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Literature summary for 1.1.1.23 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
Search for more literature for 1.1.1.23

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Mycobacterium tuberculosis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ can partially substitute for Zn2+ Mycobacterium tuberculosis
Mg2+ can partially substitute for Zn2+ Mycobacterium tuberculosis
Mn2+ best activating divalent cation Mycobacterium tuberculosis
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
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-histidinol + 2 NAD+ + H2O Mycobacterium tuberculosis via L-histidinaldehyde intermediate L-histidine + 2 NADH + 3 H+
-
 ?
L-histidinol + 2 NAD+ + H2O Mycobacterium tuberculosis H37Rv via L-histidinaldehyde intermediate L-histidine + 2 NADH + 3 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNW9 gene hisD
-
Mycobacterium tuberculosis H37Rv P9WNW9 gene hisD
-

Purification (Commentary)

Purification (Comment) Organism
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

Reaction Comment Organism Reaction ID
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]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
HisD
-
 Mycobacterium tuberculosis
histidinol dehydrogenase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

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

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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