BRENDA - Enzyme Database
show all sequences of 4.3.2.10

Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae

Chittur, S.V.; Chen, Y.; Davisson, V.J.; Protein Expr. Purif. 18, 366-377 (2000)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
catalytically active yeast HIS7 is expressed in Escherichia coli under the control of T7 polymerase promoter
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
1.7
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
246
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
gel filtration
Saccharomyces cerevisiae
57000
-
equilibrium sedimentation
Saccharomyces cerevisiae
61000
-
SDS-PAGE
Saccharomyces cerevisiae
61003
-
MALDI MS
Saccharomyces cerevisiae
61082
-
calculated from sequence
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
the enzyme represents a junction between histidine biosynthesis and de novo purine 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
Saccharomyces cerevisiae ATCC 204508
the enzyme represents a junction between histidine biosynthesis and de novo purine 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
Saccharomyces cerevisiae
P33734
-
-
Saccharomyces cerevisiae ATCC 204508
P33734
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme
Saccharomyces cerevisiae
Storage Stability
Storage Stability
Organism
-80°C, stored without loss of activity
Saccharomyces cerevisiae
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
-
749228
Saccharomyces cerevisiae
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 represents a junction between histidine biosynthesis and de novo purine biosynthesis
749228
Saccharomyces cerevisiae
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
-
749228
Saccharomyces cerevisiae ATCC 204508
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 represents a junction between histidine biosynthesis and de novo purine biosynthesis
749228
Saccharomyces cerevisiae ATCC 204508
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+
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
749228
Saccharomyces cerevisiae
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+
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
749228
Saccharomyces cerevisiae ATCC 204508
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
monomer
1 * 61000, SDS-PAGE
Saccharomyces cerevisiae
monomer
1 * 61082, calculated from sequence
Saccharomyces cerevisiae
Synonyms
Synonyms
Commentary
Organism
HIS7
-
Saccharomyces cerevisiae
IGP synthase
-
Saccharomyces cerevisiae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
3.9
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
5.2
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
glutamine-dependent activity
Saccharomyces cerevisiae
7
8.5
NH4+-dependent activity
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
catalytically active yeast HIS7 is expressed in Escherichia coli under the control of T7 polymerase promoter
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.004
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
1.7
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
246
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
gel filtration
Saccharomyces cerevisiae
57000
-
equilibrium sedimentation
Saccharomyces cerevisiae
61000
-
SDS-PAGE
Saccharomyces cerevisiae
61003
-
MALDI MS
Saccharomyces cerevisiae
61082
-
calculated from sequence
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
the enzyme represents a junction between histidine biosynthesis and de novo purine 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
Saccharomyces cerevisiae ATCC 204508
the enzyme represents a junction between histidine biosynthesis and de novo purine 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
recombinant enzyme
Saccharomyces cerevisiae
Storage Stability (protein specific)
Storage Stability
Organism
-80°C, stored without loss of activity
Saccharomyces cerevisiae
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
-
749228
Saccharomyces cerevisiae
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 represents a junction between histidine biosynthesis and de novo purine biosynthesis
749228
Saccharomyces cerevisiae
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
-
749228
Saccharomyces cerevisiae ATCC 204508
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 represents a junction between histidine biosynthesis and de novo purine biosynthesis
749228
Saccharomyces cerevisiae ATCC 204508
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+
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
749228
Saccharomyces cerevisiae
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+
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
749228
Saccharomyces cerevisiae ATCC 204508
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
monomer
1 * 61000, SDS-PAGE
Saccharomyces cerevisiae
monomer
1 * 61082, calculated from sequence
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
3.9
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
5.2
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
glutamine-dependent activity
Saccharomyces cerevisiae
7
8.5
NH4+-dependent activity
Saccharomyces cerevisiae
General Information
General Information
Commentary
Organism
metabolism
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
Saccharomyces cerevisiae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
3.1
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
950
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.024
-
NH4+
pH 7.0, 30°C
Saccharomyces cerevisiae
3.1
-
L-glutamine
pH 7.0, 30°C
Saccharomyces cerevisiae
950
-
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
Saccharomyces cerevisiae
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
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
2
-
-
-
2
-
-
-
1
-
-
-
-
6
-
-
-
-
2
1
-
-
-
-
1
1
-
2
2
747057
Chaudhuri
Toward understanding the mech ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Biochemistry
42
7003-7012
2003
-
-
-
1
-
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
747058
Myers
Substrate-induced changes in ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508
Biochemistry
42
7013-7022
2003
-
-
-
-
7
-
3
16
-
-
-
-
-
5
-
-
-
-
-
-
-
-
4
-
1
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
3
-
16
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
16
-
-
-
-
-
-
-
-
16
16
748120
Omi
Structure of imidazole glycer ...
Thermus thermophilus
J. Biochem.
132
759-765
2002
-
-
1
1
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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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6
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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
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2
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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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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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2
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5
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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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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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