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
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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 (Engineering
Engineering on EC 4.2.1.51 - prephenate dehydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E64D
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constructed by PCR-based random mutagenesis and complementation analysis, 15% reduced activity compared to the wild-type enzyme, 4.5% increased Km, 1.7fold increased kcat
E64Q
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
E64S
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
E64V
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
F185L
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
F185Y
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constructed by PCR-based random mutagenesis and complementation analysis, 96% reduced activity compared to the wild-type enzyme, 26% increased Km
R184L
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constructed by PCR-based random mutagenesis and complementation analysis, 50% reduced activity compared to the wild-type enzyme
S99A
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99C
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99L
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99M
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constructed by PCR-based random mutagenesis and complementation analysis, 30% reduced activity compared to the wild-type enzyme, insensitive to inhibition by phenylalanine
T183A
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
T183S
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constructed by PCR-based random mutagenesis and complementation analysis, highly reduced activity
T183Y
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constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
S99A
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
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S99C
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
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S99L
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constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
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S99M
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constructed by PCR-based random mutagenesis and complementation analysis, 30% reduced activity compared to the wild-type enzyme, insensitive to inhibition by phenylalanine
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E159A/E232A
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site-directed mutagenesis, 7fold increased kcat, 4.6fold decreased Km compared to the wild-type, increased activity
T278A
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site-directed mutagenesis, catalytically inactive mutant, but binds to substrate and inhibitor
T278V
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site-directed mutagenesis, catalytically inactive mutant, but binds to substrate and inhibitor
T326P
mutant harboring pheAfbr retains more than 70% of CM and PDT activities even in the presence of 200 mM L-phenylalanine, has potential in overproduction of L-phenylalanine
T326P
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mutant harboring pheAfbr retains more than 70% of CM and PDT activities even in the presence of 200 mM L-phenylalanine, has potential in overproduction of L-phenylalanine
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additional information
additional information
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alterations of Asp76, Glu89, His115, and Arg236 do not cause significant changes in the kinetics properties
additional information
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alterations of Asp76, Glu89, His115, and Arg236 do not cause significant changes in the kinetics properties
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additional information
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expression of genes contaninig P-protein domains or subdomains, comparison of their catalytic activities and activation by phenylalanine
