Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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 + NH3
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
the HisH subunit catalyzes Gln hydrolysis, and the HisF subunit catalyzes the cyclization of the allosteric activator 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide. Ammonia generated in the HisH reaction traverses the dimer interface, where it is used as a substrate in the HisF reaction
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
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--D-ribosyl)imidazole-4-carboxamide + NH3
5-amino-1-(5-phospho--D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
L-glutamine + H2O
L-glutamate + NH3
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the formation of the imidazole ring in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme participates in the pathway of histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
4900fold upregulation of glutamine hydrolysis in the presence of an acceptor substrate. Transfer of ammonia from the glutaminase site occurs through the (beta/alpha)(8) core of the protein. The conserved K258 residue is key to productive binding and the overall stoichiometry of the reaction. The binding of the ribulosyl phosphate portion of the substrate appears to be transduced through reorientation of K258 resulting in a conformational switch at the base of the (beta/alpha)(8) core that enables the passage of ammonia through the core of the protein
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
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
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the formation of the imidazole ring in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
4900fold upregulation of glutamine hydrolysis in the presence of an acceptor substrate. Transfer of ammonia from the glutaminase site occurs through the (beta/alpha)(8) core of the protein. The conserved K258 residue is key to productive binding and the overall stoichiometry of the reaction. The binding of the ribulosyl phosphate portion of the substrate appears to be transduced through reorientation of K258 resulting in a conformational switch at the base of the (beta/alpha)(8) core that enables the passage of ammonia through the core of the protein
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme participates in the pathway of histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
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
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme links histidine and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000 and 100fold, respectively, despite the active sites being more than 25 A apart
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme links histidine and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000 and 100fold, respectively, despite the active sites being more than 25 A apart
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme links histidine and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
-
glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
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+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
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+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
the yeast enzyme is distinguished from the Escherichia coli IGP synthase in its utilization of ammonia as a substrate
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
ammonia-dependent ImGP synthase reaction of isolated HisF subunit
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
ammonia-dependent ImGP synthase reaction of isolated HisF subunit
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho--D-ribosyl)imidazole-4-carboxamide + NH3
5-amino-1-(5-phospho--D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000 and 100-fold, respectively, despite the active sites being more than 25 A apart
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho--D-ribosyl)imidazole-4-carboxamide + NH3
5-amino-1-(5-phospho--D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000 and 100-fold, respectively, despite the active sites being more than 25 A apart
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
binding of the allosteric effector ligand 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide stimulates millisecond timescale motions in IGPS that enhance its catalytic function. Allosteric activation decreases to 65-fold at 70°C, compared to 4200-fold at 30°C
-
-
?
L-glutamine + H2O
L-glutamate + NH3
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000- and 100fold, respectively, despite the active sites being more than 25 A apart
-
-
?
L-glutamine + H2O
L-glutamate + NH3
the HisH subunit catalyzes Gln hydrolysis, and the HisF subunit catalyzes the cyclization of the allosteric activator 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide. Ammonia generated in the HisH reaction traverses the dimer interface, where it is used as a substrate in the HisF reaction
-
-
?
L-glutamine + H2O
L-glutamate + NH3
binding of the allosteric effector ligand 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide stimulates millisecond timescale motions in IGPS that enhance its catalytic function. Allosteric activation decreases to 65-fold at 70°C, compared to 4200-fold at 30°C
-
-
?
L-glutamine + H2O
L-glutamate + NH3
IGPS heterodimeric enzyme comprised of two proteins, HisH and HisF, that catalyze the hydrolysis of glutamine to produce NH3 in the HisH active site and the cyclization of ammonia with 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide in HisF to produce 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate. Binding of 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide and D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate stimulates glutaminase activity in the HisH enzyme over 5000- and 100fold, respectively, despite the active sites being more than 25 A apart
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
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
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
-
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the formation of the imidazole ring in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme participates in the pathway of histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the formation of the imidazole ring in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme participates in the pathway of histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme links histidine and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme is involved in histidine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme links histidine and de novo purine biosynthesis
-
-
?
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate
the enzyme catalyzes the step in the histidine biosynthetic pathway located at the branch point to de novo purine biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0015 - 0.139
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
additional information
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.0015
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 25°C, wild-type HisH-HisF complex
0.0015
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: L-glutamine
0.0016
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K
0.0017
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
0.0018
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A
0.002
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R
0.0023
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R
0.003
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A
0.004
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
0.005
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, wild-type enzyme
0.0079
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H
0.023
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: NH4+
0.046
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R
0.053
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A
0.055
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme
0.065
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A
0.072
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R
0.075
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H
0.08
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K
0.098
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A
0.139
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A
0.24
L-glutamine
-
pH 8.0, 30°C
0.32
L-glutamine
pH 8.0, 25°C, wild-type HisH-HisF complex
1.3
L-glutamine
pH 8.0, 30°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.32
L-glutamine
pH 8.0, 70°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.35
L-glutamine
pH 8.0, 40°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.36
L-glutamine
pH 8.0, 60°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.4
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.64
L-glutamine
pH 8.0, 50°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.7
L-glutamine
pH 7.0, 30°C
1.74
L-glutamine
pH 8.0, 37°C, wild-type enzyme, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.99
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V48A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
2.88
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme D98A
2.96
L-glutamine
pH 8.0, 70°C
2.96
L-glutamine
pH 8.0, 70°C, basal activity
3
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A
3.11
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme D98A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3.41
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3.57
L-glutamine
pH 8.0, 37°C, wild-type enzyme
3.76
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V48A
3.8
L-glutamine
pH 8.0, 50°C
3.8
L-glutamine
pH 8.0, 50°C, basal activity
3.89
L-glutamine
pH 8.0, 60°C
3.89
L-glutamine
pH 8.0, 60°C, basal activity
4.12
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A
4.71
L-glutamine
pH 8.0, 40°C
4.71
L-glutamine
pH 8.0, 40°C, basal activity
4.91
L-glutamine
pH 8.0, 30°C
4.91
L-glutamine
pH 8.0, 30°C, basal activity
2.2
NH4+
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
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
additional information
L-glutamine
pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.045 - 8.7
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.00165 - 9.1
L-glutamine
additional information
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.045
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A
0.126
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R
0.15
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A
0.21
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H
0.24
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A
0.29
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R
0.3
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K
0.31
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R
0.7
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A
0.8
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 25°C, wild-type HisH-HisF complex
0.845
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme
2.2
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
3.9
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
3.9
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H
4.3
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A
5
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R
5.4
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, wild-type enzyme
5.4
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A
6.1
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: NH4+
8.5
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: L-glutamine
8.7
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K
0.00165
L-glutamine
pH 8.0, 37°C, wild-type enzyme
0.00173
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A
0.00311
L-glutamine
pH 8.0, 37°C, mutant enzyme D98A
0.00328
L-glutamine
pH 8.0, 37°C, mutant enzyme V48A
0.00372
L-glutamine
pH 8.0, 30°C
0.00372
L-glutamine
pH 8.0, 30°C, basal activity
0.0054
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A
0.0571
L-glutamine
pH 8.0, 40°C
0.0571
L-glutamine
pH 8.0, 40°C, basal activity
0.139
L-glutamine
pH 8.0, 50°C
0.139
L-glutamine
pH 8.0, 50°C, basal activity
0.18
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme D98A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.204
L-glutamine
pH 8.0, 70°C
0.204
L-glutamine
pH 8.0, 70°C, basal activity
0.212
L-glutamine
pH 8.0, 60°C
0.212
L-glutamine
pH 8.0, 60°C, basal activity
0.24
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V48A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.4
L-glutamine
pH 8.0, 25°C, wild-type HisH-HisF complex
0.57
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.88
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3.62
L-glutamine
pH 8.0, 37°C, wild-type enzyme, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
4.09
L-glutamine
pH 8.0, 30°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
4.37
L-glutamine
pH 8.0, 40°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
4.89
L-glutamine
pH 8.0, 50°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
5.2
L-glutamine
pH 7.0, 30°C
5.5
L-glutamine
pH 8.0, 60°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
5.92
L-glutamine
pH 8.0, 70°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
9.1
L-glutamine
-
pH 8.0, 30°C
0.6
NH4+
pH 7.0, 30°C
2
NH4+
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
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
additional information
L-glutamine
pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.039 - 5667
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.00042 - 4480
L-glutamine
additional information
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.039
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A
0.12
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R
0.46
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A
0.5
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H
1.4
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A
2.8
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A
2.9
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H
3.8
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K
4.3
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R
5.5
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K
11
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A
60
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R
110
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R
130
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A
150
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme
265.2
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: NH4+
600
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.0, 25°C, wild-type HisH-HisF complex
950
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 7.0, 30°C
1200
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
30°C, pH 7.0, cosubstrate: L-glutamine, wild-type enzyme
1300
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
5667
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
-
pH 8.0, 30°C, cosubstrate: L-glutamine
0.00042
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A
0.00046
L-glutamine
pH 8.0, 37°C, wild-type enzyme
0.000758
L-glutamine
pH 8.0, 30°C
0.00087
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V48A
0.00107
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme D98A
0.0018
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A
0.0121
L-glutamine
pH 8.0, 40°C
0.0365
L-glutamine
pH 8.0, 50°C
0.054
L-glutamine
pH 8.0, 60°C
0.0579
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme D98A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.0689
L-glutamine
pH 8.0, 70°C
0.121
L-glutamine
pH 8.0, 40°C, basal activity
0.122
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V48A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.166
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme K19A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.365
L-glutamine
pH 8.0, 50°C, basal activity
0.544
L-glutamine
pH 8.0, 60°C, basal activity
0.688
L-glutamine
pH 8.0, 70°C, basal activity
0.758
L-glutamine
pH 8.0, 30°C, basal activity
1.34
L-glutamine
pH 8.0, 37°C, HisF mutant enzyme V12A, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
1.4
L-glutamine
pH 8.0, 25°C, wild-type enzyme HisHF
2.08
L-glutamine
pH 8.0, 37°C, wild-type enzyme, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3.1
L-glutamine
pH 7.0, 30°C
37.9
L-glutamine
-
pH 8.0, 30°C
2980
L-glutamine
pH 8.0, 50°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3150
L-glutamine
pH 8.0, 30°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
3240
L-glutamine
pH 8.0, 40°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
4040
L-glutamine
pH 8.0, 60°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
4480
L-glutamine
pH 8.0, 70°C, activated by 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
0.024
NH4+
pH 7.0, 30°C
900
NH4+
pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type
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
additional information
L-glutamine
pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K258A
about 2600fold decrease in kcat/Km for glutamine dependent cyclase reaction, basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 1:1
K258R
about 20fold decrease in kcat/Km for glutamine dependent cyclase reaction,basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 3:1
K360R
synthase activity is similar to wild type. The mutant retains both structural and functional integrity of the enzyme in the case of glutaminase functions
R239H
a 1000fold reduction in kcat/Km is observed in the glutamine dependent synthase reaction. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 154:1
R239K
a 1000fold reduction in kcat/Km is observed in the glutamine dependent synthase reaction. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 40:1
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
K258A
-
about 2600fold decrease in kcat/Km for glutamine dependent cyclase reaction, basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 1:1
-
K258R
-
about 20fold decrease in kcat/Km for glutamine dependent cyclase reaction,basal and stimulated glutaminase functions are not altered. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 3:1
-
R239K
-
a 1000fold reduction in kcat/Km is observed in the glutamine dependent synthase reaction. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 40:1
-
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
-
C9A
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_C9A are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue
D130N
mutant of subunit HisF. The catalytic efficiency kcat/Km for 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide is decreased by approximately 5 orders of magnitude
D176N
mutant of subunit HisF. Variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
D183N
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D183N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue. Both kcat and Km are drastically impaired in the mutant enzyme
D51N
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D51N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue
D98A
HisF subunit mutant, mutation reduces glutaminase activity to 3% compared to activity of wild-type enzyme
K19A
HisF subunit mutant, mutation reduces glutaminase activity to 3% compared to activity of wild-type enzyme
K19S
mutant of subunit HisF. The ammonia-dependent reactions of isolated tHisF_K19S are similarly efficient as those of wild-type tHisF. In contrast, the efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired
N103A
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_N103A are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue
T78M
mutant enzyme with reduced catalytic activity
V12A
HisF subunit mutant, mutation reduces glutaminase activity to 70% compared to activity of wild-type enzyme
V48A
HisF subunit mutant, mutation reduces glutaminase activity to 3% compared to activity of wild-type enzyme
D130N
-
mutant of subunit HisF. The catalytic efficiency kcat/Km for 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide is decreased by approximately 5 orders of magnitude
-
D176N
-
mutant of subunit HisF. Variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
-
D183N
-
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D183N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue. Both kcat and Km are drastically impaired in the mutant enzyme
-
D51N
-
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_D51N are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue
-
N103A
-
mutant of subunit HisF. The catalytic efficiencies kcat/Km of both isolated and complexed tHisF_N103A are not significantly different from wild-type tHisF, ruling out any central catalytic role for the replaced residue
-
T78M
-
mutant enzyme with reduced catalytic activity
-
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
K360A
synthase activity is similar to wild type. The stoichiometry of the reaction is 3:1 indicating some degree of uncoupling due to loss of ammonia
R239A
a 1000fold reduction in kcat/Km is observed in the glutamine dependent synthase reaction. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 122:1
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
K360A
-
synthase activity is similar to wild type. The stoichiometry of the reaction is 3:1 indicating some degree of uncoupling due to loss of ammonia
-
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
-
R239A
-
a 1000fold reduction in kcat/Km is observed in the glutamine dependent synthase reaction. The stoichiometry of reaction glutamine: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide turnover is 43:1 compared to wild-type value 122:1
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Banfield, M.J.; Lott, J.S.; Arcus, V.L.; McCarthy, A.A.; Baker, E.N.
Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum
Acta Crystallogr. Sect. D
57
1518-1525
2001
Pyrobaculum aerophilum (Q8ZY16 AND Q8ZY40), Pyrobaculum aerophilum DSM 7523 (Q8ZY16 AND Q8ZY40)
brenda
Klem, T.J.; Davisson, V.J.
Imidazole glycerol phosphate synthase the glutamine amidotransferase in histidine biosynthesis
Biochemistry
32
5177-5186
1993
Escherichia coli, Escherichia coli K12
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), Saccharomyces cerevisiae ATCC 204508 (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 ATCC 204508 (P33734)
brenda
Rivalta, I.; Lisi, G.P.; Snoeberger, N.S.; Manley, G.; Loria, J.P.; Batista, V.S.
Allosteric communication disrupted by a small molecule binding to the imidazole glycerol phosphate synthase protein-protein interface
Biochemistry
55
6484-6494
2016
Thermotoga maritima (Q9X0C8 and Q9X0C6), Thermotoga maritima ATCC 43589 (Q9X0C8 and Q9X0C6)
brenda
Amaro, R.E.; Myers, R.S.; Davisson, V.J.; Luthey-Schulten, Z.A.
Structural elements in IGP synthase exclude water to optimize ammonia transfer
Biophys. J.
89
475-487
2005
Saccharomyces cerevisiae (P33734), Saccharomyces cerevisiae ATCC 204508 (P33734)
brenda
Fujimori, K.; Ohta, D.
An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant
FEBS Lett.
428
229-234
1998
Arabidopsis thaliana (Q9SZ30), Arabidopsis thaliana
brenda
Lisi, G.; Currier, A.; Loria, J.
Glutamine hydrolysis by imidazole glycerol phosphate synthase displays temperature dependent allosteric activation
Front. Mol. Biosci.
5
4
2018
Thermotoga maritima (Q9X0C6 AND Q9X0C8), Thermotoga maritima (Q9X0C8 and Q9X0C6), Thermotoga maritima ATCC 43589 (Q9X0C6 AND Q9X0C8), Thermotoga maritima ATCC 43589 (Q9X0C8 and Q9X0C6)
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 (Q7SIC0 AND Q7SIB9)
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 (Q9X0C6 AND Q9X0C8), Thermotoga maritima ATCC 43589 (Q9X0C6 AND Q9X0C8)
brenda
Lipchock, J.; Loria, J.P.
Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima
J. Biomol. NMR
45
73-84
2009
Thermotoga maritima (Q9X0C6 AND Q9X0C8), Thermotoga maritima ATCC 43589 (Q9X0C6 AND Q9X0C8)
brenda
Lisi, G.P.; East, K.W.; Batista, V.S.; Loria, J.P.
Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity
Proc. Natl. Acad. Sci. USA
114
E3414-E3423
2017
Thermotoga maritima (Q9X0C8 and Q9X0C6)
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 ATCC 204508 (P33734)
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 (Q9X0C6 AND Q9X0C8), Thermotoga maritima ATCC 43589 (Q9X0C6 AND Q9X0C8)
brenda
Holinski, A.; Heyn, K.; Merkl, R.; Sterner, R.
Combining ancestral sequence reconstruction with protein design to identify an interface hotspot in a key metabolic enzyme complex
Proteins
85
312-321
2017
Pyrobaculum arsenaticum (A4WHB6 AND A4WHA5), Zymomonas mobilis (Q5NMD6 AND Q5NMD4), Pyrobaculum arsenaticum DSM 13514 (A4WHB6 AND A4WHA5), Zymomonas mobilis ZM4 (Q5NMD6 AND Q5NMD4)
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 (Q9X0C6 AND Q9X0C8), Thermotoga maritima ATCC 43589 (Q9X0C6 AND Q9X0C8)
brenda