BRENDA - Enzyme Database show
show all sequences of 2.6.1.9

Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase

Fernandez, F.J.; Vega, M.C.; Lehmann, F.; Sandmeier, E.; Gehring, H.; Christen, P.; Wilmanns, M.; J. Biol. Chem. 279, 21478-21488 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
Thermotoga maritima
Crystallization (Commentary)
Crystallization
Organism
wild-type and selenomethionine-labeled enzyme, with or without bound pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, sitting drop vapour diffusion method, 0.001 ml equal volumes of protein and reservoir solutions, 20°C, 50% v/v ethylene glycol, 5% w/v PEG 1000, sodium acetate, pH 5.1, 2-3 weeks, X-ray diffraction structure determination and analysis at 3.5 A resolution
Thermotoga maritima
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.8
-
L-Histidinol phosphate
pH 8.0, 20°C
Thermotoga maritima
2.3
-
L-tyrosine
pH 8.0, 20°C
Thermotoga maritima
3.4
-
L-tryptophan
pH 8.0, 20°C
Thermotoga maritima
38
-
L-phenylalanine
pH 8.0, 20°C
Thermotoga maritima
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidinol phosphate + 2-oxoglutarate
Thermotoga maritima
catalytic reaction pathway, histidine biosynthesis
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
r
additional information
Thermotoga maritima
enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermotoga maritima
Q9X0D0
gene tmHspAT
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) and B834(DE3), respectively
Thermotoga maritima
Reaction
Reaction
Commentary
Organism
L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
mechanism via gem-diamino, aldimine, and ketimine reaction intermediates, active site structure analysis, overview
Thermotoga maritima
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol phosphate + 2-oxoglutarate
-
659343
Thermotoga maritima
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
-
r
L-histidinol phosphate + 2-oxoglutarate
catalytic reaction pathway, histidine biosynthesis
659343
Thermotoga maritima
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
low activity with
659343
Thermotoga maritima
phenylpyruvate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
-
659343
Thermotoga maritima
3-indole-2-oxopropanoate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
-
659343
Thermotoga maritima
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
r
additional information
enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo
659343
Thermotoga maritima
?
-
-
-
-
additional information
no activity with L-histidine
659343
Thermotoga maritima
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
above
Thermotoga maritima
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.009
-
L-phenylalanine
pH 8.0, 25°C
Thermotoga maritima
0.014
-
L-tryptophan
pH 8.0, 25°C
Thermotoga maritima
0.043
-
L-tyrosine
pH 8.0, 25°C
Thermotoga maritima
0.046
-
L-Histidinol phosphate
pH 8.0, 25°C
Thermotoga maritima
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermotoga maritima
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
covalently bound
Thermotoga maritima
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
Thermotoga maritima
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
covalently bound
Thermotoga maritima
Crystallization (Commentary) (protein specific)
Crystallization
Organism
wild-type and selenomethionine-labeled enzyme, with or without bound pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate, sitting drop vapour diffusion method, 0.001 ml equal volumes of protein and reservoir solutions, 20°C, 50% v/v ethylene glycol, 5% w/v PEG 1000, sodium acetate, pH 5.1, 2-3 weeks, X-ray diffraction structure determination and analysis at 3.5 A resolution
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.8
-
L-Histidinol phosphate
pH 8.0, 20°C
Thermotoga maritima
2.3
-
L-tyrosine
pH 8.0, 20°C
Thermotoga maritima
3.4
-
L-tryptophan
pH 8.0, 20°C
Thermotoga maritima
38
-
L-phenylalanine
pH 8.0, 20°C
Thermotoga maritima
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-histidinol phosphate + 2-oxoglutarate
Thermotoga maritima
catalytic reaction pathway, histidine biosynthesis
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
r
additional information
Thermotoga maritima
enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) and B834(DE3), respectively
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-histidinol phosphate + 2-oxoglutarate
-
659343
Thermotoga maritima
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
-
r
L-histidinol phosphate + 2-oxoglutarate
catalytic reaction pathway, histidine biosynthesis
659343
Thermotoga maritima
3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
-
-
-
r
L-phenylalanine + 2-oxoglutarate
low activity with
659343
Thermotoga maritima
phenylpyruvate + L-glutamate
-
-
-
r
L-tryptophan + 2-oxoglutarate
-
659343
Thermotoga maritima
3-indole-2-oxopropanoate + L-glutamate
-
-
-
r
L-tyrosine + 2-oxoglutarate
-
659343
Thermotoga maritima
3-(4-hydroxyphenyl)-2-oxopropanoate + L-glutamate
-
-
-
r
additional information
enzyme might also catalyze the transamination reaction with other substrates generating aromatic amino acids in vivo
659343
Thermotoga maritima
?
-
-
-
-
additional information
no activity with L-histidine
659343
Thermotoga maritima
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
above
Thermotoga maritima
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.009
-
L-phenylalanine
pH 8.0, 25°C
Thermotoga maritima
0.014
-
L-tryptophan
pH 8.0, 25°C
Thermotoga maritima
0.043
-
L-tyrosine
pH 8.0, 25°C
Thermotoga maritima
0.046
-
L-Histidinol phosphate
pH 8.0, 25°C
Thermotoga maritima
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermotoga maritima
Other publictions for EC 2.6.1.9
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)
739670
Nasir
Crystal structures of Mycobact ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Sci. Rep.
6
18880
2016
-
-
1
1
1
-
1
3
-
-
-
-
-
4
-
-
-
-
-
-
-
-
6
-
-
-
-
3
-
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-
-
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-
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-
1
-
1
1
-
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1
-
3
-
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-
-
-
-
-
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3
737370
Nasir
Sample preparation, crystalliz ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
69
445-448
2013
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721229
Nasir
Molecular cloning, overexpress ...
Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
68
32-36
2012
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
1
-
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-
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1
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1
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-
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-
684151
Marienhagen
Insights into the structural b ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
675-685
2008
-
-
-
1
4
-
-
15
-
-
-
-
-
4
-
-
-
-
-
-
8
-
9
-
-
-
-
15
-
-
-
-
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-
-
-
-
-
-
1
4
-
-
-
-
15
-
-
-
-
-
-
-
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-
-
8
-
9
-
-
-
-
15
-
-
-
-
-
-
-
-
-
-
676602
Mo
The hpa1 mutant of Arabidopsis ...
Arabidopsis thaliana
Plant Physiol.
141
1425-1435
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
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1
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1
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1
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
659343
Fernandez
Structural studies of the cata ...
Thermotoga maritima
J. Biol. Chem.
279
21478-21488
2004
-
-
1
1
-
-
-
4
-
-
-
2
-
2
-
-
1
1
-
-
-
-
7
-
1
-
-
4
1
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
4
-
-
-
2
-
-
-
1
-
-
-
-
7
-
1
-
-
4
1
-
-
-
-
-
-
-
-
-
637153
Mizuguchi
Characterization of histidinol ...
Escherichia coli
Biochim. Biophys. Acta
1647
321-324
2003
-
-
1
-
4
-
-
-
-
-
-
-
-
2
-
-
1
-
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1
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4
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1
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637150
El Malki
Molecular characterization and ...
Nicotiana tabacum
Plant Mol. Biol.
45
191-199
2001
-
-
1
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-
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-
-
1
-
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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1
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637152
Haruyama
Structures of Escherichia coli ...
Escherichia coli
Biochemistry
40
4633-4644
2001
-
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1
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1
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3
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2
1
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1
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1
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2
1
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-
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637154
Sivaraman
Crystal structure of histidino ...
Escherichia coli
J. Mol. Biol.
311
761-776
2001
-
-
1
1
-
-
-
-
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1
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6
-
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1
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1
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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1
1
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637151
Gu
Imidazole acetol phosphate ami ...
Zymomonas mobilis
J. Bacteriol.
177
1576-1584
1995
-
-
1
-
-
-
-
3
-
-
2
-
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1
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1
1
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4
3
9
1
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2
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1
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1
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1
1
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3
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2
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1
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4
3
9
1
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2
-
1
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-
637144
Hsu
L-Histidinol phosphate aminotr ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochimie
71
477-489
1989
-
-
-
-
-
-
-
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2
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1
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1
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636659
Weigent
Purification and properties of ...
Bacillus subtilis
J. Biol. Chem.
251
6974-6980
1976
-
-
-
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1
4
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1
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2
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1
1
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1
1
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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1
-
4
-
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1
-
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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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-
-
-
-
637147
Henderson
Omega-aminoalkylagaroses in th ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
13
4335-4338
1974
-
-
-
-
-
-
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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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637146
Henderson
Crystalline L-histidinol phosp ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
248
1906-1911
1973
-
-
-
1
-
-
-
-
-
-
2
-
-
2
-
-
1
-
-
-
1
-
1
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
637149
Roberts
-
Imidazolylacetolphosphate amin ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
248
77408-7753
1973
-
-
-
-
-
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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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1
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1
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1
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2
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637143
Martin
Imidazolylacetolphosphate:L-gl ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
242
1168-1174
1967
-
-
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1
1
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1
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1
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1
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2
1
1
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Imidazolylacetolphosphate:L-gl ...
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Biosynthesis of histidine: imi ...
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