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show all sequences of 1.1.1.23

Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23)

Nunes, J.E.; Ducati, R.G.; Breda, A.; Rosado, L.A.; de Souza, B.M.; Palma, M.S.; Santos, D.S.; Basso, L.A.; Arch. Biochem. Biophys. 512, 143-153 (2011)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
EDTA
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
Mycobacterium tuberculosis
Cloned(Commentary)
Commentary
Organism
gene hisD, overexpression in Escherichia coli strain BL21(DE3)
Mycobacterium tuberculosis
Inhibitors
Inhibitors
Commentary
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
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics
Mycobacterium tuberculosis
0.0049
-
L-Histidinol
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
1.4
-
NAD+
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Mycobacterium tuberculosis
-
-
Metals/Ions
Metals/Ions
Commentary
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]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
I6Y6Z1
gene hisD
-
Mycobacterium tuberculosis H37Rv
I6Y6Z1
gene hisD
-
Purification (Commentary)
Commentary
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
Commentary
Organism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 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
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.2
-
purified recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol + 2 NAD+ + H2O
via L-histidinaldehyde intermediate
721426
Mycobacterium tuberculosis
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
via L-histidinaldehyde intermediate
721426
Mycobacterium tuberculosis H37Rv
L-histidine + 2 NADH + 3 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry
Mycobacterium tuberculosis
More
three-dimensional model analysis, overview
Mycobacterium tuberculosis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Mycobacterium tuberculosis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.45
-
L-Histidinol
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Mycobacterium tuberculosis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
pH profile, overview
Mycobacterium tuberculosis
Cofactor
Cofactor
Commentary
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
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
EDTA
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
Mycobacterium tuberculosis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hisD, overexpression in Escherichia coli strain BL21(DE3)
Mycobacterium tuberculosis
Cofactor (protein specific)
Cofactor
Commentary
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
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics
Mycobacterium tuberculosis
0.0049
-
L-Histidinol
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
1.4
-
NAD+
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Mycobacterium tuberculosis
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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+
-
-
?
Purification (Commentary) (protein specific)
Commentary
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
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.2
-
purified recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol + 2 NAD+ + H2O
via L-histidinaldehyde intermediate
721426
Mycobacterium tuberculosis
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
via L-histidinaldehyde intermediate
721426
Mycobacterium tuberculosis H37Rv
L-histidine + 2 NADH + 3 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 45378, sequence calculation, 2 * 45348, recombinant enzyme, mass spectrometry
Mycobacterium tuberculosis
More
three-dimensional model analysis, overview
Mycobacterium tuberculosis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Mycobacterium tuberculosis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.45
-
L-Histidinol
recombinant enzyme, pH 7.2, 25C
Mycobacterium tuberculosis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Mycobacterium tuberculosis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
pH profile, overview
Mycobacterium tuberculosis
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.1.1.23
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721426
Nunes
Molecular, kinetic, thermodyna ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Arch. Biochem. Biophys.
512
143-153
2011
1
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1
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2
3
1
5
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2
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9
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1
1
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1
1
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723090
Turtaut
-
Synthesis and biological evalu ...
Brucella sp.
MedChemComm
2
995-1000
2011
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1
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15
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1
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15
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1
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1
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1
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1
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-
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723322
Abdo
Anti-virulence strategy agains ...
Brucella suis
Org. Biomol. Chem.
9
3681-3690
2011
-
-
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-
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21
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1
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1
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5
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21
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1
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1
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-
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3
3
-
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-
711417
Pahwa
Structure based design of nove ...
Geotrichum candidum
Bioorg. Med. Chem. Lett.
20
3972-3976
2010
-
-
-
-
-
-
9
-
-
-
-
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2
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1
2
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8
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8
9
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-
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1
2
-
-
-
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-
-
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-
-
1
1
-
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688045
Abdo
Brucella suis histidinol dehyd ...
Brucella suis
J. Enzyme Inhib. Med. Chem.
23
357-361
2008
-
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1
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-
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11
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3
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1
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11
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1
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11
11
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1
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697254
Pahwa
Target-specific anti-fungal di ...
Geotrichum candidum
Chem. Biol. Drug Des.
72
229-234
2008
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1
1
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8
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2
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7
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7
8
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684485
Joseph
Targeting of the Brucella suis ...
Brucella suis
Antimicrob. Agents Chemother.
51
3752-3755
2007
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3
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656358
Wadud
Method for determination of hi ...
Bos taurus
J. Chromatogr. B
767
369-374
2002
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2
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2
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1
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1
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4
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1
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1
1
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657194
Barbosa
Mechanism of action and NAD+-b ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
99
1859-1864
2002
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1
1
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5
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1
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2
1
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286322
Grubmeyer
Mechanism of Salmonella typhim ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
38
7355-7362
1999
-
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2
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286323
Kanaori
Effect of excess cadmium ion o ...
Brassica oleracea
FEBS Lett.
412
301-304
1997
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1
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286324
Kheirolomoom
Steady-state kinetics of cabba ...
Brassica oleracea
Arch. Biochem. Biophys.
312
493-500
1994
-
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1
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2
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1
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286325
Nagai
Histidinol dehydrogenase loses ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biochem.
115
22-25
1994
-
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1
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1
-
-
4
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1
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2
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2
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3
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2
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1
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1
1
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1
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4
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1
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3
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2
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286326
Nagai
Site-directed mutagenesis show ...
Brassica oleracea
J. Biochem.
114
856-861
1993
-
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1
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1
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2
1
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2
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3
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3
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1
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1
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1
1
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1
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3
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1
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286327
Nagai
Overexpression of plant histid ...
Brassica oleracea
Arch. Biochem. Biophys.
295
235-239
1992
-
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1
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4
4
1
1
2
2
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3
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1
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1
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3
1
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1
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1
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1
1
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4
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4
1
1
2
2
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1
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1
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3
1
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1
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286328
Nagai
Structural and functional cons ...
Brassica oleracea
Proc. Natl. Acad. Sci. USA
88
4133-4137
1991
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5
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286329
Nagai
Purification and characterizat ...
Asparagus officinalis, Brassica oleracea, Brassica oleracea var. capitata, Cucumis sativus, Lactuca sativa, Rosa sp., Solanum melongena, Triticum aestivum
Arch. Biochem. Biophys.
284
127-132
1991
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6
2
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1
2
16
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10
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1
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2
9
2
24
1
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1
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1
8
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8
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6
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2
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1
2
16
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1
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2
9
2
24
1
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1
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1
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286330
Grubmeyer
A cysteine residue (cysteine-1 ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
25
4778-4784
1986
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3
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3
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3
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286331
Grisch
Binding of histidinal to histi ...
Salmonella enterica subsp. enterica serovar Typhimurium
Eur. J. Biochem.
150
305-308
1985
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2
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1
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2
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1
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1
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1
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2
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3
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1
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286332
Andorn
Purification and properties of ...
Escherichia coli
J. Gen. Microbiol.
128
579-584
1982
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2
1
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2
2
2
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2
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1
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1
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3
1
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1
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1
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1
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1
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2
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1
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2
2
2
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1
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1
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3
1
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1
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1
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286333
Feingold
-
Pyridine nucleotide-linked fou ...
Salmonella enterica subsp. enterica serovar Typhimurium
Trends Biochem. Sci.
6
103-105
1981
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2
2
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2
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1
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3
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1
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1
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2
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2
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2
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3
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286334
Burger
Evidence for an essential lysi ...
Salmonella enterica subsp. enterica serovar Typhimurium
Eur. J. Biochem.
118
125-130
1981
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1
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2
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2
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3
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1
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1
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1
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2
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3
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286335
Burger
The catalytically active form ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochem. J.
181
771-774
1979
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2
2
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2
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3
1
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1
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1
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2
2
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3
1
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286336
Bitar
Histidinol dehydrogenase from ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Biochim. Biophys. Acta
493
429-440
1977
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1
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4
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4
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2
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2
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6
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2
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2
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1
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4
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2
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2
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6
-
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286337
Lindsay
Purification and properties of ...
Bacillus caldolyticus, Bacillus subtilis, Bacillus subtilis HT1, Geobacillus stearothermophilus, Sporosarcina psychrophila
Biochem. J.
165
247-253
1977
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8
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4
10
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6
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1
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5
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15
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5
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4
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4
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4
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8
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4
10
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1
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5
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15
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5
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4
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286338
Yang
Studies on histidinol dehydrog ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Mol. Biol.
81
517-519
1973
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1
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1
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1
1
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2
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3
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286339
Loper
Purification and properties of ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
240
788-795
1965
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3
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2
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2
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1
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1
1
3
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1
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1
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1
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1
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3
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2
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1
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1
1
3
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1
-
1
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286340
Adams
The enzymatic synthesis of his ...
Escherichia coli, Paenarthrobacter histidinolovorans
J. Biol. Chem.
209
829-846
1954
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3
1
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4
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2
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6
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2
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2
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2
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3
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1
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4
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6
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2
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