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1.14.13.24: 3-hydroxybenzoate 6-monooxygenase

This is an abbreviated version!
For detailed information about 3-hydroxybenzoate 6-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.24

Reaction

3-hydroxybenzoate
+
NADH
 +
H+
 +
O2
=
2,5-Dihydroxybenzoate
 +
NAD+
 +
H2O

Synonyms

3-HBA-6-hydroxylase, 3-hydroxybenzoate 6-hydroxylase, 3-hydroxybenzoate-6-hydroxylase, 3-hydroxybenzoic acid-6-hydroxylase, 3HB6H, m-hydroxybenzoate 6-hydroxylase, MNX2, Mnx2p, NagX, NarX, Ncgl2923, oxygenase, 3-hydroxybenzoate 6-mono-, XlnD

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
                1.14.13.24 3-hydroxybenzoate 6-monooxygenase

Engineering

Engineering on EC 1.14.13.24 - 3-hydroxybenzoate 6-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R169E
site-directed mutagenesis, inactive mutant
A308G
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, comparison of FAD contents
Q305P
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, comparison of FAD contents
Y221F
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, comparison of FAD contents
Y306H
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, comparison of FAD contents
H213A
H213D
the mutant enzyme can bind to 3-hydroxybenzoate with similar affinity as the wild-type enzyme and form C4a-hydroperoxy intermediate. It produces 2,5-dihydroxybenzoate with yields of 52%
H213E
the mutant enzyme can bind to 3-hydroxybenzoate with similar affinity as the wild-type enzyme and form C4a-hydroperoxy intermediate. It produces 2,5-dihydroxybenzoate with yields of 92%. The hydroxylation rate constant of the mutant enzyme (35/s) is similar to that of wild-type enzyme (36/s) and this variant has an efficiency of hydroxylation (92%) similar to the wild-type enzyme (86%)
H213S
Y105F
the mutant shows less affinity for the aromatic substrate and lower catalytic efficiency compared to the wild type enzyme
Y217A
the mutant enzyme does not show any perturbation of flavin absorption upon addition of 3-hydroxybenzoate
Y217F
the mutant enzyme has a Kd value for 3-hydroxybenzoate binding of 7.5 mM, which is about 50fold larger than that found for wild-type enzyme. The results indicate that Tyr217 is necessary for substrate binding
Y217S
the mutant enzyme does not show any perturbation of flavin absorption upon addition of 3-hydroxybenzoate
additional information