1.3.1.12: prephenate dehydrogenase
This is an abbreviated version!
For detailed information about prephenate dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.12
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1.3.1.12
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l-tyrosine
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h-protein
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arogenate
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hyperglycinemia
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nonketotic
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4-hydroxyphenylpyruvate
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aminomethyltransferase
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dahp
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3-deoxy-d-arabino-heptulosonate
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cyclohexadienyl
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7-phosphate
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dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
- 1.3.1.12
- l-tyrosine
- h-protein
- arogenate
- hyperglycinemia
-
nonketotic
- 4-hydroxyphenylpyruvate
- aminomethyltransferase
- dahp
-
3-deoxy-d-arabino-heptulosonate
-
cyclohexadienyl
- 7-phosphate
- dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
Reaction
Synonyms
AceF, AroQ, bifunctional T-protein, chorismate mutase-prephenate dehydratase, chorismate mutase-prephenate dehydrogenase bifunctional enzyme, chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme, Chorismate mutase/prephenate dehydratase, CM-PD, CM-TyrAp, CM/PDT/PDHG, CMPD, dehydrogenase, prephenate, hydroxyphenylpyruvate synthase, PD, PDH, pdhE-1, PDHG, T-protein, TYR1, tyrA, TyrA dehydrogenase, TyrAp
ECTree
1.3.1.12 prephenate dehydrogenaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.3.1.12 - prephenate dehydrogenase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
trans-2,3-pleiadanedicarboxylic acid
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i.e. diacid, 50% inhibition at 0.25 mM, inhibits competitively the prephenate dehydrogenase activity, but not the chorismate mutase activity of the enzyme
iodoacetamide
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modification of only one cysteinyl residue results in the inactivation
L-Tyr
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L-Tyr inhibits TyrAp activity by 90% at concentrations higher than 0.5 mM
L-tyrosine
tyrosine binding to ACT domains inactivates the enzyme by blocking both substrate-binding sites and one NAD+ site with the ACT domain of one subunit. Interaction occurs with residues S333 and D315 for both ACT domains
L-tyrosine
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Tyr263 or residues 354 to 357 of the enzyme are involved in the feedback inhibition
L-tyrosine
the enzyme is completely inhibited by 0.2 mM L-tyrosine with either NAD+ or NADP+ as cosubstrate
L-tyrosine
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the enzyme exhibits 30% and 60% residual activity at 1 mM L-tyrosine with NAD+ or NADP+ as cosubstrate, respectively
tyrosine
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feedback-inhibitor of activity over a wide temperature range, enhances the cooperativity between subunits in the binding of prephenate
tyrosine
binds directly to the active site of the enzyme and not to an allosteric site. Linear competitive inhibition
tyrosine
is bound directly at the catalytic site as a competitive inhibitor
additional information
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EDTA, MgCl2 and ZnCl2 show no effect on enzyme activity
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additional information
phenylalanine (up to 5 mM) has no effect. Not inhibited by prephenate or NAD+ at concentrations up to 10 and 2 mM, respectively
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additional information
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phenylalanine (up to 5 mM) has no effect. Not inhibited by prephenate or NAD+ at concentrations up to 10 and 2 mM, respectively
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additional information
not inhibitory: NaCl up to 10 mM, EDTA and dithiothreitol up to 1 mM
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