1.14.13.2: 4-hydroxybenzoate 3-monooxygenase

This is an abbreviated version!
For detailed information about 4-hydroxybenzoate 3-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.2

Reaction

4-hydroxybenzoate
+
NADPH
+
H+
+
O2
=
3,4-dihydroxybenzoate
+
NADP+
+
H2O

Synonyms

4-HBA 3-hydroxylase, 4-HBA 3-monooxygenase, 4-HBA-3-hydroxylase, 4-HBMO, 4-hydroxybenzoate 3-hydroxylase, 4-hydroxybenzoate 3-monooxygenase, 4-hydroxybenzoate hydroxylase, 4-hydroxybenzoate monooxygenase, 4-hydroxybenzoic hydroxylase, 4HBA 3-hydroxylase, BxeA2040, HBH, m-hydroxybenzoate hydroxylase, MobA, ncgl1032, oxygenase, 4-hydroxybenzoate 3-mono-, p-hydroxybenzoate hydroxylase, p-hydroxybenzoate-3-hydroxylase, p-hydroxybenzoic acid hydrolase, p-hydroxybenzoic acid hydroxylase, p-hydroxybenzoic hydroxylase, para-hydroxybenzoate hydroxylase, PHBAD, PHBH, PHBHase, PobA, pobACg, POHBase

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
                1.14.13.2 4-hydroxybenzoate 3-monooxygenase

Engineering

Engineering on EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A16T/S394P/D416A
low ability to hydroxylate 3-aminophenol
A400G
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R
A400G/K429R
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
H135P
alters the enzyme's substrate specificity; low ability to hydroxylate 3-aminophenol
H135P/I217L/Y304H
low ability to hydroxylate 3-aminophenol
K326I
lacks the ability to transform phenol to catechol as the wild-type
K429R
can not transform 3-aminophenol at all
N102T/I259S/V399M
low ability to hydroxylate 3-aminophenol
N227H
is not able to transform 3-aminophenol
N227H/D416A
almost has the same transformation efficiency as mutant N227H/Q292R/D416A
N227H/Q292R/D416A
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
Q292R
is not able to transform 3-aminophenol
R152L/F364V
low ability to hydroxylate 3-aminophenol
V257A
mutation enables the mutant to transform phenol to catechol, also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol, thus broadens the substrate range. Is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol as the wild-type
A400G
-
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R
-
H135P
-
alters the enzyme's substrate specificity; low ability to hydroxylate 3-aminophenol
-
K326I
-
lacks the ability to transform phenol to catechol as the wild-type
-
V257A
-
mutation enables the mutant to transform phenol to catechol, also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol, thus broadens the substrate range. Is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol as the wild-type
-
D38A
-
kcat/KM for 4-hydroxybenzoate is 16.8fold higher than wild-type value
D38Y
-
kcat/KM for 4-hydroxybenzoate is 11.8fold higher than wild-type value
D38Y/T42R
-
kcat/KM for 4-hydroxybenzoate is 32fold higher than wild-type value
T42R
-
kcat/KM for 4-hydroxybenzoate is 7.2fold higher than wild-type value
K297M
N300D
P293S
-
mutation decreases the stability of the folded mutant protein compared to the wild-type PHBH
R220Q
-
1% of wild-type activity, lower affinity to 4-hydroxybenzoate than wild-type
S212A
-
the turnover of the substrate 2,4-dihydroxybenzoate is 1.5-fold faster than the rate observed with the wild-type
Y201F
Y385F
Y385F/T294A
-
the mutant displays much higher activity toward 3,4-dihydroxybenzoic acid than the wild type enzyme
H162D
-
no reliable turnover rate due to impaired NADPH binding
H162K
-
less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH
H162N
-
no reliable turnover rate due to impaired NADPH binding
H162R
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
H162S
-
no reliable turnover rate due to impaired NADPH binding
H162T
-
no reliable turnover rate due to impaired NADPH binding
H162Y
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
R269D
-
no reliable turnover rate due to impaired NADPH binding
R269K
-
rather efficient enzyme with similar catalytic properties as wild-type enzyme
R269N
-
no reliable turnover rate due to impaired NADPH binding
R269S
-
less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH
R269T
-
no reliable turnover rate due to impaired NADPH binding
R269Y
-
no reliable turnover rate due to impaired NADPH binding
R42K
-
low activity results from impaired binding of NADPH
R42S
-
low activity results from impaired binding of NADPH
Y222A
Y222V