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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Crystallization
Crystallization on EC 1.3.1.12 - prephenate dehydrogenase
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in complex with NAD+, by hanging drop vapor diffusion technique at room temperature, one modified nucleotide-binding domain and a novel helical prephenate binding domain, active site formed at the domain interface and shared between the subunits of the dimer, access to active site may be regulated via a gated mechanism, modulated by an ionic network involving a conserved arginine, active site residues include Ser126 and Lys246 and the catalytic His147, two functional domains of chorismate mutase-prephenate dehydrogenase are interdependent
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prephenate dehydrogenase bound with NAD+ plus either 4-hydroxyphenylpyuvate, 4-hydroxyphenylpropionate, or L-tyrosine. Resiudes His147 and Arg250 are key catalytic and binding groups, respectively, and Ser126 participates in both catalysis and substrate binding through the ligand 4-hydroxyl group. Inhibitor tyrosine binds directly to the active site of the enzyme and not to an allosteric site
structure of a ternary complex with NAD+ and tyrosine to 2.2 A resolution, a binary complex with tyrosine, and a structure of an isolated ACT domain dimer
prephenate dehydrogenase component of the TyrA protein from strain Rd KW20 in complex with inhibitor tyrosine and cofactor NAD+, sitting drop vapour diffusion method, 200 nl of 19.6 mg/ml protein in 20 mM HEPES pH 8.0, 200 mM NaCl, 40 mM imidazole, 1 mM TCEP are mixed with 200 nl reservoir solution containing 0.04 M potassium dihydrogen phosphate, 20.0% v/v glycerol and 16.0% w/v PEG 8000, X-ray diffrraction structure determination and analysis at 2.0 A resolution
to 2.1 A resolution. The N-terminal alpha/beta domain has a Rossman fold for binding a NAD+ molecule. The C-terminal domain adopts a helical architecture and is involved in homo-dimerization. NAD+ binding stabilizes the active site and facilitates the substrate, prephenate, binding