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
-
pH 9.0, stable
30 - 45
-
native enzyme, 15 min, 96% activity remaining at pH 7.5, no activity remaining at pH 10.4
30 - 55
after incubation at 30-55C for 1 h under pH 10.0, the enzyme retains over 60% of its maximal activity while it retains about no activity at 55C
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 15C and its thermostability is improved by about 6C over 10 min incubation, the conjugate is more resistant to thermal inactivation at different temperatures, ranging from 45 to 60C, the T50 value is increased from 54 to 61C 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 45C to 60C is noticeably increased after glycosylation