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55001 Sigma

L-Phenylalanine Dehydrogenase from Rhodococcus sp. M4

≥120 U/mL

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Properties

Related Categories 1.4.x.x Acting on CH-NH2, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Cell Biology, Chemical Synthesis,
form   solution (clear)
concentration   ≥120 U/mL
impurities   25 mM potassium phosphate
  250 mM NaCl
  50% glycerol
color   light yellow
storage temp.   −20°C

Description

Unit Definition

1 U corresponds to the amount of enzyme which catalyzes the oxidation of 1μmol L-phenyl-alanine per minute at pH 10.7 and 30°C to phenyl-pyruvate and ammonia (NAD+ as cofactor)

Application

L-Phenylalanine dehydrogenase (PHD) is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. It is utilized in amino acid binding and discrimination studies as well as in studies to elucidate the stereochemistry of enzyme-catalyzed hydride transfer .

Biochem/physiol Actions

L-Phenylalanine dehydrogenase (PHD) catalyzes the NAD+-dependent, reversible, oxidative deamination of L-phenylalanine to form ammonia, phenyl pyruvate, and NADH. Phenylalanine dehydrogenase isolated from Rhodococcus sp. M4 is a tetramer of 39.5-kDa monomers.

Price and Availability

Suggested Laboratory Gloves


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Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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