1.14.13.44: 2-hydroxybiphenyl 3-monooxygenase

This is an abbreviated version!
For detailed information about 2-hydroxybiphenyl 3-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.44

Reaction

2-Hydroxybiphenyl
+
NADH
+
H+
+
O2
=
2,3-Dihydroxybiphenyl
+
NAD+
+
H2O

Synonyms

2-hydroxybiphenyl 3-monooxygenase, HbpA, oxygenase, 2-hydroxybiphenyl 3-mono-

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.44 2-hydroxybiphenyl 3-monooxygenase

Engineering

Engineering on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G255F
the variant exhibits 7% compared to the specific activity of the wild-type enzyme on NADH and 2,3-dihydroxybiphenyl, suggesting inhibition of substrate entrance into the active site by the large aromatic residue
I244V
-
mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase
R242A
the variant is not active on NADH and 2,3-dihydroxybiphenyl
R242E
the variant is not active on NADH and 2,3-dihydroxybiphenyl
R242Q
the variant is not active on NADH and 2,3-dihydroxybiphenyl
V368A/L417F
-
double replacement improves the efficiency of substrate hydroxylation by reducing the uncoupled oxidation of NADH. With guaiacol as substrate, the Vmax is increased and the Km-value is decreased. With 2-tert-butylphenol as substrate the turnover number is increased more than 5fold
W225A
the variant exhibits 7% compared to the specific activity of the wild-type enzyme on NADH and 2,3-dihydroxybiphenyl
W225Y
the variant exhibits 122% compared to the specific activity of the wild-type enzyme on NADH and 2,3-dihydroxybiphenyl
I244V
-
mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase
-
V368A/L417F
-
double replacement improves the efficiency of substrate hydroxylation by reducing the uncoupled oxidation of NADH. With guaiacol as substrate, the Vmax is increased and the Km-value is decreased. With 2-tert-butylphenol as substrate the turnover number is increased more than 5fold
-
additional information