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1.14.16.1: phenylalanine 4-monooxygenase

This is an abbreviated version!
For detailed information about phenylalanine 4-monooxygenase, go to the full flat file.

Word Map on EC 1.14.16.1

Reaction

L-phenylalanine
+
a 5,6,7,8-tetrahydropteridine
 +
O2
=
L-tyrosine
 +
a 4a-hydroxy-5,6,7,8-tetrahydropteridine

Synonyms

cePAH, DicPAH, EC 1.14.3.1, EC 1.99.1.2, HPAH, L-phenylalanine 4-hydroxylase, oxygenase, phenylalanine 4-mono-, P4H, PAH, PheH, phenylalaninase, phenylalanine 4-hydroxylase, phenylalanine hydroxylase, phenylalanine monooxygenase, PheOH, phhA

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.16.1 phenylalanine 4-monooxygenase

Temperature Stability

Temperature Stability on EC 1.14.16.1 - phenylalanine 4-monooxygenase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
holo-phenylalanine hydroxylase displays a large increase in thermal stability (approximately 15°C upshift in the Tm value) compared with the apoenzyme (melting temperature at 64°C), holo-caPAH shows higher kinetic stability at optimal growth temperature (denaturing approximately 8 times more slowly than the apo form at 55°C)
44 - 76
pH 7.4, kinetics of thermal unfolding of apo- and holo-enzymes within the temperature range and with different metal cofactors: native Fe2+, or artificial Zn2+ or Co2+, unfolding profiles, transition-state analysis shows a common mechanism for all enzyme variants, at higher temperatures the unfolding rates of Zn- and Co-PAH are affected significantly by entropy, while the unfolding rates of apo- and Fe-PAH are dominated by enthalpy even at higher temperatures, overview
47
-
50% residual activity after 66 min, presence of Fe(II), after 8 min in presence of EDTA
51
L348V mutant enzyme, 50% activity after 10 min
52
-
Tm, inactivation
53
-
melting temperature of enzyme, presence of EDTA
59
recombinant wild-type enzyme, 50% activity after 10 min
63
-
melting temperature of enzyme, presence of Fe(II)
additional information