1.4.1.20: phenylalanine dehydrogenase
This is an abbreviated version!
For detailed information about phenylalanine dehydrogenase, go to the full flat file.
Reaction
Synonyms
dehydrogenase, phenylalanine, L-PheDH, L-phenylalanine dehydrogenase, L-phenylalanine:NAD+ oxidoreductase, deaminating, PDH, PHD, PheDH, phenylalanine dehydrogenase, recombinant PheDH, recombinant phenylalanine dehydrogenase
ECTree
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Crystallization
Crystallization on EC 1.4.1.20 - phenylalanine dehydrogenase
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molecular modeling of structure and docking of substrates. In mutant V144L, the distances of active/binding site and substrate with an appropriate orientation decrease for phenylalanine and increase for tyrosine. In mutant V144N, the distances of active/binding site and substrate are increased for phenylalanine and are reduced for tyrosine. In mutant V144D, distances considerably increase with an inappropriate orientation
hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Two crystal forms are obtained in the presence and absence of the enzyme substrates phenylpyruvate or Phe and its coenzyme NADH
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enzyme-NAD+-phenylpyruvate complex and enzyme-NAD+-beta-phenylpropionate complex
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phenylalanine dehydrogenase surface behaviour at the air/aqueous interface. The enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time. The immobilized films presents a homogeneous and regular deposition
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