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Information on EC 4.3.2.10 - imidazole glycerol-phosphate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P33734
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4.3.2.10 imidazole glycerol-phosphate synthaseIUBMB Comments
The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
hishf, hisfh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HIS7
-
-
-
-
hisFH
-
-
-
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IGP synthase
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate-lyase (L-glutamine-hydrolysing; 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide-forming)
The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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 + 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 + 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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
albizziin
mixed-type inhibitor versus 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide, competitive versus glutamine
rPRFAR-1
competitive inhibitor versus 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide inhibitor, mixed-type inhibitor versus glutamine
rPRFAR-2
competitive versus 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016 - 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
0.0016
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
0.0018
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
0.046
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
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045 - 8.7
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
0.045
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
0.845
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
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
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.039 - 1200
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
0.039
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the enzyme catalyzes the formation of the imidazole ring in histidine biosynthesis
metabolism
metabolism
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
metabolism
the enzyme participates in the pathway of histidine biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of a ternary complex of the substrate 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide modified by the glutamine analogue acvicin at 2.5 A. Crystal structure of the free enzyme at 2.4 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
K360A
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
R239A
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytically active yeast HIS7 is expressed in Escherichia coli under the control of T7 polymerase promoter
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
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)
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Release 2023.1 (January 2023)
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