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Literature summary for 1.3.1.12 extracted from

  • Sun, W.; Singh, S.; Zhang, R.; Turnbull, J.L.; Christendat, D.
    Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism (2006), J. Biol. Chem., 281, 12919-12928.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
into vector pET15b and expressed in Escherichia coli BL21-Gold (DE3) Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Aquifex aeolicus

Protein Variants

Protein Variants Comment Organism
additional information delta19-PDH, delta25-PDH, and delta28-PDH, which produce stable and soluble proteins, delta36-PDH, delta52-PDH, and delta55-PDH are unstable Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni-NTA column Aquifex aeolicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate + NAD+
-
Aquifex aeolicus 4-hydroxyphenylpyruvate + NADH + CO2
-
?

Subunits

Subunits Comment Organism
dimer gel filtration Aquifex aeolicus

Synonyms

Synonyms Comment Organism
PDH
-
Aquifex aeolicus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Aquifex aeolicus