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Geotrichum candidum L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Mycobacterium tuberculosis L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Burkholderia pseudomallei L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Brucella suis L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Brassica oleracea L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O the enzyme is highly specific for histidinol and NAD+ Escherichia coli L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O the enzyme is highly specific for histidinol and NAD+ Salmonella enterica subsp. enterica serovar Typhimurium L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Brucella suis 1330 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Mycobacterium tuberculosis H37Rv L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O
-
 Burkholderia pseudomallei K96243 L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 additional information active site binding structure for substrates L-histidinol, L-histamine, and L-histidine, NMR study Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.23 homodimer 2 * 52000, SDS-PAGE Escherichia coli
1.1.1.23 homodimer 2 * 47000 Brucella sp.
1.1.1.23 homodimer 2 * 47000 Geotrichum candidum
1.1.1.23 homodimer 2 * 47000 Mycobacterium tuberculosis
1.1.1.23 homodimer 2 * 47000 Burkholderia pseudomallei
1.1.1.23 homodimer 2 * 47000 Brassica oleracea
1.1.1.23 homodimer 2 * 46000-47000, SDS-PAGE Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 homodimer 2 * 49000, recombinant enzyme, SDS-PAGE Brucella suis
1.1.1.23 More native HDH forms a dimer of identical or nearly identical subunits Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 More native HDH forms a dimer of identical or nearly identical subunits, it contains an incomplete Rossmann-fold in two domains of the protein. Crystal structure comparison with the enzyme from Brucella suis Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.1.1.23 BN980_GECA03s06082g
-
 Geotrichum candidum
1.1.1.23 HDH
-
 Brucella sp.
1.1.1.23 HDH
-
 Escherichia coli
1.1.1.23 HDH
-
 Geotrichum candidum
1.1.1.23 HDH
-
 Mycobacterium tuberculosis
1.1.1.23 HDH
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 HDH
-
 Burkholderia pseudomallei
1.1.1.23 HDH
-
 Brucella suis
1.1.1.23 HDH
-
 Brassica oleracea
1.1.1.23 HisD
-
 Brucella sp.
1.1.1.23 HisD
-
 Escherichia coli
1.1.1.23 HisD
-
 Geotrichum candidum
1.1.1.23 HisD
-
 Mycobacterium tuberculosis
1.1.1.23 HisD
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 HisD
-
 Burkholderia pseudomallei
1.1.1.23 HisD
-
 Brucella suis
1.1.1.23 HisD
-
 Brassica oleracea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.23 9.5
-
-
 Escherichia coli
1.1.1.23 9.5
-
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.23 NAD+
-
 Brucella sp.
1.1.1.23 NAD+
-
 Geotrichum candidum
1.1.1.23 NAD+
-
 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 NAD+
-
 Burkholderia pseudomallei
1.1.1.23 NAD+
-
 Brucella suis
1.1.1.23 NAD+
-
 Brassica oleracea
1.1.1.23 NAD+ the amine group is responsible of the substrate orientation by interacting with the Zn2+ while the overall stabilization of the cation changed between the unbound and bound forms Mycobacterium tuberculosis
1.1.1.23 NAD+ the amine group is responsible of the substrate orientation by interacting with the Zn2+ while the overall stabilization of the cation changes between the unbound and bound forms Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.23 0.000003
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
1.1.1.23 0.000003
-
 pH and temperature not specified in the publication Brucella sp. (3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
1.1.1.23 0.00004
-
 pH and temperature not specified in the publication Brassica oleracea (3S)-3-amino-1-(4-hydroxyphenyl)-4-(1H-imidazol-4-yl)butan-2-one
1.1.1.23 0.00007
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis (3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
1.1.1.23 0.001
-
 pH and temperature not specified in the publication Escherichia coli (3S)-3-amino-4-(1H-imidazol-4-yl)-1-phenylbutan-2-one
1.1.1.23 0.005
-
 pH and temperature not specified in the publication Salmonella enterica subsp. enterica serovar Typhimurium (3S)-3-amino-4-(1H-imidazol-4-yl)butan-2-one
1.1.1.23 0.005
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis (8S)-8-[2-(biphenyl-4-yl)ethanethioyl]-7,8-dihydroimidazo[1,5-c]pyrimidine-5(6H)-thione
1.1.1.23 0.025
-
 pH and temperature not specified in the publication Mycobacterium tuberculosis (2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide

General Information

EC Number General Information Comment Organism
1.1.1.23 malfunction a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication Brucella suis
1.1.1.23 malfunction growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells Mycobacterium tuberculosis
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 Brucella sp.
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 Escherichia coli
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 Geotrichum candidum
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 Salmonella enterica subsp. enterica serovar Typhimurium
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 Burkholderia pseudomallei
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 Brassica oleracea
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 Mycobacterium tuberculosis
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 Brucella suis
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer Brucella sp.
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer Geotrichum candidum
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer Burkholderia pseudomallei
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer Brucella suis
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer, molecular homology modeling Mycobacterium tuberculosis
1.1.1.23 additional information two identical active sites, one in each subunit of the dimer, residues His261 and His326 are involved in proton transfers during catalysis Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 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 Escherichia coli
1.1.1.23 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 Brassica oleracea
1.1.1.23 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 Brucella sp.
1.1.1.23 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 Escherichia coli
1.1.1.23 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 Geotrichum candidum
1.1.1.23 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 Mycobacterium tuberculosis
1.1.1.23 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 Salmonella enterica subsp. enterica serovar Typhimurium
1.1.1.23 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 Burkholderia pseudomallei
1.1.1.23 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 Brucella suis