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Literature summary extracted from

  • Myers, R.S.; Amaro, R.E.; Luthey-Schulten, Z.A.; Davisson, V.J.
    Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase (2005), Biochemistry, 44, 11974-11985.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 0.49
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A Saccharomyces cerevisiae
4.3.1.B2 1 4 L-glutamine pH 8.0, 30°C, mutant enzyme D359A Saccharomyces cerevisiae
4.3.1.B2 1.8
-
L-glutamine pH 8.0, 30°C, wild-type enzyme Saccharomyces cerevisiae
4.3.1.B2 2.3
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A/D359A Saccharomyces cerevisiae
4.3.1.B2 4.8
-
L-glutamine pH 8.0, 30°C, mutant enzyme N13A Saccharomyces cerevisiae
4.3.1.B2 7
-
L-glutamine pH 8.0, 30°C, mutant enzyme Q397A Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.B2 Saccharomyces cerevisiae P33734
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.B2 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
-
?
4.3.1.B2 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 Saccharomyces cerevisiae ?
-
?
4.3.1.B2 NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
Saccharomyces cerevisiae D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
?

Synonyms

EC Number Synonyms Comment Organism
4.3.1.B2 IGP synthase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.B2 30
-
assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.B2 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
4.3.1.B2 0.0059
-
L-glutamine pH 8.0, 30°C, mutant enzyme D359A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 0.007
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A/D359A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 0.019
-
L-glutamine pH 8.0, 30°C, mutant enzyme N13A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 0.6
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 1.4
-
L-glutamine pH 8.0, 30°C, mutant enzyme Q397A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 6.9
-
L-glutamine pH 8.0, 30°C, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.B2 7
-
assay at Saccharomyces cerevisiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.1.B2 0.00042
-
L-glutamine pH 8.0, 30°C, mutant enzyme D359A Saccharomyces cerevisiae
4.3.1.B2 0.0032
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A/D359A Saccharomyces cerevisiae
4.3.1.B2 0.004
-
L-glutamine pH 8.0, 30°C, mutant enzyme N13A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 0.21
-
L-glutamine pH 8.0, 30°C, mutant enzyme Q397A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 1.2
-
L-glutamine pH 8.0, 30°C, mutant enzyme K196A Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 3.8
-
L-glutamine pH 8.0, 30°C, wild-type enzyme Saccharomyces cerevisiae
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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
4.3.1.B2 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