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L-glutamine + H2O
L-glutamate + NH3
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
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
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
L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
for the IGP synthase holoenzyme L-glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000. The HisF subunit alone does not ulilize L-glutamine. It supports an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH4+
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
additional information
?
-
L-glutamine + H2O
L-glutamate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
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-
?
L-glutamine + H2O
L-glutamate + NH3
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme catalyzes two different reactions at two separate active sites. At the glutaminase active site, glutamine is hydrolyzed to glutamate and ammonia, which, at the synthase active site, reacts with the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate. Ammonia is channeled between glutaminase and synthase active sites
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme catalyzes two different reactions at two separate active sites. At the glutaminase active site, glutamine is hydrolyzed to glutamate and ammonia, which, at the synthase active site, reacts with the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate. Ammonia is channeled between glutaminase and synthase active sites
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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
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
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
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
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the imidazole glycerol phosphate synthase catalyzes formation of the imidazole ring in histidine biosynthesis
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme is also a glutamine amidotransferase, which produces ammonia in a glutaminase active site and channels it through a 30 A internal tunnel to a cyclase active site
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
the enzyme catalyzes a step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
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-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
the enzyme catalyzes a step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
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-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
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?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
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-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
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-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
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-
-
-
?
additional information
?
-
the glutaminase activity for the holoenzyme is 0.8% of that in the presence of the nucleotide substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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-
?
additional information
?
-
-
the glutaminase activity for the holoenzyme is 0.8% of that in the presence of the nucleotide substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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?
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
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?
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
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?
additional information
?
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the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog
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-
?
additional information
?
-
the glutaminase activity of the enzyme is stimulated 4900fold in the presence of the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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-
?
additional information
?
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-
the glutaminase activity of the enzyme is stimulated 4900fold in the presence of the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
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?
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0.0015
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
0.00027 - 0.24
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
additional information
additional information
-
kinetic model
-
0.0015
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
0.32
L-glutamine
pH 8.5, 25°C
0.49
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
1 - 4
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
1 - 4.5
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
1.3
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
1.7
L-glutamine
pH 7.0, 30°C
1.8
L-glutamine
pH 8.0, 30°C, wild-type enzyme
1.8
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
1.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
1.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
1.96
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
2.1
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
2.3
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
4.8
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
5.4
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
6.5
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
6.5
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
7
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
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
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
0.0016
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
0.0018
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
0.002
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
0.002
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
0.0023
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
0.0028
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: L-glutamine, HisH/HisF holoenzyme with a T78M mutant subunit HisF
0.003
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
0.0036
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
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
0.004
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
0.005
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
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
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
0.0059
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: NH4+, HisH/HisF holoenzyme with a T78M mutant subunit HisF
0.008
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
0.0125
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
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
0.0175
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
0.021
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit, saturating concentrations of ammonium chloride can not be achieved due to inhibition of the enzyme activity at chloride ion concentrations
0.0218
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
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
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
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
0.0426
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
0.046
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
0.053
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
0.055
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
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
0.065
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
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
0.072
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
0.075
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
0.08
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
0.098
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
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
0.139
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
0.24
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
15
NH3
pH 8.0, 30°C, HisF subunit
16
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
1 - 1.2
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
7.4
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
13.4
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
14.3
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
266
NH4+
pH 8.0, 30°C, HisF subunit
291
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
0.00029 - 9.1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
8.6
NH3
pH 8.0, 30°C, HisF subunit
additional information
additional information
-
kinetic model
-
0.0059
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
0.007
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
0.019
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
0.025
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
0.13
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
0.16
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
0.19
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
0.4
L-glutamine
pH 8.5, 25°C
0.49
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
0.6
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
1.13
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
1.4
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
5.2
L-glutamine
pH 7.0, 30°C
6
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
6.9
L-glutamine
pH 8.0, 30°C, wild-type enzyme
6.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
6.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
8.5
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
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
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
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
0.045
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
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
0.126
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
0.15
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
0.21
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
0.24
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
0.29
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
0.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
0.31
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
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
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
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
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
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
0.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
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
0.845
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
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
1.1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
1.2
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
3.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
3.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
3.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
4.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
5.2
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
5.2
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
5.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
5.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
5.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
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
5.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
8.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
9.1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
4.3
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
4.4
NH4+
pH 8.0, 30°C, IGP synthase enzyme enzyme with a E46G mutant subunit HisF
5.7
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
5.7
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
8.6
NH4+
pH 8.0, 30°C, HisF subunit
8.8
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00042 - 5700
L-glutamine
0.0006
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
0.016 - 2800
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
additional information
additional information
-
kinetic model
-
0.00042
L-glutamine
pH 8.0, 30°C, mutant enzyme D359A
0.0011
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
0.0028
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
0.0032
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A/D359A
0.0036
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
0.004
L-glutamine
pH 8.0, 30°C, mutant enzyme N13A
0.007
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
0.013
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
0.024
L-glutamine
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
0.084
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
0.21
L-glutamine
pH 8.0, 30°C, mutant enzyme Q397A
0.247
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
0.59
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
1.2
L-glutamine
pH 8.0, 30°C, mutant enzyme K196A
1.4
L-glutamine
pH 8.5, 25°C
3.1
L-glutamine
pH 7.0, 30°C
3.8
L-glutamine
pH 8.0, 30°C, wild-type enzyme
3.8
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
5700
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
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
0.039
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
0.12
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
0.46
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
0.5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
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
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
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
1.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
2.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
2.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
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
3.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
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
4.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
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
5.5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
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
11
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
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
15
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
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
38
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
60
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
110
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
120
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
130
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
240
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
270
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
300
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
300
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
950
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
1200
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
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
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
0.55
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
0.57
NH3
pH 8.0, 30°C, HisF subunit
0.03
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
0.032
NH4+
pH 8.0, 30°C, HisF subunit
0.392
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a E46G mutant subunit HisF
0.399
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a R5H mutant subunit HisF
0.425
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a Q123R mutant subunit HisF
0.581
NH4+
pH 8.0, 30°C, IGP synthase enzyme with a C124R mutant subunit HisF
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C124R
IGP synthases formed with Q123R mutant HisF subunit has no measurable activity with glutamine in vitro
E46G
IGP synthases formed with E46G mutant HisF subunit shows 2800fold reduction in the kcat/Km ratio for glutamine
Q123R
IGP synthases formed with Q123R mutant HisF subunit has no measurable activity with glutamine in vitro
R5H
IGP synthases formed with R5H mutant HisF subunit shows 1500fold reduction in the kcat/Km ratio for glutamine
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
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
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
K258A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 43:1 (wild-type ratio is 1:1), 2600fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 385fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1055fold decrease in kcat/Km of L-glutamine
K258R
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 3:1 (wild-type ratio is 1:1), 20fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 125fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 45fold decrease in kcat/Km of L-glutamine
K360R
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 1:1 (identical to wild-type ratio), 1090fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 3.5fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 6.4fold decrease in kcat/Km of L-glutamine
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
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
R239A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 122:1 (wild-type ratio is 1:1), 860fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 5.4fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 3450fold decrease in kcat/Km of L-glutamine
R239H
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 154:1 (wild-type ratio is 1:1), 2400fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 5.2fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1360fold decrease in kcat/Km of L-glutamine
R239K
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 40:1 (wild-type ratio is 1:1), 218fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 3.9fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 540fold decrease in kcat/Km of L-glutamine
R360A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 3:1 (wild-type ratio is 1:1), 9.2fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 1.4fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 15fold decrease in kcat/Km of L-glutamine
C9A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
D11N
mutation in subunit HisF. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
D130N
the kcat value is reduced by a factor of about 400-500, and the Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is increased almost 20fold. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
D176N
mutation in subunit HisF. The variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
D183N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
D51N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
K19S
mutation in subunit HisF. The ammonia-dependent reactions of isolated subunit HisF_K19S is similarly efficient as that of wild-type HisF. The efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired
N103A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
T78M
-
the mutation does not impair substrate binding to the active site of HisF
D130N
-
the kcat value is reduced by a factor of about 400-500, and the Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is increased almost 20fold. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
-
D176N
-
mutation in subunit HisF. The variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
-
D183N
-
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
-
D51N
-
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
-
additional information
eight conserved amino acids at the putative active site of subunit HisF are exchanged by site-directed mutagenesis, and the purified variants are investigated by steady state kinetics. Aspartate 11 appears to be essential for the synthase activity both in vitro and in vivo, and aspartate 130 can be partially replaced only by glutamate
additional information
-
eight conserved amino acids at the putative active site of subunit HisF are exchanged by site-directed mutagenesis, and the purified variants are investigated by steady state kinetics. Aspartate 11 appears to be essential for the synthase activity both in vitro and in vivo, and aspartate 130 can be partially replaced only by glutamate
additional information
-
eight conserved amino acids at the putative active site of subunit HisF are exchanged by site-directed mutagenesis, and the purified variants are investigated by steady state kinetics. Aspartate 11 appears to be essential for the synthase activity both in vitro and in vivo, and aspartate 130 can be partially replaced only by glutamate
-
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Klem, T.J.; Davisson, V.J.
Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis
Biochemistry
32
5177-5186
1993
Escherichia coli (P60595 and P60664), Escherichia coli
brenda
Chaudhuri, B.N.; Lange, S.C.; Myers, R.S.; Davisson, V.J.; Smith, J.L.
Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme
Biochemistry
42
7003-7012
2003
Saccharomyces cerevisiae (P33734)
brenda
Myers, R.S.; Jensen, J.R.; Deras, I.L.; Smith, J.L.; Davisson, V.J.
Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase
Biochemistry
42
7013-7022
2003
Saccharomyces cerevisiae (P33734), Saccharomyces cerevisiae
brenda
Myers, R.S.; Amaro, R.E.; Luthey-Schulten, Z.A.; Davisson, V.J.
Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase
Biochemistry
44
11974-11985
2005
Saccharomyces cerevisiae (P33734)
brenda
Demin, O.V.; Goryanin, I.I.; Dronov, S.; Lebedeva, G.V.
Kinetic model of imidazologlycerol-phosphate synthetase from Escherichia coli
Biochemistry
69
1324-1335
2004
Escherichia coli
brenda
Klem, T.J.; Chen, Y.; Davisson, V.J.
Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase
J. Bacteriol.
182
989-996
2001
Escherichia coli (P60595 and P60664)
-
brenda
Omi, R.; Mizuguchi, H.; Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.
Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunneling
J. Biochem.
132
759-765
2002
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Chittur, S.V.; Chen, Y.; Davisson, V.J.
Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae
Protein Expr. Purif.
18
366-377
2000
Saccharomyces cerevisiae (P33734), Saccharomyces cerevisiae
brenda
Liebold, C.; List, F.; Kalbitzer, H.R.; Sterner, R.; Brunner, E.
The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy
Protein Sci.
19
1774-1782
2010
Thermotoga maritima
brenda
Douangamath, A.; Walker, M.; Beismann-Driemeyer, S.; Vega-Fernandez, M.C.; Sterner, R.; Wilmanns, M.
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex
Structure
10
185-193
2002
Thermotoga maritima (Q9X0C8 and Q9X0C6), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X0C8 and Q9X0C6)
brenda
Chaudhuri, B.N.; Lange, S.C.; Myers, R.S.; Chittur, S.V.; Davisson, V.J.; Smith, J.L.
Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites
Structure
9
987-997
2001
Saccharomyces cerevisiae (P33734), Saccharomyces cerevisiae
brenda
Beismann-Driemeyer, S.; Sterner, R.
Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex
J. Biol. Chem.
276
20387-20396
2001
Thermotoga maritima (Q9X0C8 and Q9X0C6), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X0C8 and Q9X0C6)
brenda