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phosphoenol-3-fluoropyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
enzyme does not discriminate between (E) and (Z)-form of phosphoenol-3-fluoropyruvate
-
-
?
phosphoenolpyruvate + (3S)-2-deoxyerythrose 4-phosphate + H2O
(5S)-[5H]-3,5-dideoxy-D-arabinoheptulosonate 7-phosphate + phosphate
-
-
-
-
ir
phosphoenolpyruvate + 2-deoxy-D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D,L-lyxose
2-dehydro-3-deoxy-D,L-galacto-octonate + phosphate
-
D-lyxose or L-lyxose, at 1.8% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-arabinose
2-dehydro-3-deoxy-D-gluco-octonate + phosphate
-
at 0.7% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-erythrose
2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
-
at 93% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + D-fructose 1,6-diphosphate
?
-
same activity as with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-fructose 6-phosphate
?
-
same activity as with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
phosphoenolpyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-threo-hexonate + phosphate
-
at 176% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-ribulose 5-phosphate
?
-
at 12% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-threose
2-dehydro-3-deoxy-D-xylo-heptonate + phosphate
-
at 92% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylose
2-dehydro-3-deoxy-D-ido-octonate + phosphate
-
at 1% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + glycolaldehyde
(S)-2-oxo-4,5-dihydroxypentanoate + phosphate
-
at 245% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + glyoxylate
S-4-hydroxy-2-oxo-1,5-pentanedioate + R-4-hydroxy-2-oxo-1,5-pentanedioate + phosphate
-
at 205% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-erythrose
2-dehydro-3-deoxy-L-arabino-heptonate + phosphate
-
at 70% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-threo-hexonate + phosphate
-
at 212% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-threose
2-dehydro-3-deoxy-L-xylo-heptonate + phosphate
-
at 52% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + L-xylose
2-dehydro-3-deoxy-L-ido-octonate + phosphate
-
at 1% of the activity with D-erythrose 4-phosphate
-
-
?
additional information
?
-
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate + H2O
3,5-dideoxy-D-gluco-octulosonate 8-phosphate + 3,5-dideoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
at 8% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
key regulatory enzyme in L-Phe and L-Tyr biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
effect of external factors on regulation
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
one of the key regulator enzymes of the shikimic acid pathway
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
binds 1 molecule D-erythrose 4-phosphate per subunit
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
in solution D-erythrose 4-phosphate forms dimers that are in slow equilibrium with monomers
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
r
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate binding structure analysis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate interacts with conserved residues Arg167, Arg236, Lys188, Arg94, and Lys99, condensation reaction
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-glucose 6-phosphate
?
-
at 0.5% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
as effective as D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-ribose 5-phosphate + H2O
3-deoxy-D-altro-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
at 67% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + D-xylulose 5-phosphate
?
-
at 67% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde 3-phosphate
pyruvate + phosphate
-
at 142% of the activity with D-erythrose 4-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
additional information
?
-
-
no activity with D-erythrose, D-glyceraldehyde 3-phosphate, ribose 5-phosphate, glucose 6-phosphate, glucosamine 6-phosphate, N-acetylglucosamine 6-phosphate, and pyruvate
-
-
?
additional information
?
-
-
no substrates are: D-glucose 6-phosphate, D-arabinose, DL-glyceraldehyde, D-erythrose, glycoaldehyde, DL-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
?
additional information
?
-
kinetic mechanism is rapid equilibrium sequential ordered ter ter, with the essential divalent metal ion, Mn2+, binding first, followed by phosphoenolpyruvate and D-erythrose 4-phosphate
-
-
-
additional information
?
-
-
reaction involves interaction of si face of phosphoenolpyruvate with re face of eryxthrose 4-phosphate
-
-
?
additional information
?
-
no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
-
-
?
additional information
?
-
-
no substrate: D-glyceraldehyde 3-phosphate, D-glucose 6-phosphate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
additional information
?
-
-
structure comparison between 3-deoxy-7-phosphoheptulonate synthase and 3-deoxy-D-manno-octulosonate 8-phosphate synthase, EC 4.1.2.16, reveal that they share a common ancestor and adopt the same catalytic strategy
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
key regulatory enzyme in L-Phe and L-Tyr biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
regulatory role of thioredoxin of photosystem I on the chloroplastic enzyme
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
DSH1 RNA levels increase in Arabidopsis leaves subjected either to physical wounding or to infiltration with pathogenic Pseudomonas syringae strains, DSH2 RNA levels are not increased by these treatments
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of aromatic amino acids, folic acid and phenazine 1-carboxylic acid biosynthesis pathways
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
effect of external factors on regulation
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
one of the key regulator enzymes of the shikimic acid pathway
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
no repression by the aromatic amino acids
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
first enzyme in the shikimic pathway leading to biosynthesis of aromatic amino acids
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
the plastidic enzyme form is induced by fungal elicitor of Phytophthora megasperma, the cytosolic enzyme form is not induced
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
enzyme is induced by N-[phosphomonomethyl]glycine
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
first enzyme of the aromatic amino acid biosynthesis
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate + H2O
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,2S)-1,2-epoxypropylphosphonic acid
-
-
(2R)-2-(phosphonooxy)propanoic acid
-
mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate
(2S)-2,7-bis(phosphonooxy)heptanoic acid
-
(2S)-2-(phosphonooxy)propanoic acid
-
mimicking phosphohemiketal 2 (instable), competitive to substrate phosphoenolpyruvate
(2Z)-3-phosphono-2-(trifluoromethyl)prop-2-enoic acid
-
trifluorinated phosphonate
(E)-2-methyl-3-phosphonoacrylic acid
-
most potent of the tested inhibitors mimicking intermediates in the reaction, vinyl phosphonate 4
(Z)-Phosphoenol 3-fluoropyruvate
-
-
1,10-phenanthroline
-
activity is restored by Fe2+ or Zn2+
2,3-bisphosphoglycerate
-
-
2-(phosphonomethyl)prop-2-enoic acid
-
mimics substrate phosphoenolpyruvate, and should be inert due to alkene structure but lacking an electron-donor, acts as competitive inhibitor
2-Methyl-DL-Trp
-
0.02 mM, 30% inhibition
2-phosphoglycerate
-
competitive with respect to phosphoenolpyruvate
3,4-dihydroxycinnamate
-
isoenzyme DS-Co
3-deoxy-D-arabino-heptonic acid 7-phosphate
-
-
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate
-
-
3-Methylphosphoenolpyruvate
-
-
3-Propylphosphoenolpyruvate
-
-
3-pyridine carboxyaldehyde
-
4-Methyl-DL-Trp
-
0.02 mM, 30% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-Fluoro-DL-Trp
-
0.02 mM, 56% inhibition
5-hydroxy-DL-Trp
-
0.02 mM, 10% inhibition
6-Methyl-DL-Trp
-
0.02 mM, 6% inhibition
7-Aza-DL-Trp
-
0.02 mM, 9% inhibition
7-Methyl-DL-Trp
-
0.02 mM, 14% inhibition
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
allylpyrocatechol-3,4-diacetate
-
alpha-Methylphenylalanine
-
-
beta-2-Thienyl-D,L-Ala
-
-
CN-
-
Tyr-sensitive isozyme, strong inhibition, reactivation by divalent cations only to a small extent
D-fructose 1,6-diphosphate
-
-
D-sedoheptulose 1,7-diphosphate
-
-
D-sedoheptulose 7-phosphate
-
-
diethyl dicarbonate
-
Phe-sensitive isozyme, pH-dependent, phosphoenolpyruvate protects wild-type and mutants H64G, H207G, H304G
dihydroxyphenylalanine
-
-
DL-Dibromotryptophan
-
0.02 mM, 52% inhibition
DL-erythro-beta-Methyltryptophan
-
0.02 mM, 40% inhibition
DL-Homotryptophan
-
0.02 mM, 46% inhibition
eupalitin-3-O-galactoside
-
fosmidomycin
-
uncompetitive inhibitor, maximum level of inhibition after 10 min incubation, extent of inhibition dependent on the type of the metal cofactor, competitive inhibitor with respect to phosphoenolpyruvate
H2O2
DAHP synthase enzymes are inactivated by H2O2 in vitro and in vivo, H2O2 displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide
Hg2+
-
complete inhibition at 1 mM
iodoacetamide
-
alkylation, abolishes the dependence on reducing agents
L-arogenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
m-Chlorophenylalanine
-
-
m-Fluorophenylalanine
-
-
m-hydroxyphenylalanine
-
-
Mg2+
-
no inhibition of mutant C67L; wild-type and mutants
N-alpha-methyl-DL-Trp
-
0.02 mM, 60% inhibition
N-[Phosphomonomethyl]glycine
o-chlorophenylalanine
-
-
o-Fluorophenylalanine
-
-
o-hydroxyphenylalanine
-
-
p-chloromercuribenzoate
-
complete inhibition at 0.02 mM, reversible by cysteine
p-Fluorophenylalanine
-
-
p-hydroxymercuribenzoate
-
-
phenylpyruvate
-
DAHP synthase-tyr
Phosphoenol 2-oxobutanoate
-
-
phosphoenolpyruvate
pronounced substrate inhibition above 1 mM
shikimate
-
1 mM, 3% residual activity
superoxide
displaces the iron atom from the enzyme, only the Fe2+-metalloform of the enzyme can be inactivated by hydrogen peroxide or superoxide. Superoxide stress promotes the mismetallation of DAHP synthase
tetraammonium (((carboxymethyl)[(2S,3R,4S)-2,3,4-trihydroxy-5-(phosphonatooxy)pentyl]amino)methyl)phosphonate
-
IC50: 0.0066 mM
Trinitrobenzene sulfonate
-
-
[(1E)-7-bromo-2-carboxyhept-1-en-1-yl]phosphonate
-
inhibitor based on vinyl phosphonate, designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
[2-carboxy-7-(phosphonatooxy)hept-1-en-1-yl]phosphonate
-
inhibitor based on vinyl phosphonate ratio Z:E enantiomer 1:1. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
[2-carboxy-7-(phosphonatooxy)hept-2-en-1-yl]phosphonate
-
inhibitor based on allyl phosphonate, ratio Z:E enantiomer 7:3. Inhibitor is designed to fit into the binding sites of both phosphoenolpyruvate and D-erythrose 4-phosphate substrates simultaneously. Competitive with respect to phosphoenolpyruvate
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
binding is competitive with respect to all three substrates.The oxime functional group, combined with two crystallographic waters, binds at the same location in the catalytic center as the phosphate group of the tetrahedral intermediate. DAHP oxime binds to only one subunit of each tight dimer
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
inhibitor shows a good correlation between transition state stabilization and inhibition. DAHP oxime is mimicking the first irreversible transition state of the DAHP synthase reaction, presumably phosphate departure from the tetrahedral intermediate
3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
inhibition is competitive with respect to the essential metal ion, Mn2+. Inhibition shifts from metal-competitive at physiological pH to metal-noncompetitive at pH above 8.7 in response to deprotonation of the Cys61 side chain. Metal-competitive inhibition arises from interactions between Mn2+, DAHP oxime's O4 hydroxyl group, and the Cys61 and Asp326 side chains
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
-
product inhibition
7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate
-
competitive against D-erythrose 4-phosphate and phosphoenolpyruvate
chorismate
-
50% at 0.12 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
chorismate
-
1 mM, 3% residual activity
chorismate
-
competitive against phosphoenolpyruvate, noncompetitive against D-erythrose 4-phosphate; DAHP synthase-trp
chorismate
-
main allosteric feedback inhibitor and regulator for enzyme of class AroAII
Co2+
-
weak
Co2+
-
concentrations above 0.1 mM
Cu2+
-
weak
Cu2+
-
0.02 mM, complete inactivation; Phe-sensitive isozyme, complete inactivation at 0.02 mM, destabilization of the enzymes quarternary structure; phosphoenolpyruvate protects
D-erythrose 4-phosphate
-
-
D-erythrose 4-phosphate
Phe-sensitive isozyme: in absence of phosphoenolpyruvate the enzyme is inhibited via formation of a covalent binding to Lys186 via a slow Schiff base reaction, mechanism
D-erythrose 4-phosphate
-
substrate-inhibition
D-erythrose 4-phosphate
-
isoenzyme DS-Mn: substrate inhibition above 0.5 mM
dipicolinic acid
1 mM, 1 h, 21% residual activity
dipicolinic acid
-
inactivation, reactivation by divalent cations
EDTA
2 mM, complete inactivation within 10 min
EDTA
10 mM, 1 h, 21% residual activity
EDTA
-
22.7% residual activity at 2 mM EDTA for isozyme NCgl0950 DAHP synthase, 49.1% residual activity at 2 mM EDTA for isozyme NCgl2098 DAHP synthase
EDTA
-
reversible by Co2+
EDTA
-
activity is restored by Fe2+ or Zn2+
EDTA
-
reversible by diverse divalent metal ions with varying efficiency
EDTA
-
Mn2+, Cd2+, Co2+, Fe2+, Cu2+, Mg2+ or Zn2+ reactivate, Fe2+ and Cu2+ only partially reactivate
EDTA
-
inactivation, reactivation by divalent metyl ions, in decreasing order: Co2+, Mn2+, Ca2+, Mg2+, Cu2+, Zn2+
EDTA
-
reversible by Co2+
EDTA
-
phosphoenolpyruvate or 3-deoxy-D-arabino-heptulosonate 7-phosphate and Mn2+, Co2+, Ca2+ and Mg2+ protect
EDTA
-
inactivation, restoration in decreasing order of effectiveness by Zn2+, Cd2+, Mn2+, Co2+, Ni2+, Ca2+, Hg2+, Cu2+
EDTA
-
Co2+, Zn2+, Cu2+, and Fe3+ restore activity
EDTA
-
Co2+, Mn2+, Zn2+ and Fe2+ restore activity; phosphoenolpyruvate, 2 mM, partially protects from inactivation, does not restore activity
EDTA
-
inactivation, reactivation in decreasing order by Zn2+, Cd2+, Mn2+, Cu2+, Co2+, Ni2+
EDTA
-
strong, reversible by dialysis
Fe2+
-
0.02 mM: 60% inactivation. 0.2 mM: 90% inactivation; Phe-sensitive isozyme, 60% inactivation at 0.02 mM, 90% inactivation at 0.2 mM; phosphoenolpyruvate protects
L-Phe
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition with 29.1 to 38.8% inhibition at 2 mM, NCgl2098 DAHP synthase is insensitive
L-Phe
strong feedback inhibition
L-phenylalanine
-
1 mM, 3% residual activity
L-phenylalanine
allosteric feedback inhibition
L-phenylalanine
allosteric feedback inhibition
L-phenylalanine
-
1 mM, 32% residual activity
L-phenylalanine
involved in allosteric regulation of the enzyme, inhibits the wild-type enzyme, and enzyme mutants H29A and H29S/S31H
L-Trp
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition, NCgl2098 DAHP synthase is slightly sensitive to feedback inhibition with 10-15% decrease of activity at 5 mM L-Trp
L-Trp
feedback inhibition
L-tryptophan
-
1 mM, 3% residual activity
L-tryptophan
allosteric feedback inhibition
L-tryptophan
allosteric feedback inhibition
L-Tyr
-
NCgl0950 DAHP synthase is sensitive to feedback inhibition with 80% loss of activity at 0.03 mM, NCgl2098 DAHP synthase is insensitive, Tyr-linked inhibition is competitive to phophoenolpyruvate
L-Tyr
feedback inhibition
L-tyrosine
-
1 mM, 3% residual activity
L-tyrosine
feedback inhibition of isozyme AroF
L-tyrosine
feedback inhibition
L-tyrosine
allosteric feedback inhibition
L-tyrosine
allosteric feedback inhibition
L-tyrosine
-
almost complete inhibition at 0.5 mM
L-tyrosine
-
1 mM, 23% residual activity
L-tyrosine
allosteric regulation of the enzyme is mediated by L-Tyr binding to a discrete ACT regulatory domain appended to a core catalytic (beta/alpha)8 barrel, highly reduced inhibition of enzyme mutant S31G. Comparison of the position of the regulatory ACT domain of TmaDAH7PS in the unbound and L-Tyr-bound conformations, overview
N-[Phosphomonomethyl]glycine
-
i.e. glyphosate; inhibition of isozyme DS-Co in vitro and in vivo, isozyme DS-Mn is only slightly inhibited in vitro
N-[Phosphomonomethyl]glycine
-
concentration of Co2+ markedly increases the concentration of N-[phosphomonomethyl]glycine required for inhibition; cytosolic isozyme; i.e. glyphosate
Phe
-
DSI; Phe-sensitive isozyme
Phe
-
slight inhibition of the wild-type, activation of mutants
Phe
-
0.5 mM, 60% inhibition; Phe-sensitive isozyme
Phe
-
0.04 mM, 50% inhibition of DAHP synthase-phe; L-Phe; Phe-sensitive isozyme
Phe
-
L-Phe; Phe-sensitive isozyme
Phe
-
L-Phe; Phe-sensitive isozyme; strong
Phe
-
Phe-sensitive isozyme
Phe
-
feed-back inhibition, Phe-sensitive isozyme; Phe-sensitive isozyme
Phe
-
Phe-sensitive isozyme
Phe
Phe-sensitive isozyme
Phe
-
Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Tyr-sensitive isozyme is less inhibited than the Phe-sensitive isozyme
Phe
-
competitive with respect to D-erythrose 4-phosphate and non-competitive to phosphoenolpyruvate; Phe-sensitive isozyme
Phe
-
no inhibition; Phe-sensitive isozyme; strain 12/60/X, no inhibition; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe
phenylalanine
-
1 Mn, wild-type 8.2% residual activity
phenylalanine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
non-competitive with respect to both phosphoenolpyruvate and D-erythrose 4-phosphate
phosphate
-
competitive to D-erythrose 4-phosphate, noncompetitive to phosphoenolpyruvate
phosphate
-
phosphate buffer destabilizes
prephenate
-
50% at 0.02 mM; feedback inhibition, noncompetitive against D-erythrose 4-phosphate and phosphoenolpyruvate
prephenate
-
1 mM, 3% residual activity
prephenate
-
IC50: 0.1 mM
prephenate
-
isozyme DS-Mn, competitive against D-erythrose 4-phosphate, non-competitive against phosphoenolpyruvate
Trp
-
noncompetitive to both substrates; Trp-sensitive isozyme
Trp
-
DSI; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
0.02 mM, 65% inhibition; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; strongly dependent on pH; Trp-sensitive isozyme
Trp
-
non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
allosteric, best at pH 6.0, no inhibition at pH 7.3; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
DAHP synthase-trp; non-competitive against phosphoenolpyruvate and competitive for D-erythrose 4-phosphate; Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
Trp-sensitive isozyme
Trp
-
minor feedback inhibitor
Tyr
-
DSI and DSII; Tyr-sensitive isozyme
Tyr
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme; wild-type and mutant S187A
Tyr
-
0.5 mM, 20% inhibition; Tyr-sensitive isozyme
Tyr
-
0.04 mM, 50% inhibition of DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
0.02 mM, 50% inhibition; Tyr-sensitive isozyme
Tyr
-
feedback inhibition; noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
L-Tyr; Tyr-sensitive isozyme
Tyr
-
Tyr-sensitive isozyme
Tyr
-
wild-type isozyme, mutant N8K and N-terminal deletion mutant are not inhibited, N-terminus is structurally involved in the sensitivity for feedback inhibition
Tyr
-
Tyr-sensitive isozyme
Tyr
-
L-Tyr; Tyr-sensitive isozyme
Tyr
-
DAHP synthase-tyr; L-Tyr; Tyr-sensitive isozyme
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
noncompetitive with respect to D-erythrose 4-phosphate, competitive with respect to phosphoenolpyruvate; Tyr-sensitive isozyme
Tyr
-
at pH 6.2-7.8; Tyr-sensitive isozyme
Tyr
-
strain 33/X strongly but not totally inhibited; strain H1, strain H20 and strain 3/2: cumulative inhibition of Tyr and Phe; Tyr-sensitive isozyme
tyrosine
inhibition of the synthase-chorismate mutase complex, based on mutase activity measurements at 30°C, 50 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, and 0.1 mM MnCl2
Zn2+
-
no inhibition of mutant C67L; wild-type and mutants
additional information
substrate D-erythrose 4-phosphate is not inhibitory
-
additional information
none of the downstream products of the shikimate biosynthetic pathway tested inhibits the activity of the enzyme
-
additional information
-
none of the downstream products of the shikimate biosynthetic pathway tested inhibits the activity of the enzyme
-
additional information
-
no inhibition by aromatic amino acids, folic acid, phenazine 1-carboxylic acid, anthranilic acid, shikimic acid, p-aminobenzoic acid and 3-hydroxyanthranilic acid
-
additional information
-
no inhibitory: EDTA
-
additional information
-
inhibition mechanism
-
additional information
-
structure and reaction intermediate mimic inhibitors; sulfoenolpyruvate 7 mimics substrate phosphoenolpyruvate, sulfate exchanges phosphate ester, no inhibition up to a concentration of 10 mM
-
additional information
isozyme AroG is not inhibited by L-Phe. In peroxide-stressed cells, the enzyme accumulates as an apoprotein, potentially with an oxidized cysteine residue. In superoxide-stressed cells, the enzyme acquires a nonactivating zinc ion in its active site, an apparent consequence of the repeated ejection of iron. Manganese supplementation protects the activity in both cases, which matches the ability of manganese to metallate the enzyme and to provide substantial oxidant-resistant activity. The damage to DAHP synthase can be completely restored in vivo, while in vitro, restoration is only partly, overview. Escherichia coli attempts to compensate for diminished DAHP synthase activity by increasing expression
-
additional information
-
isozyme AroG is not inhibited by L-Phe. In peroxide-stressed cells, the enzyme accumulates as an apoprotein, potentially with an oxidized cysteine residue. In superoxide-stressed cells, the enzyme acquires a nonactivating zinc ion in its active site, an apparent consequence of the repeated ejection of iron. Manganese supplementation protects the activity in both cases, which matches the ability of manganese to metallate the enzyme and to provide substantial oxidant-resistant activity. The damage to DAHP synthase can be completely restored in vivo, while in vitro, restoration is only partly, overview. Escherichia coli attempts to compensate for diminished DAHP synthase activity by increasing expression
-
additional information
no feedback inhibition by L-phenylalanine
-
additional information
-
not inhibitory: phenylalanine, tyrosine, tryptophan, chorismate
-
additional information
inhibitor screening, docking study, molecular dynamics and molecular modelling, induced fit docking scores, overview. alpha-Tocopherol, 3-pyridine carboxyaldehyde, and rutin can be drug leads to inhibit mtDAH7Ps in Mycobacterium tuberculosis
-
additional information
-
inhibitor screening, docking study, molecular dynamics and molecular modelling, induced fit docking scores, overview. alpha-Tocopherol, 3-pyridine carboxyaldehyde, and rutin can be drug leads to inhibit mtDAH7Ps in Mycobacterium tuberculosis
-
additional information
binding structure determination and analysis, overview. The side chains of enzyme residues Lys188, Arg167 and Arg236 and the main chain peptide N of Ala166 that interact with the phosphate moiety of phosphoenolpyruvate form similar interactions with the phosphate or phosphonate functionalities of the three ligands, consistent with this portion of each inhibitor being able to mimic the phosphoenolpyruvate binding characteristics well. The tetrameric quaternary structures of enzyme NmeDAH7PS bound with (S)-phospholactate and vinyl phosphonate are identical to that of the isomorphous phosphoenolpyruvate-bound parent structure, PDB ID 4HSN. The increased inhibitor potency observed for the vinyl phosphonate over the (R)-phospholactate suggests that the active site is better prepared to accommodate a planar rather than tetrahedral intermediate
-
additional information
-
binding structure determination and analysis, overview. The side chains of enzyme residues Lys188, Arg167 and Arg236 and the main chain peptide N of Ala166 that interact with the phosphate moiety of phosphoenolpyruvate form similar interactions with the phosphate or phosphonate functionalities of the three ligands, consistent with this portion of each inhibitor being able to mimic the phosphoenolpyruvate binding characteristics well. The tetrameric quaternary structures of enzyme NmeDAH7PS bound with (S)-phospholactate and vinyl phosphonate are identical to that of the isomorphous phosphoenolpyruvate-bound parent structure, PDB ID 4HSN. The increased inhibitor potency observed for the vinyl phosphonate over the (R)-phospholactate suggests that the active site is better prepared to accommodate a planar rather than tetrahedral intermediate
-
additional information
undergoes no significant conformational change on inhibitor binding, crystal structure analysis, overview. Allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme
-
additional information
-
undergoes no significant conformational change on inhibitor binding, crystal structure analysis, overview. Allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme
-
additional information
not inhibitory: phenylalanine, tyrosine, tryptophane
-
additional information
-
not inhibitory: phenylalanine, tyrosine, tryptophane
-
additional information
-
resistant to denaturation by sodium dodecyl sulfate, not inhibitory: phenylalanine, tyrosine, tryptophan
-
additional information
-
not inhibited by tryptophan
-
additional information
-
not inhibitory: L-tryptophan, chorismate, shikimate, D-phenylalanine, L-histidine
-
additional information
small angle X-ray (SAXS) scattering analysis
-
additional information
-
small angle X-ray (SAXS) scattering analysis
-
additional information
-
no inhibition by Tyr and Phe
-
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0.65
(3S)-2-deoxyerythrose 4-phosphate
-
pH 6.8
0.006
2-deoxy-D-erythrose 4-phosphate
pH 6.8, 60°C
2.5
2-deoxy-D-ribose 5-phosphate
pH 6.8, 60°C
6.8
2-deoxyribose 5-phosphate
-
recombinant enzyme, pH 7.5, 25°C
0.03 - 2.7
D-arabinose 5-phosphate
2.5
D-erythrose
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
0.0026 - 52.36
D-erythrose 4-phosphate
3.5
D-glyceraldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
1.58
D-ribose 5-phosphate
pH 6.8, 60°C
8.4
D-threose
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
3
DL-glyceraldehyde 3-phosphate
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
8.6
glycolaldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
3.6
glyoxylate
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
5.1
L-erythrose
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
3.3
L-glyceraldehyde
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
13.9
L-threose
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
0.003 - 21
phosphoenolpyruvate
6
ribose 5-phosphate
-
recombinant enzyme, pH 7.5, 25°C
additional information
additional information
-
0.03
D-arabinose 5-phosphate
-
recombinant enzyme, pH 7.5, 25°C
2.7
D-arabinose 5-phosphate
pH 6.8, 60°C
0.0026
D-erythrose 4-phosphate
-
pH 7.0, 37°C
0.006
D-erythrose 4-phosphate
-
pH 7.5, 30°C
0.009
D-erythrose 4-phosphate
pH 6.8, 60°C
0.013
D-erythrose 4-phosphate
-
pH 7.4, 37°C
0.013
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, wild-type enzyme
0.0134
D-erythrose 4-phosphate
pH 6.8, 25°C, mutant R126S
0.015
D-erythrose 4-phosphate
pH 7.5, 25°C
0.016
D-erythrose 4-phosphate
pH 7.5, 37°C, presence of Co2+
0.018
D-erythrose 4-phosphate
-
wild-type, pH 7.9, 30°C
0.021
D-erythrose 4-phosphate
-
pH 6.8
0.028
D-erythrose 4-phosphate
-
60°C, pH 6.8
0.028
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
0.03
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant H29A
0.033
D-erythrose 4-phosphate
pH 7.3, temperature not specified in the publication, mutant S31G
0.037
D-erythrose 4-phosphate
pH 6.8, 25°C, wild-type enzyme
0.04
D-erythrose 4-phosphate
pH 6.8, 30°C, mutant R126S
0.043
D-erythrose 4-phosphate
pH 6.8, 30°C, wild-type enzyme
0.055
D-erythrose 4-phosphate
-
pH 7.8, 25°C
0.0573
D-erythrose 4-phosphate
-
pH 7.5, 50°C
0.07
D-erythrose 4-phosphate
-
pH 7.0, 25°C
0.071
D-erythrose 4-phosphate
pH 7.5, 60°C, mutant enzyme I181D
0.0814
D-erythrose 4-phosphate
-
Tyr-sensitive isozyme, 25°C
0.086
D-erythrose 4-phosphate
-
Phe-sensitive isozyme, pH 6.8, 25°C
0.092
D-erythrose 4-phosphate
pH 7.5, 60°C, wild-type enzyme
0.0965
D-erythrose 4-phosphate
-
pH 7.0, 37°C
0.13
D-erythrose 4-phosphate
-
Phe-sensitive isozyme, pH 6.8, 30°C
0.138
D-erythrose 4-phosphate
-
pH 7.5, 60°C
0.141
D-erythrose 4-phosphate
-
recombinant enzyme, pH 7.5, 25°C
0.16
D-erythrose 4-phosphate
-
30°C, pH 7.0
0.195
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.0, 30°C
0.25
D-erythrose 4-phosphate
-
Trp-sensitive isozyme, pH 7.2, 37°C
0.25
D-erythrose 4-phosphate
-
wild-type, 25°C, pH 6.4
0.278
D-erythrose 4-phosphate
-
mutant I10A, 25°C, pH 6.4
0.28
D-erythrose 4-phosphate
pH 7.0, 60°C
0.29
D-erythrose 4-phosphate
-
isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
0.3506
D-erythrose 4-phosphate
-
pH 7.5, 70°C
0.392
D-erythrose 4-phosphate
-
mutant N5K, 25°C, pH 6.4
0.43
D-erythrose 4-phosphate
pH 7.5, 30°C
0.5
D-erythrose 4-phosphate
-
Tyr-sensitive isozyme, pH 6.8
0.56
D-erythrose 4-phosphate
-
DAHP synthase-trp, pH 7.0, 37°C
0.77
D-erythrose 4-phosphate
-
DAHP synthase-tyr, pH 7.0, 37°C
0.87
D-erythrose 4-phosphate
-
DAHP synthase-phe, pH 7.0, 37°C
0.9
D-erythrose 4-phosphate
-
pH 7.0, 37°C
1
D-erythrose 4-phosphate
-
DAHP synthase-tyr, pH 7.0, 37°C
1.1
D-erythrose 4-phosphate
-
DS II isozyme, pH 7.5, 37°C
1.2
D-erythrose 4-phosphate
-
pH 6.4, 37°C
1.4
D-erythrose 4-phosphate
-
at 37°C
1.76
D-erythrose 4-phosphate
-
pH 7.5, 37°C
1.95
D-erythrose 4-phosphate
-
cytosolic isozyme DS-Co, pH 8.6, 37°C
2.17
D-erythrose 4-phosphate
-
isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30°C
3.3
D-erythrose 4-phosphate
-
cytosolic isozyme, pH 8.6
3.638
D-erythrose 4-phosphate
-
at 37°C
52.36
D-erythrose 4-phosphate
-
N-terminal deletion mutant, 25°C, pH 6.4
0.003
phosphoenolpyruvate
-
pH 7.5, 30°C
0.0032
phosphoenolpyruvate
-
wild-type, pH 7.9, 30°C
0.0043
phosphoenolpyruvate
-
recombinant wild-type, 30°C, pH 6.5
0.00485
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, wild-type enzyme
0.005
phosphoenolpyruvate
-
recombinant enzyme, with D-arabinose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.0053
phosphoenolpyruvate
-
recombinant enzyme, with erythrose 4-phosphate as cosubstrate, pH 7.5, 25°C
0.0058
phosphoenolpyruvate
-
pH 7.0, 37°C
0.0067
phosphoenolpyruvate
-
pH 7.0, 37°C
0.0087
phosphoenolpyruvate
pH 6.8, 30°C, mutant S213G
0.009
phosphoenolpyruvate
-
pH 7.5
0.009
phosphoenolpyruvate
-
Phe-sensitive isozyme, pH 6.8, 25°C
0.0095
phosphoenolpyruvate
-
pH 7.5, 70°C
0.01
phosphoenolpyruvate
-
recombinant enzyme, with ribose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.011
phosphoenolpyruvate
pH 6.8, 30°C, wild-type enzyme
0.0117
phosphoenolpyruvate
-
pH 7.5, 60°C
0.0128
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant S31G
0.013
phosphoenolpyruvate
-
pH 7.5, 50°C
0.013
phosphoenolpyruvate
-
Tyr-sensitive isozyme, 25°C
0.015
phosphoenolpyruvate
-
pH 7.4, 37°C
0.015
phosphoenolpyruvate
-
recombinant enzyme, with 2-deoxyribose 5-phosphate as cosubstrate, pH 7.5, 25°C
0.015
phosphoenolpyruvate
pH 6.8, 25°C, wild-type enzyme
0.017
phosphoenolpyruvate
pH 7.5, 37°C, presence of Co2+
0.018
phosphoenolpyruvate
-
Phe-sensitive isozyme, pH 6.8, 30°C
0.0196
phosphoenolpyruvate
pH 8.0, 40°C
0.021
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29A
0.025
phosphoenolpyruvate
pH 6.8, 25°C, mutant R126S
0.028
phosphoenolpyruvate
-
mutant N5K, 25°C, pH 6.4
0.03
phosphoenolpyruvate
-
pH 7.0, 25°C
0.031
phosphoenolpyruvate
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mutant I10A, 25°C, pH 6.4
0.033
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-erythrose 4-phosphate
0.035
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate 2-deoxy-D-ribose 5-phosphate
0.035
phosphoenolpyruvate
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wild-type, 25°C, pH 6.4
0.036
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-ribose 5-phosphate
0.039
phosphoenolpyruvate
pH 7.3, temperature not specified in the publication, mutant H29S/S31H
0.043
phosphoenolpyruvate
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pH 7.8, 25°C
0.062
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-arabinose 5-phosphate
0.066
phosphoenolpyruvate
pH 7.5, 60°C, mutant enzyme I181D
0.08
phosphoenolpyruvate
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37°C, pH 7.0
0.09
phosphoenolpyruvate
pH 7.5, 30°C
0.092
phosphoenolpyruvate
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Trp-sensitive isozyme, pH 7.0, 30°C
0.093
phosphoenolpyruvate
pH 6.8, 60°C, cosubstrate D-erythrose 4-phosphate
0.112
phosphoenolpyruvate
pH 7.5, 60°C, wild-type enzyme
0.12
phosphoenolpyruvate
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60°C, pH 6.8
0.125
phosphoenolpyruvate
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Tyr-sensitive isozyme, pH 6.8
0.139
phosphoenolpyruvate
-
pH 7.5, 37°C
0.14
phosphoenolpyruvate
pH 7.5, 25°C
0.1415
phosphoenolpyruvate
-
at 37°C
0.16
phosphoenolpyruvate
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isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
0.2
phosphoenolpyruvate
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DAHP synthase-phe, pH 7.0, 37°C
0.26
phosphoenolpyruvate
-
DAHP synthase-tyr, pH 7.0, 37°C
0.3
phosphoenolpyruvate
-
30°C, pH 7.0
0.4
phosphoenolpyruvate
-
Trp-sensitive isozyme, pH 7.2, 37°C
0.4
phosphoenolpyruvate
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isozyme DS II, pH 7.5, 37°C
0.891
phosphoenolpyruvate
pH 7.0, 60°C
1
phosphoenolpyruvate
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DAHP synthase-tyr, pH 7.0, 37°C
1.11
phosphoenolpyruvate
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DAHP synthase-trp, pH 7.0, 37°C
2
phosphoenolpyruvate
Phe-sensitive isozyme, pH 6.8, 25°C
2.724
phosphoenolpyruvate
-
at 37°C
3.5
phosphoenolpyruvate
-
pH 6.4, 37°C
8.52
phosphoenolpyruvate
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isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C
12.25
phosphoenolpyruvate
-
N-terminal deletion mutant, 25°C, pH 6.4
21
phosphoenolpyruvate
Phe-sensitive isozyme, pH 6.8, 25°C
21
phosphoenolpyruvate
sensitive to metal ion
additional information
additional information
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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kinetics
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additional information
additional information
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mutants
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additional information
additional information
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mutants
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additional information
additional information
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pH-dependence
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics, kinetics in presence of inhibitors L-phe and L-Tyr
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additional information
additional information
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Michaelis-Menten kinetics, kinetics in presence of inhibitors L-phe and L-Tyr
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in complex with a manganese ion and phosphoenolpyruvate. Crystals contain a tetramer in the asymmetric unit. A water molecule occupies the presumed binding site for the phosphate group of 4-erythrose 4-phosphate
modeling of the three dimensional structure of the type II enzyme present in Arabidopsis thaliana and comparison with type I DAHPS. The enzyme belongs to the (beta/alpha)8 TIM barrel family. At the N-terminus of the Arabidopsis thaliana enzyme, there are three non-core helices, alpha0a (Ala72-Lys83), alpha0b (Ala94-Ala106) and alpha0c (Ala113-Val128), but no beta0, in contrast to the microbial type II DAHPS. Also, the (I/L)GAR motif in the type I DAHPS is substituted with xGxR in the case of type II DAHPS. A motif NK(/I)PGR(/K) is present in the sequences of type II DAHPS including At-DAHPS
structure of N-terminal domain AroQ in complex with citrate and chlorogenic acid at 1.9 A and 1.8 A resolution, respectively. Helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. Chlorogenic acid binds with a higher affinity than chorismate
in complex with inhibitor 3-deoxy-D-arabinoheptulosonate-7-phosphate oxime
native and selenomethionine-substituted protein, in complex with phosphoenolpyruvate and Mn2+, mutant E24Q in complex with phosphoenolpyruvate and Mn2+
Phe-sensitive isozyme, enzyme-Mn2+-2-phosphoglycolate-complexes, hanging drop vapour diffusion method, room temperature, all solutions, except the MnSO4 and the enzyme solution, are treated with Chelex-100 to remove metals, 0.2 mM enzyme subunit solution: 0.37 MnSO4, 4.2 mM 2-phosphoglycolate, 0.1 M Li2SO4, 12% PEG 100 w/v, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, pH 8.7, reservoir solution: 19% PEG 1000, 0.1 M Li2SO4, 20% ethanol v/v, 50 mM 1,3-bis[tris(hydroxy-methyl)methylamino]propane buffer, X-ray diffraction structure determination and analysis
Phe-sensitive isozyme, hanging drop vapour diffusion method, 22°C, with or without inhibitor phenylalanine, at pH 6.3-9.4, 0.1-0.2 M monovalent cations, PEG 1000-4000, 0.01 ml protein solution + 0.3 ml precipitant solution, X-ray diffraction structure determination and analysis
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structures of apo form and complex with the inhibitor tyrosine at 2.5 and 2.0 A resolutions, respectively. DAHPS(Tyr) has a typical (beta/alpha)8 TIM barrel, which is decorated with an N-terminal extension and an antiparallel beta sheet. Inhibitor tyrosine binds at a cavity formed by residues of helices alpha3, alpha4, strands beta6a, beta6b and the adjacent loops, and directly interacts with residues P148, Q152, S181, I213 and N8*. Conformational changes of residues P148, Q152 and I213 initiate a transmission pathway to propagate the allosteric signal from the tyrosine-binding site to the active site
structures in complex with Mn2+ and Mn+ and phosphoenolpyruvate, to 1.95 A resolution. The domains assemble as a tetramer, from either side of which chorismate mutase-like regulatory domains asymmetrically emerge to form a pair of dimers. Domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. The catalytic domain adopts a classic TIM barrel (alpha/beta)8 fold. The active site is located on the inside of the C-terminal end of the barrel and is formed by several alpha-beta-connecting loops and two beta-strands. In the holo structure, a manganese ion is present at the active site. In the phosphoenolpyruvate structure, the substrate is adjacent to the manganese ion in a similar position as has been observed in related enzymes
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in complex with chorismate mutase, hanging-drop method, in 20 mM BTP, pH 7.5, 150 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine hydrochloride, 0.2 mM phosphoenolpyruvate and 0.1 mM MnCl2, crystallization after 2 months with no ammonium sulfate and 0.1 M Tris-HCl, pH 7.9-8.0 and PEG 400 or glycerol
in complex with chorismate mutase, streak-seeding conditions in 20 mM BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane), pH 7.5, 150 mM NaCl, 0.5 mM TCEP [tris(2-carboxyethyl)phosphine hydrochloride], 0.2 mM phosphoenolpyruvate, crystallization by 0.9 M ammonium sulfate, 100 mM Tris, pH 7.9 to 8.0, and 1 to 5% PEG 400
recombinant protein, after coexpression with Escherichia coli chaperonins GroEL and GroES in Escherichia coli, crystallized as native and selenomethionine-substituted proten
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purified enzyme mutant S213G with phosphoenolpyruvate and Mn2+, hanging drop vapor diffusion, mixing of 0.001 ml of 11 mg/mL in 10 mM BTP buffer, pH 7.3, in a 1:1 v/v with a reservoir solution containing 0.2 M trimethylamine N-oxide, 0.1 M Tris, pH 8.5, 15-20% w/v PEG 2000 MME, 0.4 mM MnSO4, and 0.4 mM phosphoenolpyruvate, equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffractin structure determination and analysis at 2.0-2.1 A resolution
purified recombinant enzyme complexed with inhibitors (S)-phospholactate, (R)-phospholactate, and vinyl phosphonate, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/mL protein in 10 mM bis(tris(hydroxymethyl)methylamino)propane, pH 7.3, and 5 mM inhibitor, with 0.001 ml of crystallisation buffer containing 0.1 Tris HCl, pH 7.3, 0.2 M trimethyl-amino-N-oxide, 0.4 mM MnSO4, and 15-20% w/v PEG 2000MME, equilibration over 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.76-2.34 A resolution
purified recombinant enzyme mutant R126S, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/mL protein solution with 0.001 ml of crystallisation buffer containing 0.1 Tris HCl, pH 7.3, 0.2 M trimethyl-amino-N-oxide, 0.6 mM MnSO4, and 15-20% w/v PEG 2000MME, equilibration over 0.5 ml of reservoir solution, 20°C, 7 days, X-ray diffraction structure determination and analysis at 2.0 A resolution
structure of type II DAH7PS, encoded by phzC as part of the duplicated phenazine biosynthetic cluster, to 2.7 A resolution, space group C2221 with two DAH7PS chains present in the asymmetric unit
hanging-drop vapor diffusion, ctystal structure of wild-type enzyme and mutant enzyme I181D
recombinant enzyme, in complex with phosphoenolpyruvate
Tyr-sensitive isozyme, hanging drop vapour diffusion method, protein solution in 1:1 mixture with precipitant, 0.004 ml, + 1 ml precipitant solution: 1. 50 mM KH2PO4, 20% polyethylene glycol 8000 w/v or 2. 0.1 M Tris, pH 9.0, 10 mM NiCl2, 20% polyethylene glycol monomethylester 2000 w/v, room temperature for 3 days, X-ray diffraction structure analysis, usage of cryoprotectant glycerol for investigations
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crystals grown in presence of phosphoenolpyruvate and Cd2+, soaked with erythrose 4-phosphate
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molecular modeling of structure. The monomeric structure of Aro1A is a (beta/alpha)8 barrel structure. Phosphoenolpyruvate combines with residues R60, Q116, S119, K141, and R171 through eight hydrogen bonds. D-erythrose 4-phosphate combines with residues R60, K65, Q116, S119, K141, and R171 through nine hydrogen bonds
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C145S
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site-directed mutagenesis, 16% remaining activity compared to the wild-type, 4.6fold increased Km, 1.6fold decreased kcat, and 13.6fold decreased kcat/Km for phosphoenolpyruvate
C334S
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site-directed mutagenesis, unaltered properties
C67L
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site-directed mutagenesis, highly reduced activity, insensitive to inhibition by divalent metal ions
C67S
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site-directed mutagenesis, inactive
S187A
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site-directed mutagenesis, slightly reduced activity
S187C
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site-directed mutagenesis, reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187F
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site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
S187Y
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site-directed mutagenesis, highly reduced activity, activation by tyrosine and phenylalanine instead of inhibition like the wild-type
C328V
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oligo-nucleotide mutagenesis, expression in Escherichia coli strains, 20% reduction in the catalytic constant, 2-3fold increase in Km for the substrates, completely resistant to both spontaneous and Cu2+-catalysed inactivation
C61A
DAHP oxime binding is noncompetitive with respect to Mn2+
C61G
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site-directed mutagenesis, highly reduced activity, highly increased Km for phosphoenolpyruvate, higher pH-optimum than the wild-type
C61V
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oligo-nucleotide mutagenesis, expression in Escherichia coli strains, inactive, does not bind metal ions, resistant to metal attack, no subunit dissociation upon Cu2+ treatment
D326A
DAHP oxime binding is noncompetitive with respect to Mn2+
DELTA1-15
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N-terminal deletion of amino acids 1-15, no formation of dimeric form
E24Q
unlike tetrameric enzyme, mutant is dimeric in solution
F144A
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inhibition by phenylalanine, 30% residual activity
F209A
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inhibition by phenylalanine, 79% residual activity
H172G
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site-directed mutagenesis, inactive
H207G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, reduced kcat
H268A
DAHP oxime binding is competitive with respect to Mn2+
H268G
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site-directed mutagenesis, inactive
H304G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64G
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site-directed mutagenesis, reduced activity, increased Km values for the substrates, increased kcat
H64L
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oligo-nucleotide mutagenesis, expression in Escherichia coli strains, unstable to treatment with phosphoenolpyruvate, half-life of about 24 h at 0.4 mM compared to 6 days for the wild-type
I213P
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
L175A
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inhibition by phenylalanine, 18% residual activity
L175D
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inhibition by phenylalanine, 83% residual activity
L179A
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inhibition by phenylalanine, 82% residual activity
N8A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
N8K
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
P148A
overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
P150L
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inhibition by phenylalanine, no inhibition by phenylalanine
Q152A
overexpression of variant leads to higher accumulation of phenylalanine
S181A
overexpression of variant leads to higher accumulation of phenylalanine
V221A
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inhibition by phenylalanine, 95% residual activity
W215A
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inhibition by phenylalanine, 58% residual activity
I213P
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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N8A
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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P148A
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overexpression of variant leads to less decrease in the accumulation of phenylalanine than overexpression of wild-type
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Q152A
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overexpression of variant leads to higher accumulation of phenylalanine
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S181A
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overexpression of variant leads to higher accumulation of phenylalanine
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N8K
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similar activity and substrate affinities like the wild-type, but insensitive against inhibition by tyrosine, decreased thermostability
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R126S
site-directed mutagenesis, mutation of the residue involved in the salt bridge formation of Arg126-Glu27 results in perturbation of the less extensive interface in the enzyme tetramer and formation of enzyme dimers in solution. The dimeric NmeDAH7PSR126S variant exhibits a slight reduction in thermal stability by differential scanning calorimetry experiments and a slow loss of activity over time compared to the wild-type enzyme. Although NmeDAH7PSR126S crystallised as a tetramer, like the wild-type enzyme, structural asymmetry at the less extensive interface was observed consistent with its destabilisation
I181D
mutant enzyme is catalytically more active than the wild type enzyme from 20 to 80°C, the mutation disrupts the tetrameric structure of the enzyme, the melting temperatures of the wild-type protein are significantly higher than the melting temperatures of mutant enzyme I181D at pH values greater than 6.5
K229L
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the mutation eliminates the L-tyrosine sensitivity
P165G
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inhibited by tryptophan
Q302R
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inhibited by tryptophan
S195A
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inhibited by tryptophan
H29A
site-directed mutagenesis, the mutant is inhibited by both L-Tyr and L-Phe
H29S/S31H
site-directed mutagenesis, the mutant is inhibited to a greater extent by L-Phe than L-Tyr
S31G
site-directed mutagenesis, the mutation severely reduces inhibition by L-Tyr
I10A
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inhibition by phenylalanine, 95% residual activity
I10A
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kinetic parameter similar to wild-type, part of enzyme is monomer instead of dimer
L175Q
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inhibition by phenylalanine, 44% residual activity
L175Q
phenylalanine-feedback-insensitive mutant
N5K
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inhibition by phenylalanine, 33% residual activity
N5K
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kinetic parameter similar to wild-type
S213G
site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
S213G
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site-directed mutagenesis, a single Ser residue at the bottom of the inhibitor-binding cavity is substituted to Gly, which alters inhibitor specificity from L-Phe to L-Tyr
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additional information
random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
additional information
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random mutagenesis, the AroF variant with a deficiency in residue Ile11 is insensitive to L-tyrosine. Construction of feedback-resistant 3-deoxy-D-arabino-heptulosonate-7-phosphate synthases by engineering the N-terminal domain for L-phenylalanine synthesis, generation of nine AroF variants with truncation of different N-terminal fragments, the variants AroFD(1-9), AroFD(1-10), AroFD(1-12) and, in particular, AroFD(1-11) significantly lead to the accumulation of L-phenylalanine, overview. Mutant AroFDELTA(1-11) does not show any feedback inhibition by L-Phe, demonstrated in a strain that has a high L-Phe level through coexpression of L-Phe producing chorismate mutase-4-prephenate dehydratase
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additional information
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deletion mutant of Tr-sensitive isozyme, gene aroF, lacking the first 7 amino acid residues of the N-terminus, mutant is insensitive against inhibition by tyrosine
additional information
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N-terminal deletion mutant, no inhibition by phenylalanine
additional information
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KDPGal aldolase mutant EC03-1 (F33I/D58N/Q72H/A75V/V85A/V154F) develops increased DAHP synthase activity
additional information
recombinant expression of aroG in transgenic Solanum lycopersicum cv. 82 fruits results in ripe AroG-expressing tomato fruits that have a preferred floral aroma compare with fruits of the wild-type line. Plants expressing the bacterial gene exhibit enhanced levels of a number of aromatic specialized metabolites in a manner that is specific to the bacterial enzyme. Metabolic profiling of transgenic tomato plants expressing a bacterial feedback-insensitive AroG gene, overview
additional information
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deletion mutant of Tr-sensitive isozyme, gene aroF, lacking the first 7 amino acid residues of the N-terminus, mutant is insensitive against inhibition by tyrosine
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additional information
overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
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overexpression of 3-deoxy-7-phosphoheptulonate synthase gene from Gossypium hirsutum enhances Arabidopsis resistance to infection by Verticillium dahliae and Verticillium wilt. GhDHS1 overexpression is associated with longer primary roots for Arabidopsis plants. GhDHS1 overexpression increases xylem lignification of Arabidopsis plants in response to Verticillium dahliae infection
additional information
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loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
additional information
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loss of 81 N-terminal amino acid resiudes leads to more flexibility in global terms of structure and a higher degree of compaction. A strain carrying the mutant shows an increased 2-phenylethanol production
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