4.2.1.51: prephenate dehydratase
This is an abbreviated version!
For detailed information about prephenate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.51
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4.2.1.51
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l-phenylalanine
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arogenate
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l-tyrosine
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dahp
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l-phe
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7-phosphate
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cyclohexadienyl
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l-tyr
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3-deoxy-d-arabino-heptulosonate
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feedback-inhibited
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5.4.99.5
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synthesis
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industry
- 4.2.1.51
- l-phenylalanine
- arogenate
- l-tyrosine
- dahp
- l-phe
- 7-phosphate
-
cyclohexadienyl
- l-tyr
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3-deoxy-d-arabino-heptulosonate
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feedback-inhibited
-
5.4.99.5
- synthesis
- industry
Reaction
Synonyms
ADT1, ADT2, ADT6, AroQ, chorismate mutase prephenate dehydratase, chorismate mutase-prephenate dehydratase, Chorismate mutase/prephenate dehydratase, CM-PD, CM/PDT/PDHG, Cmut1, CM–PDT, Ct-PDT, cyclohexydienyl dehydratase, dehydratase, prephenate, Gmut11, Gmut9, MjPDT, monofunctional prephenate dehydratase, MtbPDT, P-protein, P-protein dehydratase, PDT, PDT protein, PheA, PpADT-B, PpADT-C, PpADT-G, prephenate dehydratase, prephenate dehydratase 1, Sa-PDT
ECTree
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Subunits
Subunits on EC 4.2.1.51 - prephenate dehydratase
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dimer
homohexamer
homotetramer
octamer
oligomer
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L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
tetramer
additional information
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the enzyme consists of 3 domains: a chorismate mutase domain, a prephenate dehydratase domain, and a regulatory domain
?
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x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE
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2 * 35000, low activity in absence of activators, high activity in presence of activators
dimer
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2 * 43111, smallest native species of enzyme, calculation from nucleotide sequence
dimer
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L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
determined by small angle X-ray scattering and analytical ultracentrifugation
homotetramer
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determined by small angle X-ray scattering and analytical ultracentrifugation
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tetramer
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L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
tetramer
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4 * 18000, bifunctional enzyme prephenate dehydratase-arogenate dehydratase, SDS-PAGE