BRENDA - Enzyme Database show
show all sequences of 4.3.1.B2

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)
Commentary
Organism
expressed in a bacterial system 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
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
Saccharomyces cerevisiae
1.7
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
gel filtration
Saccharomyces cerevisiae
61000
-
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
61082
-
1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
Saccharomyces cerevisiae
-
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P33734
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition
the production of the soluble HIS7 is highest at 25C with 1 mM isopropyl beta-D-thiogalactopyranoside and this condition is used for the large-scale protein preparations
Saccharomyces cerevisiae
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728731
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728731
Saccharomyces cerevisiae
L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
additional information
the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog
728731
Saccharomyces cerevisiae
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain; 1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
Saccharomyces cerevisiae
5.2
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in a bacterial system 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
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
Saccharomyces cerevisiae
1.7
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
gel filtration
Saccharomyces cerevisiae
61000
-
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
61082
-
1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
Saccharomyces cerevisiae
-
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition
the production of the soluble HIS7 is highest at 25C with 1 mM isopropyl beta-D-thiogalactopyranoside and this condition is used for the large-scale protein preparations
Saccharomyces cerevisiae
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728731
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728731
Saccharomyces cerevisiae
L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
additional information
the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog
728731
Saccharomyces cerevisiae
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain; 1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
Saccharomyces cerevisiae
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
Saccharomyces cerevisiae
5.2
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Saccharomyces cerevisiae
General Information
General Information
Commentary
Organism
physiological function
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
Saccharomyces cerevisiae
General Information (protein specific)
General Information
Commentary
Organism
physiological function
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
3.1
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
950
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
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
3.1
-
L-glutamine
pH 7.0, 30C
Saccharomyces cerevisiae
950
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30C
Saccharomyces cerevisiae
Other publictions for EC 4.3.1.B2
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)
728756
Liebold
The interaction of ammonia and ...
Thermotoga maritima
Protein Sci.
19
1774-1782
2010
-
-
1
-
1
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
726941
Myers
Reaction coupling through inte ...
Saccharomyces cerevisiae
Biochemistry
44
11974-11985
2005
-
-
-
-
5
-
-
18
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
18
18
727051
Demin
Kinetic model of imidazologlyc ...
Escherichia coli
Biochemistry
69
1324-1335
2004
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
726938
Chaudhuri
Toward understanding the mecha ...
Saccharomyces cerevisiae
Biochemistry
42
7003-7012
2003
-
-
-
1
-
-
2
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726939
Myers
Substrate-induced changes in t ...
Saccharomyces cerevisiae
Biochemistry
42
7013-7022
2003
-
-
-
-
7
-
3
22
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
1
-
-
22
1
-
-
-
7
-
-
-
-
-
-
-
7
-
-
3
7
22
-
-
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
22
1
-
-
-
-
-
-
-
24
24
727791
Omi
Structure of imidazole glycero ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biochem.
132
759-765
2002
-
-
-
1
-
-
-
-
-
-
-
2
-
93
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
728807
Douangamath
Structural evidence for ammoni ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Structure
10
185-193
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
727736
Klem
-
Subunit interactions and gluta ...
Escherichia coli
J. Bacteriol.
182
989-996
2001
-
-
1
-
4
-
-
10
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
10
-
-
-
1
-
-
-
1
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
-
-
9
9
728818
Chaudhuri
Crystal structure of imidazole ...
Saccharomyces cerevisiae
Structure
9
987-997
2001
-
-
-
1
-
-
1
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
748148
Beismann-Driemeyer
Imidazole glycerol phosphate ...
Thermotoga maritima, Thermotoga maritima DSM 3109
J. Biol. Chem.
276
20387-20396
2001
-
-
1
-
9
-
-
2
-
-
-
-
-
6
-
-
1
-
-
-
-
-
6
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
9
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
6
-
1
-
-
2
1
-
-
-
-
1
1
-
2
2
728731
Chittur
Expression and purification of ...
Saccharomyces cerevisiae
Protein Expr. Purif.
18
366-377
2000
-
-
1
-
-
-
-
2
-
-
3
1
-
3
-
-
1
-
-
1
-
-
3
1
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
3
1
-
-
-
1
-
1
-
-
3
1
1
-
-
2
1
-
-
-
-
1
1
-
2
2
726928
Klem
Imidazole glycerol phosphate s ...
Escherichia coli
Biochemistry
32
5177-5186
1993
-
-
1
-
-
-
2
7
-
-
5
1
-
2
-
-
1
3
-
-
-
1
4
1
1
-
1
6
3
2
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
7
-
-
5
1
-
-
-
1
-
-
-
1
4
1
1
-
1
6
3
2
-
-
-
-
-
-
7
7