Any feedback?
Information on EC 4.3.1.B2 - imidazole glycerol phosphate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P33734
for references in articles please use BRENDA:EC4.3.1.B2preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.3.1.B2 imidazole glycerol phosphate synthaseSpecify your search results
Word Map
- 4.3.1.B2
- glutaminase
- ammonia
-
amidotransferase
- maritima
-
thermotoga
-
allostery
- cyclase
-
prfar
- ribonucleotide
-
heterodimeric
-
bienzyme
- aicar
-
millisecond
- 5-aminoimidazole-4-carboxamide
-
betaalpha8-barrels
-
v-type
-
half-barrels
-
timescale
- ribotide
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
+
=
+
+
+
=
+
+
Synonyms
imidazole glycerol phosphate synthase, imgp synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-imidazole-glycerol-phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the imidazole glycerol phosphate synthase catalyzes formation of the imidazole ring in histidine biosynthesis
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the enzyme is also a glutamine amidotransferase, which produces ammonia in a glutaminase active site and channels it through a 30 A internal tunnel to a cyclase active site
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
?
additional information
?
-
the enzyme also shows glutaminase activity. The glutaminase activity of the glutaminase domain is tightly regulated by the acceptor substrate domain. In IGP synthase the glutaminase and N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding sites are separated by 30 A. Using kinetic analyses of site-specific mutants and molecular dynamic simulations, it is determined that an interdomain salt bridge in IGP synthase between D359 and K196 (approximately 16 A from the N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate binding site) plays a key role in mediating communication between the two active sites. This interdomain contact modulates the glutaminase loop containing the histidine and glutamic acid of the catalytic triad to control glutamine hydrolysis
-
-
?
additional information
?
-
the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog
-
-
?
additional information
?
-
-
the enzyme shows a low basal level glutaminase activity that can be enhanced 1000fold in the presence of a nucleotide substrate or analog
-
-
?
additional information
?
-
the glutaminase activity of the enzyme is stimulated 4900fold in the presence of the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
-
?
additional information
?
-
-
the glutaminase activity of the enzyme is stimulated 4900fold in the presence of the acceptor substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
-
?
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
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
the imidazole glycerol phosphate synthase catalyzes formation of the imidazole ring in histidine biosynthesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
albizziin
mixed type inhibition versus N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, competitive inhibition versus L-glutamine
N1-[(5'-phosphoarabinitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
competitive versus N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mixed type inhibition versus L-glutamine
N1-[(5'-phosphoribitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
competitive versus N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00027 - 0.139
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
1.3
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
1.8
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
1.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
1.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
1.96
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
2.1
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
6.5
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
6.5
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
0.00027
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
0.0013
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
0.0016
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
0.0018
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
0.002
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
0.0023
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
0.003
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
0.0036
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
0.004
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
0.005
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
0.005
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
0.0055
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
0.008
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
0.0141
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
0.026
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
0.03
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
0.034
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
0.046
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
0.053
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
0.055
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
0.055
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
0.065
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
0.071
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
0.072
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
0.075
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
0.08
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
0.098
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
0.109
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
0.139
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00029 - 8.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
0.025
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
0.16
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
0.49
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
1.13
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
6
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
6.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
6.9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
9
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
0.00029
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
0.007
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
0.01 - 1
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
0.045
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
0.11
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
0.126
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
0.15
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
0.21
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
0.24
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
0.29
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
0.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
0.31
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
0.35
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
0.38
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
0.39
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
0.46
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
0.56
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
0.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
0.74
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
0.845
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
0.845
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
3.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
3.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
4.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
5.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
5.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
5.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
8.7
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016 - 2800
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
0.0011
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239A
0.0028
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239H
0.0036
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258A
0.007
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme R239K
0.084
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K258R
0.247
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360A
0.59
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, mutant enzyme K360R
3.8
L-glutamine
pH 7.0, 30°C, cosubstrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate, wild-type enzyme
0.016
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme Q397A
0.039
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258A
0.12
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K258R
0.46
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258A
0.5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239H
0.51
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A/D359A
0.52
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme D359A
1.2
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme Q397A
1.4
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239A
2.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239A
2.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239H
3.6
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme D359A
3.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme R239K
3.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A/D359A
4.3
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360R
4.9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme N13A
5.5
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme R239K
9
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme N13A
11
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, mutant enzyme K360A
14
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, mutant enzyme K196A
15
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: NH4+, wild-type enzyme
15
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: NH4+, wild-type enzyme
60
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K258R
110
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360R
130
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K360A
950
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C
1200
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 7.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
1200
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, wild-type enzyme
2800
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, cosubstrate: L-glutamine, mutant enzyme K196A
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00067 - 0.003
N1-[(5'-phosphoarabinitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
0.004
N1-[(5'-phosphoribitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
pH 7.0, 30°C, N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
0.6
albizziin
pH 7.0, 30°C, competitive inhibition constant, substrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
1.6
albizziin
pH 7.0, 30°C, uncompetitive inhibition constant, substrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
0.00067
N1-[(5'-phosphoarabinitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
pH 7.0, 30°C, substrate: N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
0.0016
N1-[(5'-phosphoarabinitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
pH 7.0, 30°C, substrate: L-glutamine, uncompetitive inhibition constant
0.003
N1-[(5'-phosphoarabinitolyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
pH 7.0, 30°C, substrate: L-glutamine, competitive inhibition constant
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the production of the soluble HIS7 is highest at 25°C with 1 mM isopropyl beta-D-thiogalactopyranoside and this condition is used for the large-scale protein preparations
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme represents a junction between histidine biosynthesis and de novo purine biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61000
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
61082
1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 61000, SDS-PAGE, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
monomer
1 * 61082, calculated from sequence, the protein is bifunctional, representing a fusion between the N-terminal HisH domain and a C-terminal HisF domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization at 20°C by hanging-drop vapor diffusion from a 1:1 mixture of protein solution and reservoir solution [22%28% polyethylene glycol MME 5000, 0.1 M MES (pH 6.57.0), and 0.2 M (NH4)2SO4]. Crystals grow in 710 days to an average size of 0.12 * 0.12 * 0.08 mM. The 2.1 A crystal structure of imidazole glycerol phosphate synthase reveals extensive interaction of the glutaminase and cyclase catalytic domains. At the domain interface, the glutaminase active site points into the bottomof the (beta/alpha)8 barrel of the cyclase domain. An ammonia tunnel through the (beta/alpha)8 barrel connects the glutaminase docking site at the bottom to the cyclase active site at the top. A conserved gate of four charged residues controls access to the tunnel
structures of a complex of the substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate and imidazole glycerol phosphate synthase covalently modified by the glutamine analogue acvicin at 2.5 A, apoenzyme at 2.4 A, and imidazole glycerol phosphate synthase inactivated by the glutamine analogue 6-diazo-5-oxo-L-norleucine at 2.5 A. Comparison of the free, acivicin-, and 6-diazo-5-oxo-L-norleucine-inactivated forms of the glutaminase active site reveals structural changes relevant to activation. The N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate-bound and -free forms of the enzyme shed light on flexible parts of the molecule with potential roles in crosstalk between active sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 7.5fold decrease in kcat/Km of L-glutamine
K196A
0.43fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 3fold decrease in kcat/Km of L-glutamine
K196A/D359A
2300fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 4fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1fold decrease in kcat/Km of L-glutamine
K258A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 43:1 (wild-type ratio is 1:1), 2600fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 385fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1055fold decrease in kcat/Km of L-glutamine
K258R
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 3:1 (wild-type ratio is 1:1), 20fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 125fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 45fold decrease in kcat/Km of L-glutamine
K360R
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 1:1 (identical to wild-type ratio), 1090fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 3.5fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 6.4fold decrease in kcat/Km of L-glutamine
N13A
130fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 3fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 350fold decrease in kcat/Km of L-glutamine
Q397A
7.5fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: L-glutamine), 1fold decrease in kcat/Km of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 18fold decrease in kcat/Km of L-glutamine
R239A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 122:1 (wild-type ratio is 1:1), 860fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 5.4fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 3450fold decrease in kcat/Km of L-glutamine
R239H
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 154:1 (wild-type ratio is 1:1), 2400fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 5.2fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 1360fold decrease in kcat/Km of L-glutamine
R239K
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 40:1 (wild-type ratio is 1:1), 218fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 3.9fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 540fold decrease in kcat/Km of L-glutamine
R360A
ratio of glutamine turnover to N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate turnover is 3:1 (wild-type ratio is 1:1), 9.2fold decrease in kcat/KM of N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate L-glutamine), 1.4fold decrease in kcat/Km N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate (cosubstrate: NH4+), 15fold decrease in kcat/Km of L-glutamine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a bacterial system 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)
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
Myers, R.S.; Amaro, R.E.; Luthey-Schulten, Z.A.; Davisson, V.J.
Reaction coupling through interdomain contacts in imidazole glycerol phosphate synthase
Biochemistry
44
11974-11985
2005
Saccharomyces cerevisiae (P33734)
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
Chaudhuri, B.N.; Lange, S.C.; Myers, R.S.; Chittur, S.V.; Davisson, V.J.; Smith, J.L.
Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites
Structure
9
987-997
2001
Saccharomyces cerevisiae (P33734), Saccharomyces cerevisiae
EXTERNAL LINKS (specific for EC-Number 4.3.1.B2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
