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
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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
4.2.1.51 prephenate dehydrataseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.2.1.51 - prephenate dehydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
L-phenylalanine
inhibits activity at 5 microM, competitive inhibition
L-phenylalanine
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feedback inhibition, Ser99 is involved, mutants S99M, S99T, S99A, S99C, or S99L are not sensitive to inhibition
L-phenylalanine
feedback inhibition. PDT of Escherichia coli WSH-Z06 is almost completely inhibited by 10 mM L-phenylalanine (92.9% activity loss). PDT of Escherichia coli WSH-Z06 (pAP-B03) exhibits strong resistance to 200 mM L-phenylalanine, manifested by the high residual activities (10 mM L-phenylalanine with only 7.1% loss of activity)
L-phenylalanine
feedback regulation wild-type, mutant enzyme MTR1 (PDT S298I) shows a reduced feedback sensitivity, resulting in phenylalanine accumulation; inhibits activity of wild-type enzyme, mutant enzyme shows reduced feedback sensitivity, accumulation of L-phenylalanine
NaCl
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enzyme activity is completely abolished in the presence of 200 mM and higher concentrations of NaCl
additional information
changes in the ESRP sequence, involved in allosteric binding of phenylalanine, lead to desensitization to inhibition by phenylalanine, permitting the overproduction of the amino aid in vivo
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additional information
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changes in the ESRP sequence, involved in allosteric binding of phenylalanine, lead to desensitization to inhibition by phenylalanine, permitting the overproduction of the amino aid in vivo
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