Literature summary for 4.3.2.10 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 .

Search for more literature for 4.3.2.10

Protein Variants

Protein Variants	Comment	Organism
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
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
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]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	L-glutamine	pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes	Saccharomyces cerevisiae
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?
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

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P33734	-	-
Saccharomyces cerevisiae ATCC 204508	P33734	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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

Synonyms	Comment	Organism
IGP synthase	-	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	L-glutamine	pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes	Saccharomyces cerevisiae
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

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

General Information

General Information	Comment	Organism
metabolism	the enzyme participates in the pathway of histidine biosynthesis	Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
additional information	-	L-glutamine	pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes	Saccharomyces cerevisiae
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

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Release 2023.1 (January 2023)