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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
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additional information
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
removal of a non-acidic hydrogen atom in the dehydration reaction
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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additional information
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mechanism shows an enzyme-catalyzed formation of a high-energy imidazolate intermediate. Changes in manganese coordination chemistry dominate all aspects of catalysis. In the first part of the reaction, the enzyme harnesses the substrate binding energy to create a distorted, ligand-depleted metal center, which serves to remove kinetic barriers to the production of the imidazolate intermediate. Subsequently, a second switch in coordination chemistry restores the octahedral coordination of the metal ion, leading to critical torsion angle changes to the substrate that are necessary for concomitant production of the diazafulvene
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additional information
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mechanism shows an enzyme-catalyzed formation of a high-energy imidazolate intermediate. Changes in manganese coordination chemistry dominate all aspects of catalysis. In the first part of the reaction, the enzyme harnesses the substrate binding energy to create a distorted, ligand-depleted metal center, which serves to remove kinetic barriers to the production of the imidazolate intermediate. Subsequently, a second switch in coordination chemistry restores the octahedral coordination of the metal ion, leading to critical torsion angle changes to the substrate that are necessary for concomitant production of the diazafulvene
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additional information
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sixth step in histidine biosynthesis
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Chiariotti, L.; Nappo, A.G.; Carlomagno, M.S.; Bruni, C.B.
Gene strucutre in the histidine operon of Escherichia coli. Identification and nucleotide sequence oh the hisB gene
Mol. Gen. Genet.
202
42-47
1986
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
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Staples, M.A.; Houston, L.L.
Purification of the bifunctional enzyme imidazoleglycerolphosphate dehydratase-histidinol phosphatase of Salmonella typhimurium
Biochim. Biophys. Acta
613
210-219
1980
Salmonella enterica subsp. enterica serovar Typhimurium
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Struhl, K.; Stinchcomb, D.T.; Davis, R.W.
A physiological study of functional expression in Escherichia coli of the cloned yeast imidazoleglycerolphosphate dehydratase gene
J. Mol. Biol.
136
291-307
1980
Saccharomyces cerevisiae
brenda
Struhl, K.; Davis, R.W.
Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazoleglycerolphoshate dehydratase (his3)
Proc. Natl. Acad. Sci. USA
74
5255-5259
1977
Saccharomyces cerevisiae
brenda
Glaser, R.D.; Houston, L.L.
Subunit structure and photooxidation of yeast imidazoleglycerolphosphate dehydratase
Biochemistry
13
5145-5152
1974
Saccharomyces cerevisiae
brenda
Brady, D.R.; Houston, L.L.
Some properties of the catalytic sites of imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase, a bifunctional enzyme from Salmonella typhimurium
J. Biol. Chem.
248
2588-2592
1973
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Burke, M.E.; Pattee, P.A.
Histidine biosynthetic pathway in Staphylococcus aureus
Can. J. Microbiol.
18
569-576
1972
Staphylococcus aureus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Staples, M.A.; Houston, L.L.
Proteolytic degradation of imidazoleglycerolphosphate dehydratase-histidinol phosphatase from Salmonella typhimurium and the isolation of a resistant bifunctional core enzyme
J. Biol. Chem.
254
1395-1401
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ames, B.N.
The biosynthesis of histidine: D-erythro-imidazole-glycerol phosphate dehydrase
J. Biol. Chem.
228
131-143
1957
Neurospora crassa
brenda
Goldman, G.H.; Demolder, J.; Dewaele, S.; Herrera-Estrella, A.; Geremia, R.A.; van Montagu, M.; Contreras, R.
Molecular cloning of the imidazoleglycerolphosphate dehydratase gene of Trichoderma harzianum by genetic complementation in Saccharomyces cerevisiae using a direct expression vector
Mol. Gen. Genet.
234
481-488
1992
Trichoderma harzianum
brenda
Mano, J.; Hatano, M.; Koizumi, S.; Tada, S.; Hashimoto, M.; Scheidegger, A.
Purification and properties of a monofunctional imidazoleglycerol-phosphate dehydratase from wheat
Plant Physiol.
103
733-739
1993
Brassica oleracea, Hordeum vulgare, Oryza sativa, Rosa sp., Triticum aestivum, Zea mays
brenda
Parker, A.R.; Moore, T.D.E.; Edman, J.C.; Schwab, J.M.; Davisson, V.J.
Cloning, sequencing and expression of the gene encoding imidazole glycerol phosphate dehydratase in Cryptococcus neoformans
Gene
145
135-138
1994
Cryptococcus neoformans
brenda
Tada, S.; Volrath, S.; Guyer, D.; Scheidegger, A.; Ryals, J.; Ohta, D.; Ward, E.
Isolation and characterization of cDNAs encoding imidazoleglycerolphosphate dehydratase from Arabidopsis thaliana
Plant Physiol.
105
579-583
1994
Arabidopsis thaliana
brenda
Wilkinson, K.W.; Baker, P.J.; Rice, D.W.; Rodgers, F.; Stillman, T.J.
Crystallization and analysis of subunits assembly and quarternary structure of imidazoleglycerol phosphate dehydratase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
51
845-847
1995
Saccharomyces cerevisiae
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Parker, A.R.; Moore, J.A.; Schwab, J.M.; Davisson, V.J.
Escherichia coli imidazoleglycerol phosphate dehydratase: spectroscopic characterization of the enzymic product and the steric course of the reaction
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117
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1995
Escherichia coli
-
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Tada, S.; Hatano, M.; Nakayama, Y.; Volrath, S.; Guyer, D.; Ward, E.; Ohta, D.
Insect cell expression of recombinant imidazoleglycerolphosphate dehydratase of Arabidopsis and wheat and inhibition by triazole herbicides
Plant Physiol.
109
153-159
1995
Arabidopsis thaliana, Triticum aestivum
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Hawkes, T.R.; Thomas, P.G.; Edwards, L.S.; Rayner, S.J.; Wilkinson, K.W.
Purification and characterization of the imidazoleglycerol-phosphate dehydratase of Saccharomyces cerevisiae from recombinant Escherichia coli
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306
385-397
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Saccharomyces cerevisiae
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Mori, I.; Fonne-Pfister Matsunaga, S.i.; Tada, S.; Kimura, Y.; Iwasaki, G.; Mano, J.i.; Hatano, M.; Nakano, T.; Koizumi, S.i.; Scheidegger, A.; Hayakawa, K.; Ohta, D.
A novel class of herbicides. Specific inhibitors of imidazoleglycerol phosphate dehydratase
Plant Physiol.
107
719-723
1995
Triticum aestivum
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Sinha, S.C.; Chaudhuri, B.N.; Burgner, J.W.; Yakovleva, G.; Davisson, V.J.; Smith, J.L.
Crystal structure of imidazole glycerol-phosphate dehydratase: Duplication of an unusual fold
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279
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2004
Cryptococcus neoformans (P0CO22)
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Glynn, S.E.; Baker, P.J.; Sedelnikova, S.E.; Levy, C.W.; Rodgers, H.F.; Blank, J.; Hawkes, T.R.; Rice, D.W.
Purification, crystallization and preliminary crystallographic analysis of Arabidopsis thaliana imidazoleglycerol-phosphate dehydratase
Acta Crystallogr. Sect. F
F61
776-778
2005
Arabidopsis thaliana
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Glynn, S.E.; Baker, P.J.; Sedelnikova, S.E.; Davies, C.L.; Eadsforth, T.C.; Levy, C.W.; Rodgers, H.F.; Blackburn, G.M.; Hawkes, T.R.; Viner, R.; Rice, D.W.
Structure and mechanism of imidazoleglycerol-phosphate dehydratase
Structure
13
1809-1817
2005
Arabidopsis thaliana
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Structures of native, substrate-bound and inhibited forms of Mycobacterium tuberculosis imidazoleglycerol-phosphate dehydratase
Acta Crystallogr. Sect. D
69
2461-2467
2013
Mycobacterium tuberculosis
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Park, E.H.; Kwun, S.Y.; Han, S.A.; Lee, J.S.; Kim, M.D.
Cloning and functional verification of the Candida milleri HIS3 gene encoding imidazoleglycerol phosphate dehydratase
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22
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Kazachstania humilis (H9C4A4), Kazachstania humilis, Kazachstania humilis CBS 8195 (H9C4A4)
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Crystal structures reveal that the reaction mechanism of imidazoleglycerol-phosphate dehydratase is controlled by switching Mn(II) coordination
Structure
23
1236-1245
2015
Arabidopsis thaliana (O23346), Arabidopsis thaliana
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