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Literature summary extracted from

  • Amaro, R.E.; Myers, R.S.; Davisson, V.J.; Luthey-Schulten, Z.A.
    Structural elements in IGP synthase exclude water to optimize ammonia transfer (2005), Biophys. J., 89, 475-487 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.10 K360A formation of a larger opening between chamber I and chamber II, mutation results in a threefold decrease in the overall reaction stoichiometry. Although the mutation facilitates the passage of ammonia into the channel, without the lysine side chain the ammonia diffuses more easily around the interface Saccharomyces cerevisiae
4.3.2.10 R239A the mutation creates a large hole in the exposed side of the interface, the mutation results in a 1000 decrease in kcat/Km values for the cyclase reaction, the mutation allows bulk water molecules to penetrate chamber II, thereby disrupting the passage of ammonia and destroying the tightly coupled reaction kinetics Saccharomyces cerevisiae
4.3.2.10 Y144F no loss in protein function occurrs with the Y138F mutation. This indicates that the main function of this residue is to prevent bulk water from entering the interface during the reaction and keep ammonia sequestered within the intermolecular channel Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.2.10 additional information
-
 L-glutamine pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae
4.3.2.10 additional information
-
 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine Saccharomyces cerevisiae the enzyme participates in the pathway of histidine biosynthesis 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine Saccharomyces cerevisiae ATCC 204508 the enzyme participates in the pathway of histidine biosynthesis 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.10 Saccharomyces cerevisiae P33734
-
-
4.3.2.10 Saccharomyces cerevisiae ATCC 204508 P33734
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.2.10 His-tagged IGP synthase Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the enzyme participates in the pathway of histidine biosynthesis Saccharomyces cerevisiae 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the first domain of IGP synthase, a triad glutamine amidotransferase, hydrolyzes glutamine to form glutamate and ammonia. Its activity is tightly regulated by the binding of the substrate 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide to its partner synthase domain. Structural elements in IGP synthase exclude water to optimize ammonia transfer Saccharomyces cerevisiae 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the enzyme participates in the pathway of histidine biosynthesis Saccharomyces cerevisiae ATCC 204508 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine the first domain of IGP synthase, a triad glutamine amidotransferase, hydrolyzes glutamine to form glutamate and ammonia. Its activity is tightly regulated by the binding of the substrate 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide to its partner synthase domain. Structural elements in IGP synthase exclude water to optimize ammonia transfer Saccharomyces cerevisiae ATCC 204508 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
-
 Saccharomyces cerevisiae 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
 ?
4.3.2.10 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
-
 Saccharomyces cerevisiae ATCC 204508 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.2.10 IGP synthase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.2.10 additional information
-
 L-glutamine pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae
4.3.2.10 additional information
-
 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.2.10 7
-
 assay at Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
4.3.2.10 metabolism the enzyme participates in the pathway of histidine biosynthesis 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
4.3.2.10 additional information
-
 L-glutamine pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae
4.3.2.10 additional information
-
 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes Saccharomyces cerevisiae