BRENDA - Enzyme Database show
show all sequences of 1.1.1.23

Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase

Barbosa, J.A.; Sivaraman, J.; Li, Y.; Larocque, R.; Matte, A.; Schrag, J.D.; Cygler, M.; Proc. Natl. Acad. Sci. USA 99, 1859-1864 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene hisD, expression as glutathione S-transferase fusion protein with a thrombin cleavage site between tag and enzyme
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18°C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
binding site structure
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidinol + NAD+
Escherichia coli
part of L-histidine biosynthesis
L-histidine + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P06988
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme fusion protein
Escherichia coli
Reaction
Reaction
Commentary
Organism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 3 H+
reaction mechanism, amino acid residues Glu326 and His327 are involved in catalysis
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol + NAD+
part of L-histidine biosynthesis
657194
Escherichia coli
L-histidine + NADH
-
-
-
?
L-histidinol + NAD+
-
657194
Escherichia coli
L-histidinal + NADH + H+
-
-
-
ir
Subunits
Subunits
Commentary
Organism
dimer
dynamic light scattering
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
binding site structure
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hisD, expression as glutathione S-transferase fusion protein with a thrombin cleavage site between tag and enzyme
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
binding site structure
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18°C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
binding site structure
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidinol + NAD+
Escherichia coli
part of L-histidine biosynthesis
L-histidine + NADH
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme fusion protein
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol + NAD+
part of L-histidine biosynthesis
657194
Escherichia coli
L-histidine + NADH
-
-
-
?
L-histidinol + NAD+
-
657194
Escherichia coli
L-histidinal + NADH + H+
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
dynamic light scattering
Escherichia coli
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
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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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723322
Abdo
Anti-virulence strategy agains ...
Brucella suis
Org. Biomol. Chem.
9
3681-3690
2011
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21
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21
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1
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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
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9
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1
2
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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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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
-
1
1
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-
-
8
-
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2
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7
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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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4
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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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7
1
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7
1
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1
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1
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657194
Barbosa
Mechanism of action and NAD+-b ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
99
1859-1864
2002
-
-
1
1
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1
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1
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5
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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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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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2
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3
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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
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4
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1
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2
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4
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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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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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286328
Nagai
Structural and functional cons ...
Brassica oleracea
Proc. Natl. Acad. Sci. USA
88
4133-4137
1991
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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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9
2
24
1
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8
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6
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16
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2
24
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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286331
Görisch
Binding of histidinal to histi ...
Salmonella enterica subsp. enterica serovar Typhimurium
Eur. J. Biochem.
150
305-308
1985
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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
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2
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1
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2
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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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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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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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1
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1
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1
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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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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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10
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6
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5
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15
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4
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4
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8
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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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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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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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1
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3
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1
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2
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1
1
3
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1
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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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6
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