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Literature summary extracted from

  • Nunes, J.E.; Ducati, R.G.; Breda, A.; Rosado, L.A.; de Souza, B.M.; Palma, M.S.; Santos, D.S.; Basso, L.A.
    Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23) (2011), Arch. Biochem. Biophys., 512, 143-153.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.23 EDTA 118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.23 gene hisD, overexpression in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.23 1,10-phenanthroline 54% inhibition at 1 mM, 96% at 5 mM Mycobacterium tuberculosis
1.1.1.23 EDTA 118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.23 additional information
-
 additional information steady-state kinetics Mycobacterium tuberculosis
1.1.1.23 0.0049
-
 L-histidinol recombinant enzyme, pH 7.2, 25°C Mycobacterium tuberculosis
1.1.1.23 1.4
-
 NAD+ recombinant enzyme, pH 7.2, 25°C Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.23 soluble
-
 Mycobacterium tuberculosis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.23 Ca2+ can partially substitute for Zn2+ Mycobacterium tuberculosis
1.1.1.23 Mg2+ can partially substitute for Zn2+ Mycobacterium tuberculosis
1.1.1.23 Mn2+ best activating divalent cation Mycobacterium tuberculosis
1.1.1.23 additional information the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview Mycobacterium tuberculosis
1.1.1.23 Zn2+ required, one Zn2+ bound per subunit of the dimer. Zn2+ ion is octahedrally coordinated to Gln267, His270, Asp369, His428, and two ligands from L-histidinol Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.23 45348
-
 2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry Mycobacterium tuberculosis
1.1.1.23 45378
-
 2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry Mycobacterium tuberculosis
1.1.1.23 101800
-
 gel filtration, recombinant enzyme Mycobacterium tuberculosis

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 Mycobacterium tuberculosis via L-histidinaldehyde intermediate L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O Mycobacterium tuberculosis H37Rv via L-histidinaldehyde intermediate L-histidine + 2 NADH + 3 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.23 Mycobacterium tuberculosis P9WNW9 gene hisD
-
1.1.1.23 Mycobacterium tuberculosis H37Rv P9WNW9 gene hisD
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.23 recombinant enzyme from Escherichia coli strain BL21(DE3) 40fold to homogeneity by anion exchange chromatography, ultrafiltration, gel filtration, and another step of anion exchange chromatography 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+ bi uni uni bi ping-pong enzyme mechanism for MtHisD-catalyzed chemical reaction, involves abstraction of the hydroxyl group proton of L-histidinol by His336 and concomitant hydride transfer from the reactive carbon (carbon bound to the hydroxyl group that upon hydride transfer adopts the sp2 configuration) to NAD+, forming L-histidinaldehyde and transiently protonated His336 Mycobacterium tuberculosis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.23 1.2
-
 purified recombinant enzyme, pH 7.2, 25°C Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.23 L-histidinol + 2 NAD+ + H2O via L-histidinaldehyde intermediate Mycobacterium tuberculosis L-histidine + 2 NADH + 3 H+
-
 ?
1.1.1.23 L-histidinol + 2 NAD+ + H2O via L-histidinaldehyde intermediate Mycobacterium tuberculosis H37Rv L-histidine + 2 NADH + 3 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.23 dimer 2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry Mycobacterium tuberculosis
1.1.1.23 More three-dimensional model analysis, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.23 HisD
-
 Mycobacterium tuberculosis
1.1.1.23 histidinol dehydrogenase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.23 25
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.23 1.45
-
 L-histidinol recombinant enzyme, pH 7.2, 25°C Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.23 7.2
-
 assay at Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.23 additional information
-
 pH profile, overview Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.23 NAD+ amino acid residues contributing to NAD+ binding include Tyr129, Gly132, and Asn221 for phosphate binding, Gln193 and Asn221 for adenosine sugar binding, and Phe58, Gln193, and Tyr223 for adenine base binding Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.1.1.23 additional information 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 Mycobacterium tuberculosis