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Information on EC 4.3.1.B2 - imidazole glycerol phosphate synthase and Organism(s) Thermotoga maritima and UniProt Accession Q9X0C8

for references in articles please use BRENDA:EC4.3.1.B2
preliminary BRENDA-supplied EC number
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.B2 imidazole glycerol phosphate synthase
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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X0C8 not found.
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The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
imidazole glycerol phosphate synthase, imgp synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazoleglycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
-
-
?
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
the enzyme constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with N'-((5'-phosphoribulosyl)formimino)-5-aminoimidazole-4-carboxamide-ribonucleotide to yield the products imidazole glycerol phosphate and 5-aminoimidazole-4-carboxamide ribotide. Isolated subunit HisH shows no detectable glutaminase activity but is stimulated by complex formation with subunit HisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound
-
-
?
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
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
L-glutamine
pH 8.5, 25°C
0.0015
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
0.002 - 0.0059
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
L-glutamine
pH 8.5, 25°C
0.8
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
1.1 - 1.2
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
L-glutamine
pH 8.5, 25°C
0.0006
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate
pH 8.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method is used to obtain crystals with a rod-like morphology of a maximum size of about 0.4 x 0.2 x 0.2 mm3. Crystal structure of the heterodimeric bienzyme ImGP synthase comprising the glutaminase subunit HisH and the cyclase subunit HisF, at 2.4 A resolution.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C9A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
D11N
mutation in subunit HisF. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
D130N
the kcat value is reduced by a factor of about 400-500, and the Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is increased almost 20fold. Catalytic efficiency kcat/Km for N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-monophosphate is decreased by approximately 5 orders of magnitude
D176N
mutation in subunit HisF. The variant tHisF_D176N shows a 40-50 fold decrease in kcat, both in isolated form and in complex with tHisH
D183N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
D51N
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
K19S
mutation in subunit HisF. The ammonia-dependent reactions of isolated subunit HisF_K19S is similarly efficient as that of wild-type HisF. The efficiencies of the glutamine-dependent reactions of the tHisHtHisF_K19S complex are significantly impaired
N103A
mutation in subunit HisF. Catalytic efficiencies kcat/Km of both isolated and complexed mutant subunit HisF is not significantly different from wild-type HisF
T78M
-
the mutation does not impair substrate binding to the active site of HisF
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli and purified. Wild-type and active site mutants
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
subunits HisH and HisF from Thermotoga maritima are produced in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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 (Q9X0C8 and Q9X0C6), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X0C8 and Q9X0C6)
Manually annotated by BRENDA team
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 (Q9X0C8 and Q9X0C6), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X0C8 and Q9X0C6)
Manually annotated by BRENDA team