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2,3-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
2,4-dihydroxybenzoate + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
2,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
2-chloro-4-hydroxybenzoate + NADH + O2
?
2-fluoro-4-hydroxybenzoate + NADH + O2
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
3,4-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
3,4-dihydroxybenzoic acid + NADPH + H+ + O2
gallic acid + NADP+ + H2O
-
weak activity
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
3-bromo-4-hydroxybenzoate + NADPH + O2
?
-
3.2% of the activity with 4-hydroxybenzoate
-
-
?
3-Chloro-4-hydroxybenzoate + NADPH + O2
?
-
6.5% of the activity with 4-hydroxybenzoate
-
-
?
3-chlorophenol + NADPH + O2
? + NADP+ + H2O
-
-
-
?
3-Fluoro-4-hydroxybenzoate + NADPH + O2
?
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
3-hydroxyanthranilate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-aminobenzoate + NADPH + O2
?
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
4-chlorophenol + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-chlororesorcinol + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
4-hydroxybenzoate + NADPH + ferricyanide
protocatechuate + NADP+ + ferrocyanide
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
4-hydroxybenzoate + NADPH + O2
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
4-mercaptobenzoate + NADPH + O2
4,4'-dithiobisbenzoate + ?
4-nitrophenol + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-toluate + NADPH + O2
?
-
0.29% of the activity with 4-hydroxybenzoate
-
-
?
benzene sulfonate + NADPH + O2
?
-
0.34% of the activity with 4-hydroxybenzoate
-
-
?
hydroquinone + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
?
m-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
p-hydroxybenzoate + NADPH + O2
? + NADP+ + H2O
is transformed to a lesser extent than m-hydroxybenzoate
-
-
?
additional information
?
-
2,3-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2,3-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
3.1% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
about 1% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
1.5% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
slow reaction, formation of at least 3 intermediates, a spectral intermediate that is believed to be an oxygenated form of the enzyme-bound flavin prosthetic group
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
8% of the activity with 4-hydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + NADPH + O2
2,3,4-trihydroxybenzoate + 2,4,5-trihydroxybenzoate + NADP+ + H2O
-
8% of the activity with 4-hydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
2-chloro-4-hydroxybenzoate + NADH + O2
?
-
40% of the activity with 4-hydroxybenzoate
-
-
?
2-chloro-4-hydroxybenzoate + NADH + O2
?
-
40% of the activity with 4-hydroxybenzoate
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
?
-
50% of the activity with 4-hydroxybenzoate
-
-
?
2-fluoro-4-hydroxybenzoate + NADH + O2
?
-
50% of the activity with 4-hydroxybenzoate
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
activity of enzyme mutants DA015 and DA016, no activity with the wild-type enzyme
-
-
?
3,4-dihydroxybenzoate + NADPH + H+ + O2
gallic acid + NADP+ + H2O
good substrate of enzyme mutants Y385F and L199V/Y385F, poor activity with the wild-type enzyme PobA
-
-
?
3,4-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
3,4-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
the enzyme prefers NADPH to NADH
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
protocatechuate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
ir
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
ir
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
ir
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme is expressed at basal level, presence of 4-hydroxybenzoate enhances activity
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
degradation of 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
degradation of 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
inducible enzyme
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
first step in the bacterial metabolism when 4-hydroxybenzoate is used as growth substrate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme catalyzes an intermediate step in the degradation of aromatic compounds in soil microorganisms
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH. 4HBA hydroxylase can be induced by 4HBA, 4-cresol, and 4-hydroxybenzaldehyde
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
390020, 390021, 390022, 390023, 390025, 390027, 390030, 390032, 390033, 390034, 390041, 390042, 390044, 390046, 390049, 686087 -
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
at least three intermediates
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-mercaptobenzoate + NADPH + O2
4,4'-dithiobisbenzoate + ?
-
-
-
-
?
4-mercaptobenzoate + NADPH + O2
4,4'-dithiobisbenzoate + ?
-
50% of the activity with 4-hydroxybenzoate
-
?
additional information
?
-
-
the enzyme also shows low activities with 2- and 3-hydroxybenzoate as well as D-glucose
-
-
?
additional information
?
-
-
substrate binding analysis and structure, each subunit of the dimeric enzyme contains a split substrate-binding domain, overview
-
-
-
additional information
?
-
-
substrate binding analysis and structure, each subunit of the dimeric enzyme contains a split substrate-binding domain, overview
-
-
-
additional information
?
-
-
p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
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?
additional information
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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
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?
additional information
?
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no hydroxylase activity is observed with 3-hydroxybenzoate, resorcinol, 3-nitrophenol, benzoate, 2,4-dihydroxybenzoate, 4-chlorobenzoate, 4-aminobenzoate, 4-aminophenol, 4-nitrophenol, and 4-dinitrobenzene
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?
additional information
?
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a Tyr seems to be involved in substrate activation
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?
additional information
?
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mutant enzyme Y385F hydroxylates 3,4-dihydroxybenzoate to form gallic acid
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?
additional information
?
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3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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additional information
?
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3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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-
additional information
?
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3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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-
additional information
?
-
3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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-
-
additional information
?
-
3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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-
additional information
?
-
3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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additional information
?
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3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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-
additional information
?
-
3,4-dihydroxybenzoate is no substrate for hydroxylation by the enzyme. But PHBH can bind to other benzoate derivatives in addition to 4-hydroxybenzoate
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additional information
?
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mechanism of oxygen insertion
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?
additional information
?
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Arg42 is involved in binding of the 2'-phosphoadenosine moiety of NADPH
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?
additional information
?
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under anaerobic conditions, the enzyme can catalyze a reduction of FAD by NADPH provided that 4-hydroxybenzoate is present
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?
additional information
?
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development of a colorimetric coupled assay: the glucose-6-phosphate dehydrogenase (G6PD) catalyzes the specific dehydrogenation of glucose-6-phosphate (G-6-P) by consuming the oxidized form of beta-nicotinamide adenine dinucleotide phosphate (NADP+) to generate NADPH. And the formed NADPH initiates the irreversible hydroxylation of p-hydroxybenzoate by p-hydroxybenzoate hydroxylase (PHBH) to generate 3,4-dihydroxybenzoate (DHB), which results in the subsequent in situ generation of a photoresponsive nanozyme of DHB coordinated SrTiO3 (SrTiO3/DHB) nanosheets. The photoresponsive nanozyme has intriguing interfacial charge transfer (ICT) characteristics and thus realizes the efficiently catalytic oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) under light irradiation for signal readout. Optimization and evaluation of the ultrasensitive colorimetric bioassay for versatile targets, overview
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additional information
?
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development of a colorimetric coupled assay: the glucose-6-phosphate dehydrogenase (G6PD) catalyzes the specific dehydrogenation of glucose-6-phosphate (G-6-P) by consuming the oxidized form of beta-nicotinamide adenine dinucleotide phosphate (NADP+) to generate NADPH. And the formed NADPH initiates the irreversible hydroxylation of p-hydroxybenzoate by p-hydroxybenzoate hydroxylase (PHBH) to generate 3,4-dihydroxybenzoate (DHB), which results in the subsequent in situ generation of a photoresponsive nanozyme of DHB coordinated SrTiO3 (SrTiO3/DHB) nanosheets. The photoresponsive nanozyme has intriguing interfacial charge transfer (ICT) characteristics and thus realizes the efficiently catalytic oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) under light irradiation for signal readout. Optimization and evaluation of the ultrasensitive colorimetric bioassay for versatile targets, overview
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additional information
?
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comparisons of substrate binding structure analysis mechanism
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additional information
?
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comparisons of substrate binding structure analysis mechanism
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additional information
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comparisons of substrate binding structure analysis mechanism
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additional information
?
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the enzyme also shows low activities with 2- and 3-hydroxybenzoate as well as D-glucose
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?
additional information
?
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no activity with 2-hydroxybenzoate and 3-hydroxybenzoate
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?
additional information
?
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no activity with 2-hydroxybenzoate and 3-hydroxybenzoate
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?
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4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
4-hydroxybenzoate + NADPH + O2
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
additional information
?
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p-hydroxybenzoate induces the expression of p-hydroxybenzoate hydroxylase
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?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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ir
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
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ir
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
3,4-dihydroxybenzoate + NADP+ + H2O
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-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
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-
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?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
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?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
4-hydroxybenzoate degradation proceeds via hdroxylation to 3,4-dihydroxybenzoic acid and then conversion to catechol, which is cleaved to cis,cis-muconic acid through ortho-catechol cleavage
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?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
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-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
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-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
ir
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
-
-
-
-
?
4-hydroxybenzoate + NADPH + H+ + O2
protocatechuate + NADP+ + H2O
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-
-
-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
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?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
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?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
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?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme is expressed at basal level, presence of 4-hydroxybenzoate enhances activity
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?
4-hydroxybenzoate + NADPH + O2
?
-
degradation of 4-hydroxybenzoate
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?
4-hydroxybenzoate + NADPH + O2
?
-
degradation of 4-hydroxybenzoate
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?
4-hydroxybenzoate + NADPH + O2
?
-
inducible enzyme
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?
4-hydroxybenzoate + NADPH + O2
?
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first step in the bacterial metabolism when 4-hydroxybenzoate is used as growth substrate
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?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme catalyzes an intermediate step in the degradation of aromatic compounds in soil microorganisms
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-
?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
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?
4-hydroxybenzoate + NADPH + O2
?
-
enzyme of the toluene-4-monooxygenase catabolic pathway
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-
?
4-hydroxybenzoate + NADPH + O2
?
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
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-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
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-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
the enzyme prefers NADPH to NADH. 4HBA hydroxylase can be induced by 4HBA, 4-cresol, and 4-hydroxybenzaldehyde
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-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
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-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
-
enzyme is induced by 4-hydroxybenzoate
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-
?
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evolution
amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
evolution
-
evolutionary relationship between the NAD(P)H-dependent FAD-containing 4-hydroxybenzoate hydroxylases and phylogenetic analysis of group A FPMOs, overview
evolution
-
phylogenetic analysis shows that FAD-dependent 4-hydroxybenzoate hydroxylases reside in distinct clades of the group A flavoprotein monooxygenase (FPMO) family, indicating their separate divergence from a common ancestor. Protein homology modeling reveals that the fungal 4-hydroxybenzoate 3-hydroxylase PhhA is structurally related to phenol hydroxylase (PHHY) and 3-hydroxybenzoate 4-hydroxylase (3HB4H). 4-Hydroxybenzoate 1-hydroxylase (4HB1H) from yeast catalyzes an oxidative decarboxylation reaction and is structurally similar to 3-hydroxybenzoate 6-hydroxylase (3HB6H), salicylate hydroxylase (SALH) and 6-hydroxynicotinate 3-monooxygenase (6HNMO). Group A FPMOs are involved in the aerobic microbial catabolism of 4-hydroxybenzoate. Phylogenetic analysis and structure comparisons, detailed overview
evolution
the PobA enzyme structure is highly conserved across various organisms. Active-site residues Tyr201, Ser212, Arg214, Tyr222 and Pro293 interact with the carboxyl and phenolic components of 4-HB and are essential for its oxidative catalysis
evolution
-
the PobA enzyme structure is highly conserved across various organisms. Active-site residues Tyr201, Ser212, Arg214, Tyr222 and Pro293 interact with the carboxyl and phenolic components of 4-HB and are essential for its oxidative catalysis
-
evolution
-
evolutionary relationship between the NAD(P)H-dependent FAD-containing 4-hydroxybenzoate hydroxylases and phylogenetic analysis of group A FPMOs, overview
-
evolution
-
phylogenetic analysis shows that FAD-dependent 4-hydroxybenzoate hydroxylases reside in distinct clades of the group A flavoprotein monooxygenase (FPMO) family, indicating their separate divergence from a common ancestor. Protein homology modeling reveals that the fungal 4-hydroxybenzoate 3-hydroxylase PhhA is structurally related to phenol hydroxylase (PHHY) and 3-hydroxybenzoate 4-hydroxylase (3HB4H). 4-Hydroxybenzoate 1-hydroxylase (4HB1H) from yeast catalyzes an oxidative decarboxylation reaction and is structurally similar to 3-hydroxybenzoate 6-hydroxylase (3HB6H), salicylate hydroxylase (SALH) and 6-hydroxynicotinate 3-monooxygenase (6HNMO). Group A FPMOs are involved in the aerobic microbial catabolism of 4-hydroxybenzoate. Phylogenetic analysis and structure comparisons, detailed overview
-
malfunction
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
malfunction
-
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
metabolism
-
enzyme PHBH is almost exclusively found in prokaryotes, where its induction, usually as a consequence of lignin degradation, results in the regioselective formation of protocatechuate, one of the central intermediates in the global carbon cycle
metabolism
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
metabolism
-
enzyme PHBH is almost exclusively found in prokaryotes, where its induction, usually as a consequence of lignin degradation, results in the regioselective formation of protocatechuate, one of the central intermediates in the global carbon cycle
-
metabolism
-
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis
-
physiological function
-
the pobA gene encoding the 4-hydroxybenzoate 3-monooxygenase is expressed during growth on hydroxybenzoic acids and glucose
physiological function
-
4-hydroxybenzoate (4-HB) is a common intermediate in lignin degradation. It is one of the aromatic acids that arise from the Calpha-Cbeta cleavage of lignin components. In aerobic bacteria, 4-HB usually is converted to the ring-fission substrate 3,4-dihydroxybenzoate (protocatechuate, PCA). This reaction is catalyzed by the NAD(P)H-dependent flavoprotein monooxygenase (FPMO) 4-hydroxybenzoate 3-hydroxylase (PHBH)
physiological function
PobA is a flavin-dependent monooxygenase that utilizes one O atom from O2 to hydroxylate 4-hydroxybenzoate, while reducing the other O atom to water
physiological function
-
PobA is a flavin-dependent monooxygenase that utilizes one O atom from O2 to hydroxylate 4-hydroxybenzoate, while reducing the other O atom to water
-
physiological function
-
4-hydroxybenzoate (4-HB) is a common intermediate in lignin degradation. It is one of the aromatic acids that arise from the Calpha-Cbeta cleavage of lignin components. In aerobic bacteria, 4-HB usually is converted to the ring-fission substrate 3,4-dihydroxybenzoate (protocatechuate, PCA). This reaction is catalyzed by the NAD(P)H-dependent flavoprotein monooxygenase (FPMO) 4-hydroxybenzoate 3-hydroxylase (PHBH)
-
additional information
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
additional information
-
enzyme protein homology modeling of An_PhhA using the structure file of Tc_PHHY (PDB ID 1pn0) as template, overview. Hydroxylase enzymes structure comparisons, overview
additional information
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
additional information
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
additional information
-
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
additional information
-
sequence comparisons, three-dimensional enzyme structure analysis, and structure comparisons with 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum, overview. Despite having only 14% similarity in their primary sequences, pairwise structure alignments of PobA from Pseudomonas putida with HbpA from Pseudomonas nitroreducens and MHPCO from Mesorhizobium japonicum reveal local similarities between these structures. Key residues in the FAD-binding and substrate-binding sites of PobA are highly conserved spatially across the proteins from all three species. The PobA from Pseudomonas putida is structurally very similar to PobA from Pseudomonas fluorescens and from Pseudomonas aeruginosa. Key secondary-structure elements important for catalysis, such as the betaalphabeta fold, beta-sheet wall and alpha12 helix, are conserved across this expanded class of oxygenases
-
additional information
-
enzyme protein homology modeling of An_PhhA using the structure file of Tc_PHHY (PDB ID 1pn0) as template, overview. Hydroxylase enzymes structure comparisons, overview
-
additional information
-
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016
-
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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/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
-
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
L199A
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
L199A/Y385F
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
L199D
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
L199D/Y385F
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
L199G
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
L199G/Y385A
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
L199G/Y385F
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
L199H
site-directed mutagenesis, the mutant enzyme is almost inactive with 3,4-dihydroxybenzoate
L199K
site-directed mutagenesis, the mutant enzyme is almost inactive with 3,4-dihydroxybenzoate
L199R/T294C/Y385M
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
L199S
site-directed mutagenesis, the mutant enzyme is almost inactive with 3,4-dihydroxybenzoate
L199V
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
L199V/Y385A
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
L199V/Y385F
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation, and the L199V mutation in addition to the Y385F mutation allows the OH moiety in the peroxide group of C-(4a)-flavin hydroperoxide to come into the proximity of the C5 atom of 3,4-DOHB
L199V/Y385V
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is increased compared to the wild-type enzyme
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
V47I/L199N/T294A/Y385I
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
Y385A
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
Y385F/T294A
-
the mutant displays much higher activity toward 3,4-dihydroxybenzoic acid than the wild type enzyme
Y385S
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
Y385T
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly reduced compared to the wild-type enzyme
Y385V
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly reduced compared to the wild-type enzyme
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
L199A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is unaltered compared to the wild-type enzyme
-
L199D
-
site-directed mutagenesis, the mutant enzyme is inactive with 3,4-dihydroxybenzoate
-
L199R/T294C/Y385M
-
site-directed and random mutagenesis, mutant DA015, in the DA015 model, L199R supports Y201 and forms a new contact to the ligand 3-hydroxyl. Y385M makes space, no substitution occurs at V47, which maintains close hydrophobic packing against L199R, and T294C loosens the helix for increased flexibility and improved backbone hydrogen bonding to the 4-hydroxyl. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
V47I/L199N/T294A/Y385I
-
site-directed and random mutagenesis, mutant DA016, in the DA016 model, L199N forms interactions stabilizing S212 and to the ligand 3-hydroxyl. Y385I creates space, V47I braces L199N to minimize side-chain mobility, and T294A allows P293 to move closer to 3,4-DHBA. The mutation orients 3,4-DHBA such that the 5-carbon is optimally exposed to FAD for hydroxylation
-
Y385A
-
site-directed mutagenesis, the activity of the mutant with 3,4-dihydroxybenzoate is slightly increased compared to the wild-type enzyme
-
Y385F
-
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
-
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
H135P
alters the enzyme's substrate specificity
H135P
low ability to hydroxylate 3-aminophenol
H135P
-
alters the enzyme's substrate specificity
-
H135P
-
low ability to hydroxylate 3-aminophenol
-
E49Q
-
mutant has lost the ability in the oxidized state to rapidly exchange the product, i.e., 3,4-dihydroxybenzoate, for the substrate, p-hydroxybenzoate
E49Q
-
mutation enhances the positive charge in the active site of PHBH, rate of hydroxylation is above that of wild-type, the rate of release of product is slower than the rate of return of the flavin to the oxidized state
E49Q
-
investigation of oxygen half-reaction
H72N
-
rate of turnover is only about 8% of wild-type enzyme at all pH values
H72N
disruption of proton-transfer network, kinetic analysis
H72N
-
investigation of oxygen half-reaction
K297M
-
decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme. Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme
K297M
-
mutation decreases the positive charge in the active site of PHBH but does not interfere with with the H-bond network, 25fold decrease in the rate of hydroxylation compared to wild-type enzyme
K297M
-
investigation of oxygen half-reaction
N300D
-
mutation has profound effect on enzyme structure. The side chain of Asp300 moves away from the flavin, disrupting the interaction of the carboxamide group with the flavin O(2) atom, and the alpha-helix H10 that begins at residue 297 is displaced, altering its dipole interaction with the flavin ring
N300D
-
330fold reduced reduction rate of the flavin of the enzyme by NADPH compared to wild-type enzyme, redox potential of the flavin is 20-40mV lower than that of the wild-type enzyme. The mutation interferes with the orientation of pyridine nucleotide and flavin during reduction, stabilizes flavin C(4a) intermediates, prevents substrate ionization, and alters the rates and strengths of ligand binding
N300D
-
decreased positive charge in active site, about 35fold slower hydroxylation rate than the wild-type enzyme, Substitution of 8-Cl-FAD in the mutant gives about 1.8fold increase in hydroxylation rate compared to the wild-type enzyme
Y201F
-
crystals differ from the wild-type enzyme at two surface positions, 228 and 249
Y201F
-
less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 10fold, when the mutant enzyme-4-hydroxybenzoate complex reacts with oxygen, a long-lived flavin-C(4a)-hydroperoxide is observed, which slowly eliminates H2O2 with very little hydroxylation
Y201F
-
investigation of oxygen half-reaction
Y385F
-
crystals differ from the wild-type enzyme at two surface positions, 228 and 249
Y385F
-
mutant enzyme with a disrupted hydrogen-bonding network, substitution of 8-Cl-FAD in the mutant gives about 1.5fold increase in hydroxylation rate compared to the wild-type enzyme
Y385F
-
less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 100fold, the mutant enzyme reacts with oxygen to form 25% oxidized enzyme and 75% flavin hydroperoxide, which successfully hydroxylates the substrate. The mutant also hydroxylates the product 3,4-dihydroxybenzoate to form gallic acid
Y385F
-
in the oxygen half-reaction, the rate of hydroxylation is 25fold slower than that for the wild-type enzyme at pH 6.5, in contrast to wild-type enzyme there is some formation of H2O2 in the reaction
Y385F
-
investigation of oxygen half-reaction
Y385F
-
the mutant displays higher activity toward 3,4-dihydroxybenzoic acid than the wild type enzyme
Y385F
site-directed mutagenesis, the Y385F mutation facilitates the deprotonation of the 4-hydroxy group of 3,4-dihydroxybenzoate, which is necessary for initiating hydroxylation
Y222A
-
inactive
Y222A
-
mutation makes the lifetime distribution of FAD in the enzyme simpler by removing the ultrafast 10-15 ps lifetime component
Y222V
-
inactive
Y222V
-
mutation makes the lifetime distribution of FAD in the enzyme simpler by removing the ultrafast 10-15 ps lifetime component
additional information
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
additional information
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
additional information
-
for directed evolution of an NADPH-dependent monooxygenase Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to engineer high activity for a non-native substrate, 3,4-dihydroxybenzoic acid (3,4-DHBA) which is the precursor of a natural product antioxidant, gallic acid (GA), an aerobic, growth-based selection platform is founded on NADP(H) redox balance restoration in Escherichia coli strain MX203. Application in the high-throughput evolution of the oxygenase. A single round of selection followed by a facile growth assay enables Pseudomonas aeruginosa 4-hydroxybenzoate hydroxylase (PobA) to efficiently hydroxylate both 4-hydroxybenzoic acid (4-HBA) and 3,4-dihydroxybenzoic acid (3,4-DHBA), two consecutive steps in gallic acid biosynthesis. Reorganization of active site hydrogen bond network. Mutant variants with roughly 8fold improved apparent catalytic efficiency (kcat/KM) for 3,4-DHBA, compared to the wild type, are obtained. Engineered Escherichia coli strain (MX203) has a growth deficiency linked to NADPH/NADP+ imbalance. The perturbed redox state results from deletion of central metabolism genes, glucose-6-phosphate isomerase gene pgi and phosphogluconate dehydratase gene edd, a critical rebalancing tool, soluble pyridine nucleotide transhydrogenase gene udhA, and a significant sink for reduced nicotinamide cofactors, NAD(P)H:quinone oxidoreductase gene qor. These disruptions cause MX203 to exhibit poor growth in glucose minimal media. Possibility of the universal application of this selection platform in engineering NADPH-dependent oxidoreductases. Mutants modeling and docking of 3,4-DHBA, overview
-
additional information
-
molecular mechanism underlying this higher catalytic activity of some enzyme mutants, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview
-
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