4.2.1.19: imidazoleglycerol-phosphate dehydratase
This is an abbreviated version!
For detailed information about imidazoleglycerol-phosphate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.19
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4.2.1.19
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herbicide
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auxotrophs
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3-amino-1,2,4-triazole
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phosphonate
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histidinol
- 4.2.1.19
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herbicide
-
auxotrophs
- 3-amino-1,2,4-triazole
- phosphonate
- histidinol
Reaction
Synonyms
dehydratase, imidazoleglycerol phosphate, His3, HisB, HisN5B, IGP dehydratase, IGPD, imidazoleglycerol phosphate dehydratase, imidazoleglycerolphoshate dehydratase
ECTree
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Substrates Products
Substrates Products on EC 4.2.1.19 - imidazoleglycerol-phosphate dehydratase
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REACTION DIAGRAM
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
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
-
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
?
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
3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
-
-
-
-
?
?
-
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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?