Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-naphthoic acid + AH2 + O2
5-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
-
-
?
2-naphthoic acid + AH2 + O2
7-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
-
-
?
2-naphthoic acid + AH2 + O2
8-hydroxy-2-naphthoic acid + A + H2O
only the wild-type enzyme hydroxylates 2-naphthoic acid at the C-7 and C-8 positions, whereas all of the active F185 mutants exhibit a preference for C-5 hydroxylation
-
-
?
3,4-dimethoxybenzoate + NADH + O2
4-hydroxy-3-methoxybenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
3-chlorobenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
3-nitro-4-methoxybenzoate + NADH + O2
3-nitro-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
3-nitro-4-methoxybenzoate + NADPH + O2
3-nitro-4-hydroxybenzoate + NADP+ + H2O + formaldehyde
-
-
-
-
r
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
4-aminobenzoate + NADH + O2
4-amino-3-hydroxybenzoate + NAD+ + H2O
-
-
-
-
?
4-chlorobenzaldehyde + NADH + O2
4-chlorobenzoate + NAD+ + H2O
-
-
-
-
?
4-chlorobenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-coumaric acid + AH2 + O2
caffeic acid + A + H2O
the F185L mutant exhibits 5.5times higher hydroxylation activity for 4-coumaric acid than the wild-type enzyme, good substrate of enzyme mutant F185L, low activity with enzyme mutant sF185V, F185I, F185G, and F185A, moderate activity with the wild-type enzyme and mutants F185Y, F185W, F185S, and F185T with 4-coumaric acid
-
-
?
4-ethoxybenzoate + NADH + O2
4-hydroxybenzoate + acetaldehyde + NAD+ + H2O
-
-
-
-
?
4-ethylbenzoate + AH2 + O2
4-(1-hydroxyethyl)-benzoate + 4-vinylbenzoate + A + H2O
-
a C-C bond dehydrogenation of an unbranched alkyl group, computational docking of 4-ethylbenzoate into the active site suggests that the substrate carboxylate oxygens interact with Ser97 and Ser247, and the beta-methyl group is located over the heme iron by Phe185, this binding orientation is consistent with the observed product profile of exclusive attack at the para substituent, overview
-
-
?
4-ethylbenzoate + AH2 + O2
?
4-ethylbenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-Hydroxy-3-methoxybenzoate + NADH + O2
?
-
vanillate, partial uncoupler
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
4-isopropylbenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
4-methoxybenzaldehyde + AH2 + O2
4-hydroxybenzaldehyde + formaldehyde + A + H2O
4-methoxybenzamide + AH2 + O2
4-hydroxybenzamide + formaldehyde + A + H2O
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
4-methoxybenzoate + NADH + O2
4-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
4-methoxybenzoate + NADPH + O2
4-hydroxybenzoate + NADP+ + H2O + formaldehyde
-
-
-
-
r
4-methoxybenzoate + reduced ferredoxin + O2
4-hydroxybenzoate + formaldehyde + ferredoxin + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
4-methoxybenzoate + reduced putidaredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized putidaredoxin + H2O
-
very low activity with putidaredoxin
-
-
?
4-methoxybenzoic acid + NADH + O2
4-hydroxybenzoate + formaldehyde + NAD+ + H2O
-
-
-
-
?
4-methoxyphenylacetate + AH2 + O2
4-hydroxyphenylacetate + formaldehyde + A + H2O
low activity
-
-
?
4-methoxyphenylboronic acid + AH2 + O2
4-hydroxyphenylboronic acid + formaldehyde + A + H2O
low activity
-
-
?
4-methylbenzoate + AH2 + O2
?
low activity
-
-
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
4-methylbenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-methylmercaptobenzoate + NADH + O2
?
-
-
-
-
?
4-methylphenylacetate + AH2 + O2
?
low activity
-
-
?
4-methylsalicylic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-t-butylbenzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
4-trifluoromethylbenzoate + NADH + O2
?
-
-
-
-
?
4-vinylbenzoate + NADH + O2
4-glycylbenzoate + NAD+ + H2O
-
external dioxygenase reaction by substrate induced modulation
-
-
?
alkylbenzoates
?
-
-
-
-
?
benzoate + NADH + O2
?
-
-
-
-
?
benzoic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
cinnamic acid + AH2 + O2
? + A + H2O
good substrate of enzyme mutant F185L, and F185G, low activity with enzyme mutants F185V, F185I, F185A F185S, and F185T, no activity with the wild-type enzyme and mutants F185Y and F185W with cinnamic acid
-
-
?
L-perillic acid + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
N,N'-dimethyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
N-methyl-4-aminobenzoate + NADH + O2
4-aminobenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
additional information
?
-
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
-
piperonylate
protocatechuate
?
3,4-methylenedioxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde
-
piperonylate
protocatechuate
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
partial uncoupler
in the uncoupled part of the reaction, 3-hydroxybenzoate is not hydroxylated and H2O2 is a product, too
?
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
partial uncoupler
-
?
3-methoxybenzoate + NADH + O2
3-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
partial uncoupler
in the uncoupled part of the reaction 3-methoxybenzoate is not hydroxylated, and H2O2 is a product, too
?
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
-
-
-
?
3-phenyl-4-methoxybenzoate + NADH + O2
3-phenyl-4-hydroxybenzoate + NAD+ + H2O + formaldehyde
-
partial uncoupler
in the uncoupled part of the reaction 3-phenyl-4-methoxybenzoate is not hydroxylated and H2O2 is also a product of the reaction
?
4-ethylbenzoate + AH2 + O2
?
computational docking study
-
-
?
4-ethylbenzoate + AH2 + O2
?
computational docking study
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
4-hydroxybenzoate + NADH + O2
3,4-dihydroxybenzoate + NAD+ + H2O
-
-
ring hydroxylation
?
4-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
low activity
-
-
?
4-methoxyacetophenone + AH2 + O2
4-hydroxyacetophenone + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzaldehyde + AH2 + O2
4-hydroxybenzaldehyde + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzaldehyde + AH2 + O2
4-hydroxybenzaldehyde + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzamide + AH2 + O2
4-hydroxybenzamide + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzamide + AH2 + O2
4-hydroxybenzamide + formaldehyde + A + H2O
low activity
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
?
4-methoxybenzoate + AH2 + O2
4-hydroxybenzoate + formaldehyde + A + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
-
-
-
?
4-methoxybenzoate + reduced palustrisredoxin + O2
4-hydroxybenzoate + formaldehyde + oxidized palustrisredoxin + H2O
-
-
-
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
-
-
-
-
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
-
p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
-
p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
4-methylbenzoate + NADH + O2
4-carboxybenzylalcohol + NAD+ + H2O
-
p-toluate, partial uncoupler
in the uncoupled part of the reaction, p-toluate is not hydroxylated and H2O2 is a product, too
?
veratrate + AH2 + O2
?
-
-
-
?
veratrate + AH2 + O2
?
-
-
-
?
additional information
?
-
-
substrate binding induces a large type I spin-state shift, highest shifts are observed with benzoic acids and benzaldehydes containing a substitutent at the 4-position. Palustrisredoxin A is the natural electron transfer cofactor protein
-
-
?
additional information
?
-
-
CYP199A2 shows a strong preference for para-substituted benzoate over identically substituted ortho- and meta- benzoates, and para-substituted benzenes, benzyl alcohols and benzaldehydes, a cytochrome P450 enzyme, the substrate binding pocket is hydrophobic, with Ser97 and Ser247 being the only polar residues, substrate binding and substrate channeling mechanism and structure, overview
-
-
?
additional information
?
-
-
CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation
-
-
?
additional information
?
-
-
CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
-
-
?
additional information
?
-
-
the enzyme performs regioselective oxidation of indole- and quinolinecarboxylic acids, it oxidizes 2-naphthoic acid and 4-ethylbenzoic acid, substrate specificity and regioselectivity of CYP199A2, overview. CYP199A2 does not exhibit any activity towards indole and indole-3-carboxylic acid, whereas this enzyme oxidizes indole-2-carboxylic acid, indole-5-carboxylic acid, and indole-6-carboxylic acid. Indole-2-carboxylic acid is converted to 5- and 6-hydroxyindole-2-carboxylic acids at a ratio of 59:41. In contrast, the indole-6-carboxylic acid oxidation generates only one product, 2-indolinone-6-carboxylic acid. The oxidation product of quinoline-6-carboxylic acid is 3-hydroxyquinoline-6-carboxylic acid
-
-
?
additional information
?
-
CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
-
CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
substrate specficities of wild-type and F185 mutants, overview. The enzyme exhibits oxidation activity for aromatic carboxylic acids, including 2-naphthoic acid, 4-ethylbenzoic acid, and indole-and quinolinecarboxylic acids. No activity of the wild-type enzyme with cinnamic acid
-
-
?
additional information
?
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
-
-
?
additional information
?
-
-
CYP199A2 is a heme monooxygenase that catalyses the oxidation of para-substituted benzoic acids, the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation
-
-
?
additional information
?
-
-
CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin, Pux, and a flavoprotein palustrisredoxin reductase, PuR. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system, overview
-
-
?
additional information
?
-
CYP199A2 oxidizes para-substituted benzoic acids with almost total NADH-to-product conversion with the highest activity being observed in the oxidative demethylation of 4-methoxybenzoate. Exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
exclusive attack by CYP199A2 and CYP199A4 at the methoxy methyl group, leading to demethylation to form 4-hydroxybenzoate as the only product
-
-
?
additional information
?
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
-
-
?
additional information
?
-
-
no activity with 4-methoxybenzyl alcohol, 4-methylbenzenesulfonic acid, 4-methylbenzenesulfinic acid, 4-methoxynitrobenzene, 4-methoxyphenol, and 4-methoxybenzoic acid methyl ester
-
-
?
additional information
additional information
-
-
-
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates that are not oxygenized while NADH-oxidation and O2-consumption are catalyzed, such as: benzoate, 3-chlorobenzoate, 4-chlorobenzoate, 2-hydroxybenzoate, 4-bromobenzoate, 2-aminobenzoate, 3-aminobenzoate, 4-trifluoromethylbenzoate, 4-tert-butylbenzoate
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
additional information
additional information
-
-
overview: substrates being absolutely planar aromatic rings with a directly bound dissociable carboxy group are oxygenated under stoichiometric consumption of O2 and NADH
uncoupling substrates are not oxygenized, NAD+ and H2O2 being the only products of the reaction
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.002
-
4-hyroxybenzoate, reductase
0.004
-
4-hydroxybenzoate, monooxygenase
0.008
-
3-methoxybenzoate, 4-methoxybenzoate, cell-free extract
0.009
-
N,N-dimethyl-4-aminobenzoate
0.018
-
superoxide anion instead of substrate, putidamonooxin
0.021
-
4-hydroxy-3-methoxybenzoate
0.023
-
3-hydroxybenzoate, reconstituted enzyme
0.024
-
4-ethoxybenzoate, N-methyl-4-aminobenzoate
0.025
-
3,4-dimethoxybenzoate
0.04
-
4-methoxybenzoate, cell-free extract
0.055
-
4-hyxdroxybenzoate
0.077
-
4-hydroxybenzoate, reconstituted enzyme
0.178
-
N-methyl-4-aminobenzoate
0.192
-
3-nitro-4-methoxybenzoate, putidamonooxin
0.27
-
4-methoxybenzoate, putidamonooxin
0.314
-
4-ethoxybenzoate, piperonylate
0.345
-
3,4-dimethoxybenzoate
194.5
-
3-phenyl-4-[2H3]-methoxybenzoate, product formation, reaction in H2O
207.8
-
4-trifluoromethylbenzoate, oxygen uptake, reaction in D2O
21.96
-
4-methoxybenzoate
239.8
-
3-phenyl-4-[2H3]-methoxybenzoate, product formation, reaction in D2O
265.6
-
benzoate, oxygen uptake, reaction in D2O
295.1
-
benzoate, oxygen uptake, reaction in H2O
303.9
-
3-phenyl-4-[1H3]-methoxybenzoate, product formation, reaction in H2O
305.2
-
4-methylbenzoate, NADH oxidation, reaction in H2O
315.5
-
4-trifluoromethylbenzoate, NADH oxidation, reaction in D2O
317.2
-
4-methylbenzoate, NADH oxidation, reaction in D2O
317.4
-
3-phenyl-4-[1H3]-methoxybenzoate, product formation, reaction in D2O
326.7
-
3-phenyl-4-[1H3]-methoxybenzoate, oxygen uptake, reaction in H2O
329.2
-
3-phenyl-4-[1H3]-methoxybenzoate, oxygen uptake, reaction in D2O
339.1
-
benzoate, NADH oxidation, reaction in D2O
340.2
-
3-phenyl-4-[2H3]-methoxybenzoate, NADH oxidation, reaction in H2O
345
-
4-trifluoromethylbenzoate, oxygen uptake, reaction in H2O
345.6
-
benzoate, NADH oxidation, reaction in H2O
353.5
-
3-phenyl-4-[2H3]-methoxybenzoate, NADH oxidation, reaction in D2O
360.4
-
3-phenyl-4-[1H3]-methoxybenzoate, NADH oxidation, reaction in H2O
367
-
4-methylbenzoate, oxygen uptake, reaction in H2O
368
-
4-methylbenzoate, oxygen uptake, reaction in D2O
380.2
-
3-phenyl-4-[1H3]-methoxybenzoate, NADH oxidation, reaction in D2O
391.5
-
4-methoxybenzoate, oxygen uptake, reaction in D2O
394.1
-
4-methoxybenzoate, oxygen uptake, reaction in H2O
402.6
-
3-nitro-4-methoxybenzoate, NADH oxidation, reaction in D2O
409.7
-
4-trifluoromethylbenzoate, NADH oxidation, reaction in H2O
422.1
-
3-nitro-4-methoxybenzoate, NADH oxidation, reaction in H2O
432.4
-
3-nitro-4-methoxybenzoate, oxygen uptake, reaction in H2O
432.7
-
3-nitro-4-methoxybenzoate, oxygen uptake, reaction in D2O
442.2
-
4-methoxybenzoate, NADH oxidation, reaction in D2O
445
-
4-methoxybenzoate, NADH oxidation, reaction in H2O
450.9
-
3-nitro-4-methoxybenzoate, product formation, reaction in H2O
487.3
-
3-nitro-4-methoxybenzoate, product formation, reaction in D2O
310.1
-
3-phenyl-4-[2H3]-methoxybenzoate, oxygen uptake, reaction in D2O
310.1
-
3-phenyl-4-[2H3]-methoxybenzoate, oxygen uptake, reaction in H2O
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bernhardt, F.H.; Bill, E.; Trautwein, A.X.; Twilfer, H.
4-Methoxybenzoate monooxygenase from Pseudomonas putida: isolation, biochemical properties, substrate specificity, and reaction mechanisms of the enzyme components
Methods Enzymol.
161
281-294
1988
Pseudomonas putida
brenda
Wende, P.; Pfleger, K.; Bernhardt, F.H.
Dioxygen activation by putidamonooxin: substrate-modulated reaction of activated dioxygen
Biochem. Biophys. Res. Commun.
140
527-532
1982
Pseudomonas putida
-
brenda
Twilfer, H.; Bernhardt, F.H.; Gersonde, K.
An electron-spin-resonance study on the redox-active centers of the 4-methoxybenzoate monooxygenase from Pseudomonas putida
Eur. J. Biochem.
119
595-602
1981
Pseudomonas putida
brenda
Bernhardt, F.H.; Kuthan, H.
Dioxygen activation by putidamonooxin. The oxygen species formed and released under uncoupling conditions
Eur. J. Biochem.
120
547-555
1981
Pseudomonas putida
brenda
Bernhardt, F.H.; Nastainczyk, W.; Seydewitz, U.
Kinetic studies on a 4-methoxybenzoate O-demethylase from Pseudomonas putida
Eur. J. Biochem.
72
107-115
1977
Pseudomonas putida
brenda
Bernhardt, F.H.; Heymann, E.; Traylor, P.S.
Chemical and spectral properties of putidamonooxin, the iron-containing and acid-labile-sulfur-containing monooxygenase of a 4-methoxybenzoate O-demethylase from Pseudomonas putida
Eur. J. Biochem.
92
209-223
1978
Pseudomonas putida
brenda
Bernhardt, F.H.; Pachowsky, H.; Staudinger, H.
A 4-methoxybenzoate O-demethylase from Pseudomonas putida. A new type of monooxygenase system
Eur. J. Biochem.
57
241-256
1975
Pseudomonas putida
brenda
Bernhardt, F.H.; Ruf, H.H.; Ehrig, H.
A 4-methoxybenzoate monooxygenase system from Pseudomonas putida. Circular dichroism studies on the iron--sulfur protein
FEBS Lett.
43
53-55
1974
Pseudomonas putida
brenda
Bernhardt, F.H.; Erdin, N.; Staudinger, H.; Ullrich, V.
Interactions of substrates with a purified 4-methoxybenzoate monooxygenase system (O-demethylating) from Pseudomonas putida
Eur. J. Biochem.
35
126-134
1973
Pseudomonas putida
brenda
Twilfer,H.; Sandfort, G; Bernhardt, F.H.
Substrate and solvent isotope effects on the fate of the active oxygen species in substrate-modulated reactions of putidamonooxin
Eur. J. Biochem.
267
5926-5934
2000
Pseudomonas putida
brenda
Bell, S.G.; Hoskins, N.; Xu, F.; Caprotti, D.; Rao, Z.; Wong, L.L.
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris
Biochem. Biophys. Res. Commun.
342
191-196
2006
Rhodopseudomonas palustris
brenda
Bell, S.G.; Xu, F.; Forward, I.; Bartlam, M.; Rao, Z.; Wong, L.L.
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris
J. Mol. Biol.
383
561-574
2008
Rhodopseudomonas palustris
brenda
Bell, S.G.; Xu, F.; Johnson, E.O.; Forward, I.M.; Bartlam, M.; Rao, Z.; Wong, L.L.
Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris
J. Biol. Inorg. Chem.
15
315-328
2009
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Furuya, T.; Kino, K.
Regioselective oxidation of indole- and quinolinecarboxylic acids by cytochrome P450 CYP199A2
Appl. Microbiol. Biotechnol.
85
1861-1868
2010
Rhodopseudomonas palustris
brenda
Furuya, T.; Arai, Y.; Kino, K.
Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2
Appl. Environ. Microbiol.
78
6087-6094
2012
Rhodopseudomonas palustris (Q6N8N2)
brenda
Bell, S.; Yang, W.; Tan, A.; Zhou, R.; Johnson, E.; Zhang, A.; Zhou, W.; Rao, Z.; Wong, L.
The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: Structural changes on substrate binding and the identification of an anion binding site
Dalton Trans.
41
8703-8714
2012
Rhodopseudomonas palustris (Q2IU02), Rhodopseudomonas palustris (Q6N8N2), Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009 (Q6N8N2), Rhodopseudomonas palustris HaA2 (Q2IU02)
brenda
Coleman, T.; Chao, R.R.; De Voss, J.J.; Bell, S.G.
The importance of the benzoic acid carboxylate moiety for substrate recognition by CYP199A4 from Rhodopseudomonas palustris HaA2
Biochim. Biophys. Acta
1864
667-675
2016
Rhodopseudomonas palustris (Q2IU02), Rhodopseudomonas palustris HaA2 (Q2IU02), Rhodopseudomonas palustris HaA2
brenda