1.4.1.20: phenylalanine dehydrogenase

This is an abbreviated version!
For detailed information about phenylalanine dehydrogenase, go to the full flat file.

Word Map on EC 1.4.1.20

Reaction

L-phenylalanine
+
H2O
+
NAD+
=
phenylpyruvate
+
NH3
+
NADH
+
H+

Synonyms

dehydrogenase, phenylalanine, L-PheDH, L-phenylalanine dehydrogenase, L-phenylalanine:NAD+ oxidoreductase, deaminating, PDH, PHD, PheDH, phenylalanine dehydrogenase, recombinant PheDH, recombinant phenylalanine dehydrogenase

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.20 phenylalanine dehydrogenase

General Stability

General Stability on EC 1.4.1.20 - phenylalanine dehydrogenase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2.5 mM L-Phe after 21 days of incubation at 4°C in 50 mM sodium phosphate buffer, pH 7.0
-
20% glycerol, 0.25 M sodium malonate or 0.5 M sodium glutarate stabilize the enzyme during storage at 4°C
-
after pre-treatment with 1 M NaCl at 55°C for 1 h, the enzyme exhibits high activity and retains over 50% of its maximal activity during pH 7.0-8.5
glycosylation increases temperature stability
-
PheDH covalently immobilized on amino-activated cellulose membrane by cross-linking with glutaraldehyde retains 82% of the initial activity, the enzyme-coated electrode retains full electrocatalytic activity after 16 days of storage at 4°C in 50 mM sodium phosphate buffer (pH 7.0)
-
the enzyme chemically glycosylated with an end-group aminated dextran shows improved thermal and conformational stability
-
the enzyme-coated Au-CD electrode is highly stable, retaining about 97% of its initial electrocatalytic response toward
-
unstable in absence of glycerol and salt
-