2.5.1.111: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase

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For detailed information about 4-hydroxyphenylpyruvate 3-dimethylallyltransferase, go to the full flat file.

Reaction

Synonyms

4HPP dimethylallyltransferase, apT, aromatic prenyltransferase, CloQ, FamD1, isoprenyl transferase, NovQ

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.111 4-hydroxyphenylpyruvate 3-dimethylallyltransferase

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Results	in table
5	AA Sequence
2	Application
8	Cloned(Commentary)
4	Crystallization (Commentary)
1	Expression
4	General Information
3	Inhibitors
13	kcat/KM [mM/s]
17	KM Value [mM]
8	Metals/Ions
3	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
18	Organism
3	Pathway
4	pH Optimum
23	Protein Variants
7	Purification (Commentary)
1	Reaction
16	Reference
51	Substrates and Products (Substrate)
8	Subunits
22	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
15	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.5.1.111 - 4-hydroxyphenylpyruvate 3-dimethylallyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor diffusion method, using 1.0 M sodium citrate, 0.1 M imidazole, pH 8.0

Fischerella ambigua

A0A1J0AKI6

746999

crystals are grown by hanging-drop vapor diffusion at 20 °C. Structure of of the apoenzyme, of CloQ complexed with 4-hydroxyphenylpyruvate, of mutant enzyme C215S complexed with 4-hydroxyphenylpyruvate and of the mutant enzyme R66S complexed with 4-hydroxyphenylpyruvate. Structure of CloQ complexed with 4-hydroxyphenylpyruvate reveals the formation of a covalent link between the substrate and Cys215 to yield a thiohemiketal species

Streptomyces roseochromogenus subsp. oscitans

Q8GHB2

722973

crystals are grown by vapour diffusion. The protein crystallizes in space group I4(1)22, with unit-cell parameters a = b = 135.19, c = 98.13 A. Native data from a single crystal are recorded to a resolution of 2.2 A in-house

Streptomyces roseochromogenus subsp. oscitans

Q8GHB2

721178

molecular mechanics and hybrid quantum mechanics/molecular mechanics molecular dynamics simulations. Positively charged basic residues line the inside of the beta-barrel of CloQ to activate the diphosphate leaving group to replace the function of the Mg(2+) cofactor in other APTases. The effect of the replacement of the Mg(2+) cofactor with basic residues yields a similar activation barrier for prenylation to Mg(2+)-dependent APTases like NphB. The topology of the binding pocket for 4-hydroxyphenylpyruvate is important for selective prenylation at the ortho position of the ring. Methylation at this position alters the conformation of the substrate for O-prenylation at the phenol group

Streptomyces roseochromogenus subsp. oscitans

Q8GHB2

737697