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

Temperature Stability

Temperature Stability on EC 1.4.1.20 - phenylalanine dehydrogenase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
after incubation at 30-55°C for 1 h under pH 10.0, the enzyme retains over 60% of its maximal activity while it retains about no activity at 55°C
30 - 45
-
native enzyme, 15 min, 96% activity remaining at pH 7.5, no activity remaining at pH 10.4
30
-
pH 9.0, stable
37
-
t1/2: 48 min, in absence of substrate or coenzyme. t1/2: 2000 min, in presence of 10 mM L-Leu and 1.0 mM NAD+
45 - 61
-
the optimum temperature for the glycosylated enzyme is increased by 15°C and its thermostability is improved by about 6°C over 10 min incubation, the conjugate is more resistant to thermal inactivation at different temperatures, ranging from 45 to 60°C, the T50 value is increased from 54 to 61°C for PheDH after glycosidation
53
-
pH 6.0, 5 min, 50% loss of activity; pH 9.5-10, 2 h, 50% loss of activity; phenylpyruvate destabilizes the activity, 1 M sorbitol or 1 M glycerol stabilize
58
-
pH 7.0-9.5, 60 min, chimeric enzyme, loss of activity above
62
-
T50-value of the dextran-modified enzyme
65 - 70
70
-
60 min, wild-type enzyme is stable
additional information
-
the enzyme glycosylated with mono-6-amino-6-deoxy-beta-cyclodextrin and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-beta-cyclodextrin contains about 18 mol and 15 mol oligosaccharide per mol of protein and retains 60% and 81% of the initial activity, respectively. the thermostability profile of the enzyme is improved abd its resistance to thermal inactivation at different temperatures ranging from 45°C to 60°C is noticeably increased after glycosylation