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Literature summary for 4.3.1.B2 extracted from

  • Klem, T.J.; Davisson, V.J.
    Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis (1993), Biochemistry, 32, 5177-5186.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
MgCl2 10 mM, activity is reduced by 22% Escherichia coli
MnCl2 10 mM, activity is reduced by 58% Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
L-glutamine pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
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 Escherichia coli
0.24
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
15
-
NH3 pH 8.0, 30°C, HisF subunit Escherichia coli
16
-
NH3 pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
266
-
NH4+ pH 8.0, 30°C, HisF subunit Escherichia coli
291
-
NH4+ pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
11600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli
21655
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli
28457
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli
31600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli
47500
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine Escherichia coli 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 L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P60595 and P60664 P60595: IGP synthase glutamine amidotransferase subunit, P60664: IGP synthase cyclase subunit
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-glutamine + H2O = L-glutamate + NH3 (1a) Escherichia coli
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 overall reaction Escherichia coli
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 (1b) Escherichia coli

Storage Stability

Storage Stability Organism
27°C, 30 days, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Escherichia coli ?
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine 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 Escherichia coli L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 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 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 Escherichia coli D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 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 + NH4+ 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 Escherichia coli D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide 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 ?

Subunits

Subunits Comment Organism
dimer 1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli
dimer 1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme Escherichia coli

Synonyms

Synonyms Comment Organism
HIS7
-
Escherichia coli
IGP synthase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
27
-
30 d, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity. The HisF and HisH proteins exhibit half-lives of less than 48 h under similar conditions Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.7
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate pH 8.0, 30°C, HisF subunit Escherichia coli
8.5
-
L-glutamine pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
8.6
-
NH3 pH 8.0, 30°C, HisF subunit Escherichia coli
8.6
-
NH4+ pH 8.0, 30°C, HisF subunit Escherichia coli
8.8
-
NH4+ pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
9.1
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8 L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme Escherichia coli
8
-
assay at Escherichia coli
8 9 ammonia-dependent activity catalyzed by HisF Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
8.5
-
85% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme Escherichia coli
9.5
-
22% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.03
-
NH4+ pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
0.032
-
NH4+ pH 8.0, 30°C, HisF subunit Escherichia coli
0.55
-
NH3 pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
0.57
-
NH3 pH 8.0, 30°C, HisF subunit Escherichia coli
38
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli
270
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate pH 8.0, 30°C, HisF subunit Escherichia coli
5700
-
L-glutamine pH 8.0, 30°C, IGP synthase holoenzyme Escherichia coli