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
-
tetrahydrofolate-dependent
-
glycine-cleavage
-
aminomethyl
-
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
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Subunits
Subunits on EC 1.3.1.12 - prephenate dehydrogenase
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dimer
homohexamer
additional information
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MW of recombinant enzyme fragments, overview, structural localization of the different enzyme activities on the enzyme molecule
dimer
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wild-type full length enzyme and some enzyme fragments form homodimers
dimer
SDS-PAGE and gel filtration, the dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain, structure comparisons, overview
dimer
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SDS-PAGE and gel filtration, the dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain, structure comparisons, overview
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