Description
Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine €-dehydrogenase, and meso-a,€-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure.
Abbr
PheDH, Native (Thermoactinomyces intermedius)
Source
Thermoactinomyces intermedius
Appearance
Ammonium sulphate suspension
Enzyme Commission Number
EC 1.4.1.20
Contaminants
(as PheDH activity = 100 %)
NADH oxidase: < 0.01 %;
Lactate dehydrogenase: < 0.01 %.
Molecular Weight
ca. 380,000; Subunit molecular weight : ca. 40,000.
Michaelis Constant
(200 mM Gly-KCl-KOH buffer, pH 11.0, at 30 °C)
L-Phenylalanine: 0.66 mM;
NAD+: 0.05 mM.
Specificity
L-Phenylalanine: 100 %;
L-Tyrosine: 7.6 %;
L-Methionine: 1.5 %.
Unit Definition
One unit of activity is defined as the amount of PheDH that forms 1 μmol of NADH per minute at 30 °C.
Thermal stability
No detectable decrease in activity up to 50 °C.
Storage
Stable at 0 to 4 °C for at least six months (Do not freeze).
Synonyms
phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9
Specific Activity
more than 30 U/mg protein
Reaction
L-Phenylalanine + NAD+ + H2O ←→ Phenylpyruvate + NH4+ + NADH
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