BRENDA - Enzyme Database
show all sequences of 4.3.2.10

Imidazole glycerol phosphate synthase the glutamine amidotransferase in histidine biosynthesis

Klem, T.J.; Davisson, V.J.; Biochemistry 32, 5177-5186 (1993)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
Escherichia coli
N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
Escherichia coli
Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli FB1
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
0.023
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
0.24
-
L-glutamine
pH 8.0, 30C
Escherichia coli
291
-
NH4+
pH 8.0, 30C
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47500
-
1:1 dimeric complex of HisH and HisF proteins, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
Escherichia coli
the enzyme is involved in histidine biosynthesis
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
Escherichia coli K12
the enzyme is involved in histidine biosynthesis
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia coli K12
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
the enzyme is involved in histidine biosynthesis
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
the enzyme is involved in histidine biosynthesis
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
1 * 21653 (subunit HisH) + 1 * 28454 (subunit HisF), calculated from sequence, HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the IGP synthase holoenzyme
Escherichia coli
Synonyms
Synonyms
Commentary
Organism
hisFH
-
Escherichia coli
IGP synthase
-
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.1
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
8.5
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
8.8
-
NH4+
pH 8.0, 30C
Escherichia coli
9.1
-
L-glutamine
pH 8.0, 30C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
activity with glutamine
Escherichia coli
8
9
activity with NH4+
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
9.5
the pH optimum with glutamine is broad over the range of values from 6.0 to 8.0 but diminishes to 85% at pH 8.5 and 22% at pH 9.5
Escherichia coli
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
Escherichia coli
N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli FB1
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
0.023
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
0.24
-
L-glutamine
pH 8.0, 30C
Escherichia coli
291
-
NH4+
pH 8.0, 30C
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47500
-
1:1 dimeric complex of HisH and HisF proteins, gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
Escherichia coli
the enzyme is involved in histidine biosynthesis
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
Escherichia coli K12
the enzyme is involved in histidine biosynthesis
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
the enzyme is involved in histidine biosynthesis
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
the enzyme is involved in histidine biosynthesis
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
747052
Escherichia coli K12
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
1 * 21653 (subunit HisH) + 1 * 28454 (subunit HisF), calculated from sequence, HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the IGP synthase holoenzyme
Escherichia coli
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.1
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
8.5
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
8.8
-
NH4+
pH 8.0, 30C
Escherichia coli
9.1
-
L-glutamine
pH 8.0, 30C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
activity with glutamine
Escherichia coli
8
9
activity with NH4+
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
9.5
the pH optimum with glutamine is broad over the range of values from 6.0 to 8.0 but diminishes to 85% at pH 8.5 and 22% at pH 9.5
Escherichia coli
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in histidine biosynthesis
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in histidine biosynthesis
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.03
-
NH4+
pH 8.0, 30C
Escherichia coli
37.9
-
L-glutamine
pH 8.0, 30C
Escherichia coli
265.2
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
5667
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.03
-
NH4+
pH 8.0, 30C
Escherichia coli
37.9
-
L-glutamine
pH 8.0, 30C
Escherichia coli
265.2
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: NH4+
Escherichia coli
5667
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 30C, cosubstrate: L-glutamine
Escherichia coli
Other publictions for EC 4.3.2.10
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
Synonyms
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)
747861
Lisi
Glutamine hydrolysis by imida ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Front. Mol. Biosci.
5
4
2018
1
-
2
-
-
-
-
15
-
-
-
2
-
9
-
-
2
-
-
-
-
-
8
-
2
1
1
-
15
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
15
-
-
-
2
-
-
-
2
-
-
-
-
8
-
1
1
-
15
1
-
-
-
-
1
1
-
15
15
749186
Lisi
Altering the allosteric pathw ...
Thermotoga maritima
Proc. Natl. Acad. Sci. USA
114
E3414-E3423
2017
-
2
-
-
4
-
-
10
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
10
-
-
-
-
-
-
-
-
2
-
-
-
4
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
10
-
-
-
-
-
1
1
-
10
10
749258
Holinski
Combining ancestral sequence ...
Pyrobaculum arsenaticum, Zymomonas mobilis, Pyrobaculum arsenaticum DSM 13514, Zymomonas mobilis ZM4
Proteins
85
312-321
2017
-
-
2
-
-
-
-
-
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747112
Rivalta
Allosteric communication disr ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Biochemistry
55
6484-6494
2016
-
2
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
749239
Liebold
The interaction of ammonia an ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Protein Sci.
19
1774-1782
2010
-
-
1
-
1
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
748246
Lipchock
Millisecond dynamics in the a ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
J. Biomol. NMR
45
73-84
2009
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747285
Amaro
Structural elements in IGP sy ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Biophys. J.
89
475-487
2005
-
-
-
-
3
-
-
2
-
-
-
2
-
5
-
-
1
-
-
-
-
-
6
-
1
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1
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6
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2
1
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1
1
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2
2
747057
Chaudhuri
Toward understanding the mech ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Biochemistry
42
7003-7012
2003
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1
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5
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6
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1
1
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747058
Myers
Substrate-induced changes in ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Biochemistry
42
7013-7022
2003
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7
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3
16
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5
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4
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1
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16
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7
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3
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16
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4
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16
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16
16
748120
Omi
Structure of imidazole glycer ...
Thermus thermophilus
J. Biochem.
132
759-765
2002
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1
1
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1
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2
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1
1
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749381
Douangamath
Structural evidence for ammon ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
Structure
10
185-193
2002
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1
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2
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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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4
1
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1
1
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746612
Banfield
Structure of HisF, a histidin ...
Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523
Acta Crystallogr. Sect. D
57
1518-1525
2001
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1
1
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2
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1
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748148
Beismann-Driemeyer
Imidazole glycerol phosphate ...
Thermotoga maritima, Thermotoga maritima ATCC 43589
J. Biol. Chem.
276
20387-20396
2001
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1
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7
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4
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2
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6
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1
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1
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7
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1
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6
1
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4
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1
1
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4
4
749228
Chittur
Expression and purification o ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Protein Expr. Purif.
18
366-377
2000
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1
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3
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5
2
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5
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1
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2
2
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3
2
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3
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2
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1
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1
6
2
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3
2
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1
1
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3
3
747754
Fujimori
An Arabidopsis cDNA encoding ...
Arabidopsis thaliana
FEBS Lett.
428
229-234
1998
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1
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7
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747052
Klem
Imidazole glycerol phosphate ...
Escherichia coli, Escherichia coli K12
Biochemistry
32
5177-5186
1993
2
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1
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4
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1
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1
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2
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1
1
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2
1
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1
1
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4
4