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

Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase

Myers, R.S.; Amaro, R.E.; Luthey-Schulten, Z.A.; Davisson, V.J.; Biochemistry 44, 11974-11985 (2005)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 7.5fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
K196A
0.43fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 3fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
K196A/D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
N13A
130fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 3fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 350fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
Q397A
7.5fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 18fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00027
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
Saccharomyces cerevisiae
0.0013
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
0.0036
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.005
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
0.0055
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
0.0141
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.026
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.03
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
0.034
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
0.055
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
0.071
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
0.109
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
0.49
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
1
4
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
1.8
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
2.3
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
4.8
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
7
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P33734
-
-
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
-
726941
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
additional information
the enzyme also shows glutaminase activity. The glutaminase activity of the glutaminase domain is tightly regulated by the acceptor substrate domain. In IGP synthase the glutaminase and N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding sites are separated by 30 A. Using kinetic analyses of site-specific mutants and molecular dynamic simulations, it is determined that an interdomain salt bridge in IGP synthase between D359 and K196 (approximately 16 A from the N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding site) plays a key role in mediating communication between the two active sites. This interdomain contact modulates the glutaminase loop containing the histidine and glutamic acid of the catalytic triad to control glutamine hydrolysis
726941
Saccharomyces cerevisiae
?
-
-
-
-
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
726941
Saccharomyces cerevisiae
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
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
0.00029
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
0.0059
-
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
0.007
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.007
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.01
1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
0.019
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
0.11
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.35
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
0.38
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
0.39
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
0.46
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
0.56
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.6
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
0.74
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
Saccharomyces cerevisiae
0.845
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
1.4
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
Saccharomyces cerevisiae
5.4
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
6.9
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 7.5fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
K196A
0.43fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 3fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
K196A/D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
N13A
130fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 3fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 350fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
Q397A
7.5fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 18fold decrease in kcat/Km of L-glutamine
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00027
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
Saccharomyces cerevisiae
0.0013
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
0.0036
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.005
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
0.0055
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
0.0141
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.026
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.03
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
0.034
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
0.055
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
0.071
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
0.109
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
0.49
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
1
4
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
1.8
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
2.3
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
4.8
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
7
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
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
-
726941
Saccharomyces cerevisiae
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
additional information
the enzyme also shows glutaminase activity. The glutaminase activity of the glutaminase domain is tightly regulated by the acceptor substrate domain. In IGP synthase the glutaminase and N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding sites are separated by 30 A. Using kinetic analyses of site-specific mutants and molecular dynamic simulations, it is determined that an interdomain salt bridge in IGP synthase between D359 and K196 (approximately 16 A from the N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding site) plays a key role in mediating communication between the two active sites. This interdomain contact modulates the glutaminase loop containing the histidine and glutamic acid of the catalytic triad to control glutamine hydrolysis
726941
Saccharomyces cerevisiae
?
-
-
-
-
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
726941
Saccharomyces cerevisiae
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
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
0.00029
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
0.0059
-
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
0.007
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.007
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.01
1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
0.019
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
0.11
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.35
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
0.38
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
0.39
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
0.46
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
0.56
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.6
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
0.74
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
Saccharomyces cerevisiae
0.845
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
1.4
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
Saccharomyces cerevisiae
5.4
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
6.9
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Saccharomyces cerevisiae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00042
-
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
0.0032
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.004
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
0.016
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.21
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
Saccharomyces cerevisiae
0.51
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.52
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
1.2
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
1.2
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
3.6
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
3.8
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
3.8
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
4.9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
14
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
15
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
1200
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
2800
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
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
0.00042
-
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
Saccharomyces cerevisiae
0.0032
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.004
-
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
Saccharomyces cerevisiae
0.016
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
Saccharomyces cerevisiae
0.21
-
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
Saccharomyces cerevisiae
0.51
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
0.52
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
Saccharomyces cerevisiae
1.2
-
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
Saccharomyces cerevisiae
1.2
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
Saccharomyces cerevisiae
3.6
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
Saccharomyces cerevisiae
3.8
-
L-glutamine
pH 8.0, 30°C, wild-type enzyme
Saccharomyces cerevisiae
3.8
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
Saccharomyces cerevisiae
4.9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
Saccharomyces cerevisiae
9
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
Saccharomyces cerevisiae
14
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
Saccharomyces cerevisiae
15
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
Saccharomyces cerevisiae
1200
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
Saccharomyces cerevisiae
2800
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
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