Any feedback?
Information on EC 1.14.12.11 - toluene dioxygenase and Organism(s) Pseudomonas putida and UniProt Accession A5W4F2
for references in articles please use BRENDA:EC1.14.12.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.12.11 toluene dioxygenaseIUBMB Comments
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis-dihydrodiols.
Specify your search results
Word Map
- 1.14.12.11
- putida
- naphthalene
- trichloroethylene
- ethylbenzene
- chlorobenzene
- cis-dihydrodiols
- dihydrodiols
-
cis-dihydroxylation
- dot-t1e
-
ring-hydroxylating
-
cis-toluene
- indene
-
cis-diols
- pseudoalcaligenes
- 1-indanone
-
toluene-grown
- 3-methylcatechol
- synthesis
- analysis
- degradation
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
toluene dioxygenase, todc1c2ba, isptol, toluene 2,3-dioxygenase, oxygenasetol, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ISPTOL
-
oxygenase component of the toluene dioxygenase multienzyme system
oxygenase, toluene 2,3-di-
-
-
-
-
TDO
additional information
-
part of a multiple enzyme complex: reductase, ferredoxin, dioxygenase
TDO
-
-
-
-
TDO
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
toluene + NADH + H+ + O2 = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
reaction mechanism, structure-function reklationship of the enzyme organized in a multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system, overview
-
toluene + NADH + H+ + O2 = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
formation of a stable charge transfer complex between the reduced reductase and NAD+ at the end of the reductive half-reaction, which is substantially less reactive toward dioxygen than the reduced reductase in the absence of NAD+. The nicotinamide ring and the protein matrix shield the reactive C4a position of the isoalloxazine ring and force the tricycle into an atypical planar conformation, both factors disfavoring the reaction of the reduced flavin with dioxygen. A rapid electron transfer from the charge transfer complex to electron acceptors further reduces the risk of unwanted side reactions, there is a short distance between the electron-donating and -accepting cofactors. Attraction between the two proteins is likely mediated by opposite charges at one large patch of the complex interface
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
oxidation
-
-
-
-
reduction
-
-
-
-
redox reaction
-
-
-
-
redox reaction
-
the toluene 2,3-dioxygenase consists of three components: a reductase transfers electrons from NADH to a Rieske [2Fe-2S] ferredoxin which shuttles electrons to a dioxygenase which catalyzes the formation of (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
toluene,NADH:oxygen oxidoreductase (1,2-hydroxylating)
A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis-dihydrodiols.
CAS REGISTRY NUMBER
COMMENTARY
120038-36-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
toluene + NADH + H+ + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
(+)-(S)-indan-1-ol + O2 + NADH
(-)-(R)-indan-1-ol + indan-1-one + (+)-trans-(1S,3S)-1,3-dihydroxyindane + (-)-(3R)-3-hydroxyindan-1-one + NAD+
-
biotransformation with intact cells
-
?
(+/-)-trans-2-phenyl-1-cyclohexanol + NADH + O2
3-(2-hydroxycyclohexanyl)-3,5-cyclohexadiene-1,2-diol + ?
-
-
-
?
(-)-(R)-indan-1-ol + NADH + O2
trans-(1R,3R)-1,3-dihydroxyindane + (-)-(1R,4R,5S)-1,4,5-trihydroxy-4,5-dihydroindane + NAD+
-
biotransformation with intact cell
-
?
(1R,2S)-(-)-trans-2-phenyl-1-cyclohexanol + NADH + O2
3-(2-hydroxycyclohexanyl)-3,5-cyclohexadiene-1,2-diol + ?
-
-
-
?
(4S,5S,6S)-4,5-dihydroxy-6-methoxycyclohex-2-enone + NADH + H+ + O2
(2S,3S,4S)-3,4-dihydroxy-2-methoxycyclohexanone + NAD+
-
-
-
-
?
(cis)-2-chloro-2-butene + NADH + O2
2-chloro-2-butene-1-ol + NAD+
-
12% of the activity with toluene
-
?
(R)-1-phenyl-1-ethanol + NADH + O2
3-[1(R)-hydroxyethyl]cyclohexa-3,5-diene-1(S),2(R)-diol + ?
-
-
-
?
(R)-2-phenylcyclohexanone + NADH + O2
(4S,4aR,9aR)-4,6,7,8,9,9a-hexahydro-4aH-dibenzofuran-4,5a-diol + ?
-
-
-
?
(S)-1-phenyl-1-ethanol + O2 + NADH + O2
3-[1(S)-hydroxyethyl]cyclohexa-3,5-diene-1(S),2(R)-diol + ?
-
-
-
?
(S)-2-phenylcyclohexanone + NADH + O2
(1S,5'S,6'R)-5',6'-dihydroxybicyclohexyl-1',3'-diene-2-one + ?
-
-
-
?
(trans)-2-chloro-2-butene + NADH + O2
?
-
4% of the activity with toluene
-
-
?
1,1-dichloro-1-propene + NADH + O2
3,3-dichloro-2-propene-1-ol + NAD+
-
6% of the activity with toluene
-
?
1,1-dichloro-1-propene + NADH + O2
?
-
18% of the activity with toluene
-
-
?
1-bromo-2-ethylbenzene + NADH + H+ + O2
(1S,2R)-4-bromo-3-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-bromo-3-ethylbenzene + NADH + H+ + O2
(1S,2R)-5-bromo-3-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-bromo-4-ethylbenzene + NADH + H+ + O2
(1R,2R)-3-bromo-6-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-bromo-4-propylbenzene + NADH + H+ + O2
(1R,2R)-3-bromo-6-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-chloro-2-ethylbenzene + NADH + H+ + O2
(1S,2R)-4-chloro-3-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-chloro-2-methyl-1-propene + NADH + O2
2-chloro-2-butene-1-ol + NAD+
-
13% of the activity with toluene
-
?
1-chloro-3-ethylbenzene + NADH + H+ + O2
(1S,2R)-5-chloro-3-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-chloro-3-propylbenzene + NADH + H+ + O2
(1S,2R)-5-chloro-3-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-chloro-4-ethylbenzene + NADH + H+ + O2
(1R,2R)-3-chloro-6-ethylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-chloro-4-propylbenzene + NADH + H+ + O2
(1R,2R)-3-chloro-6-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-ethyl-2-fluorobenzene + NADH + H+ + O2
(1S,2R)-3-ethyl-4-fluorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-ethyl-2-iodobenzene + NADH + H+ + O2
(1S,2R)-3-ethyl-4-iodocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-ethyl-3-fluorobenzene + NADH + H+ + O2
(1S,2R)-3-ethyl-5-fluorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-ethyl-4-fluorobenzene + NADH + H+ + O2
(1R,2R)-3-ethyl-6-fluorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-ethyl-4-iodobenzene + NADH + H+ + O2
(1R,2R)-3-ethyl-6-iodocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-fluoro-2-propylbenzene + NADH + H+ + O2
(1S,2R)-4-fluoro-3-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-fluoro-4-propylbenzene + NADH + H+ + O2
(1R,2R)-3-fluoro-6-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
1-phenylcyclohexene + NADH + O2
(1S,2R)-3-(1-cyclohexenyl)-3,5-cyclohexadiene-1,2-diol + ?
-
-
-
?
2,3-dichloro-1-propene + NADH + O2
2,3-dichloro-2-propene-1-ol + NAD+
-
19% of the activity with toluene
-
?
2-acetoxyindane + O2 + NADH
indan-2-ol + (-)-cis-(1S,2R)-1,2-dihydroxyindane + (-)-trans-(1R,2R)-1,2-dihydroxyindane + (-)-(2R)-2-hydroxyindan-1-one + NAD+
-
biotransformation with intact cells
-
?
2-bromoindane + O2 + NADH
(-)-cis-(1S,2R)-2-bromoindan-1-ol + (+)-trans-(1S,3S)-1,3-dihydroxy-2-bromoindane + NAD+
-
biotransformation with intact cells
-
?
2-carbamoylindane + O2 + NADH
(-)-cis-(1S,2R)-2-azoindan-1-ol + NAD+
-
biotransformation with intact cells
-
?
2-chloroaniline + NADH + H+ + O2
? + NAD+
-
degradation rates in decreasing order: 4-chloroaniline, 3-chloroaniline, 2-chloroaniline, 3,4-dichloroaniline
-
-
?
2-chloroindane + O2 + NADH
(-)-cis-(1S,2R)-2-chloroindan-1-ol + (+)-trans-(1R,2R)-2-chloroindan-1-ol + NAD+
-
biotransformation with intact cells
-
?
2-chloroindane + O2 + NADH
(-)-trans-(1S,3S)-1,3-dihydroxy-2-chloroindane + NAD+
-
biotransformation with intact cells
-
?
2-cresol + NADH + H+ + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2,4-triol + (2R)-6-methylcyclohexa-3,5-diene-1,1,2-triol + NAD+
-
poor substrate
-
-
?
2-indanone + NADH + O2
(S)-2-hydroxy-1-indanone + NAD+
-
no reaction with 1-indanone
95% S-enantiomer, product is formed by incorporation of a single atom of molecular oxygen rather than by dioxygenation of enol tautomers of the ketone substrate
?
2-iodoindane + O2 + NADH
(-)-cis-(1S,2R)-1,2-dihydroxyindane + (-)-(1R)-1-hydroxyindene + (+)-(1S,3S)-1,3-dihydroxy-2-iodoindane + NAD+
-
biotransformation with intact cells
-
-
?
2-methoxyindane + O2 + NADH
(-)-cis-(1S,2R)-2-methoxyindan-1-ol + (-)-trans-(1R,2R)-2-methoxyindan-1-ol + NAD+
-
biotransformation with intact cells
-
?
2-methoxyphenol + NADH + H+ + O2
(4S,5S)-4,5-dihydroxy-2-methoxycyclohex-2-enone + NAD+
-
-
-
-
?
2-methylindan + O2 + NADH
(-)-trans-(1R,3R)-1,3-dihydroxy-2-methylindane + (-)-cis-(2S,3R)-3-hydroxy-2-methylindan-1-one + (-)-cis-(1R,2R)-1-hydroxy-2-methylindane + (-)-(2R)-2-methyindan-1-one + NAD+
-
biotransformation with intact cells
-
?
3,4-dichloro-1-butene + NADH + O2
3,4-dichlorobutane-1,2-diol + NAD+
-
23% of the activity with toluene
-
?
3,4-dichloroaniline + NADH + H+ + O2
? + NAD+
-
degradation rates in decreasing order: 4-chloroaniline, 3-chloroaniline, 2-chloroaniline, 3,4-dichloroaniline
-
-
?
3-(propan-2-yl)benzene-1,2-diol + NADH + H+ + O2
(4R,5S)-4,5-dihydroxy-3-(propan-2-yl)cyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction. In addition to the cyclohexenone cis-diols, (4R,5S)-4,5-dihydroxy-3-(propan-2-yl)cyclohex-2-en-1-one, and triols, (1R,2S,4R)-6-(propan-2-yl)cyclohex-5-ene-1,2,4-triol, are obtained from biotransformation of the phenol parent compound in strain UV4 cultures
-
?
3-(trifluoromethyl)benzene-1,2-diol + NADH + H+ + O2
(4R,5S)-4,5-dihydroxy-3-(trifluoromethyl)cyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction. In addition to the cyclohexenone cis-diols, (4R,5S)-4,5-dihydroxy-3-(trifluoromethyl)cyclohex-2-en-1-one, and triols, (1R,2S,4R)-6-(trifluoromethyl)cyclohex-5-ene-1,2,4-triol, are obtained from biotransformation of the phenol parent compound in strain UV4 cultures
-
?
3-chloroaniline + NADH + H+ + O2
? + NAD+
-
degradation rates in decreasing order: 4-chloroaniline, 3-chloroaniline, 2-chloroaniline, 3,4-dichloroaniline
-
-
?
3-cresol + NADH + H+ + O2
(1R,2S)-6-methylcyclohexa-3,5-diene-1,2,4-triol + (2S)-3-methylcyclohexa-3,5-diene-1,1,2-triol + NAD+
-
-
-
-
?
3-ethylbenzene-1,2-diol + NADH + H+ + O2
(4R,5S)-3-ethyl-4,5-dihydroxycyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction. In addition to the cyclohexenone cis-diols, (4R,5S)-3-ethyl-4,5-dihydroxycyclohex-2-en-1-one, and triols, (1R,2S,4R)-6-ethylcyclohex-5-ene-1,2,4-triol, are obtained from biotransformation of the phenol parent compound in strain UV4 cultures
-
?
3-iodobenzene-1,2-diol + NADH + H+ + O2
(4S,5S)-4,5-dihydroxy-3-iodocyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction
-
?
3-methoxyphenol + NADH + H+ + O2
(1S,2S)-6-methoxycyclohexa-3,5-diene-1,2,4-triol + (2S)-3-methoxycyclohexa-3,5-diene-1,1,2-triol + NAD+
-
-
-
-
?
3-methoxyphenol + NADH + H+ + O2
(4S,5S)-4,5-dihydroxy-3-methoxycyclohex-2-enone + NAD+
-
-
-
-
?
3-methylbenzene-1,2-diol + NADH + H+ + O2
(4R,5S)-4,5-dihydroxy-3-methylcyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction
-
?
3-phenylcyclohexene + NADH + O2
(1S,2R)-3-(cyclohexenyl)-3,5-cyclohexadiene-1,2-diol + ?
-
-
-
?
3-phenylphenol + NADH + H+ + O2
(2R,3S)-2,3-dihydro[1,1'-biphenyl]-2,3,5-triol + (2S)-[1,1'-biphenyl]-2,3,3(2H)-triol + NAD+
-
-
-
-
?
3-tert-butylbenzene-1,2-diol + NADH + H+ + O2
(4R,5S)-3-tert-butyl-4,5-dihydroxycyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction. In addition to the cyclohexenone cis-diols, (4R,5S)-3-tert-butyl-4,5-dihydroxycyclohex-2-en-1-one, and triols, (1R,2S,4R)-6-tert-butylcyclohex-5-ene-1,2,4-triol, are obtained from biotransformation of the phenol parent compound in strain UV4 cultures
-
?
4-cresol + NADH + H+ + O2
(1R,2R)-6-methylcyclohexa-3,5-diene-1,2,3-triol + (2S)-4-methylcyclohexa-3,5-diene-1,1,2-triol + NAD+
-
-
-
-
?
4-picoline + NADH + O2
3-hydroxy-4-picoline + ?
-
E. coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits 5.6-times higher activity towards 4-picoline than the wild-type enzyme
-
?
4-xylene + NADH + H+ + O2
4-xylenol + NAD+ + H2O
-
activity in strain 39/D
-
-
?
allyl 2-bromobenzoate + NADH + H+ + O2
prop-2-en-1-yl (3S,4S)-2-bromo-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + allyl (5S,6R)-5,6-dihydroxy-2-bromocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
allyl 2-chlorobenzoate + NADH + H+ + O2
prop-2-en-1-yl (3S,4S)-2-chloro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + allyl (5S,6R)-5,6-dihydroxy-2-chlorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
allyl 2-fluorobenzoate + NADH + H+ + O2
prop-2-en-1-yl (3S,4S)-2-fluoro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + allyl (5S,6R)-5,6-dihydroxy-2-fluorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
allyl 2-iodobenzoate + NADH + H+ + O2
prop-2-en-1-yl (3S,4S)-3,4-dihydroxy-2-iodocyclohexa-1,5-diene-1-carboxylate + allyl (5S,6R)-5,6-dihydroxy-2-iodocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
biphenyl-2,3-diol + NADH + H+ + O2
(4R,5S)-4,5-dihydroxy-3-phenylcyclohex-2-en-1-one + NAD+
-
-
alkyl-substituted cyclohexenone cis-diols are formed as the most significant metabolites prior to extraction. In addition to the cyclohexenone cis-diols, (4R,5S)-4,5-dihydroxy-3-phenylcyclohex-2-en-1-one, and triols, (1R,2S,4R)-6-phenylcyclohex-5-ene-1,2,4-triol, are obtained from biotransformation of the phenol parent compound in strain UV4 cultures
-
?
bromobenzene + NADH + H+ + O2
(1S,2S)-3-bromocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
bromobenzene + NADH + H+ + O2
cis-(1S,2S)-3-bromocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
butyl phenyl sulfide + NADH + O2
(R)-butyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
chlorobenzene + NADH + H+ + O2
(1S,2S)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
cis-1,2-dichloroethene + NADH + O2
?
-
12% of the activity with toluene
-
-
?
cis-1,4-dichloro-2-butene + NADH + O2
1,4-dichlorobutane-2,3-diol
-
18% of the activity with toluene
-
?
cis-1-bromo-1-propene + NADH + O2
?
-
11% of the activity with toluene
-
-
?
cis-1-chloro-1-propene + NADH + O2
?
-
5% of the activity with toluene
-
-
?
cis-2-pentene + NADH + O2
pentane-2,3-diol + NAD+
-
16% of the activity with toluene
-
?
cis-dibromoethene + NADH + O2
1,2-dibromoethane-1,2-diol + NAD+
-
13% of the activity with toluene
-
?
diphenylmethane + NADH + O2
(1S,2R)-3-benzylcyclohexa-3,5-diene-1,2-diol + ?
-
-
-
-
?
ethenyl phenyl sulfide + NADH + O2
(R)-ethenyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
ethyl 2-bromobenzoate + NADH + H+ + O2
ethyl (3S,4S)-2-bromo-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + ethyl (5S,6R)-5,6-dihydroxy-2-bromocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
ethyl 2-chlorobenzoate + NADH + H+ + O2
ethyl (3S,4S)-2-chloro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + ethyl (5S,6R)-5,6-dihydroxy-2-chlorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
ethyl 2-fluorobenzoate + NADH + H+ + O2
ethyl (3S,4S)-2-fluoro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + ethyl (5S,6R)-5,6-dihydroxy-2-fluorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
ethyl 2-iodobenzoate + NADH + H+ + O2
ethyl (3S,4S)-3,4-dihydroxy-2-iodocyclohex-1,5-dienecarboxylate + ethyl (5S,6R)-5,6-dihydroxy-2-iodocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
ethyl phenyl sulfide + NADH + O2
(R)-ethyl phenyl sulfoxide
-
-
more than 98% R-enantiomer
?
ethylbenzene + NADH + H+ + O2
cis-2,3-dihydroxy-2,3-dihydroethylbenzene + NAD+
-
-
-
-
?
ethylbenzene + NADH + H+ + O2
ethylbenzene cis-dihydrodiol + NAD+
-
-
-
-
?
indan-1-ol + O2 + NADH
(-)-cis-(1S,2R)-1,2-dihydroxyindane + (-)-trans-(1R,2R)-1,2-dihydroxyindane + (-)-(2R)-2-hydroxyindan-1-one + NAD+
-
biotransformation with intact cells
-
?
indan-2-ol + O2 + NADH
(-)-cis-(1S,2R)-1,2-dihydroxyindane + (-)-trans-(1R,2R)-1,2-dihydroxyindane + NAD+
-
biotransformation with intact cells
-
?
indan-2-one + O2 + NADH
indan-2-ol + (-)-cis-(1S,2R)-1,2-dihydroxy-indane + (-)-trans-(1R,2R)-1,2-dihydroxy-indane + NAD+
-
biotransformation with intact cells
-
?
indene + NADH + H+ + O2
cis-(1S, 2R)-indandiol + 1-indenol + 1-indanone + NAD+
-
-
-
-
?
indene + NADH + H+ + O2
cis-(1S,2R)-indandiol + (1S)-indenol + NAD+
-
-
-
-
?
indene + O2 + NADH
(-)-cis-(1S,2R)-dihydroxyindan + (+)-(1S)-indenol + ?
-
monooxygenase reaction of toluene dioxygenase
in addition the enzyme catalyzes the dioxygen addition of the nonaromatic double bond of indene to form cis-1,2-indanediol. The oxygen atom in 1-indenol and cis,1,2-indanediol is derived from molecular oxygen
?
iodobenzene + NADH + H+ + O2
(1S,2S)-3-iodocyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
isopropyl phenyl sulfide + NADH + O2
(R)-isopropyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
methoxymethyl phenyl sulfide + NADH + O2
(R)-methoxymethyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
methyl (2-pyridyl) sulfide + NADH + O2
(R)-methyl (2-pyridyl) sulfoxide + ?
-
-
more than 98% R-enantiomer
?
methyl (2-thienyl) sulfide + NADH + O2
(R)-methyl (2-thienyl) sulfoxide + ?
-
-
more than 98% R-enantiomer
?
methyl 2-bromobenzoate + NADH + H+ + O2
methyl (3S,4S)-2-bromo-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + methyl (5S,6R)-2-bromo-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
methyl 2-chlorobenzoate + NADH + H+ + O2
methyl (3S,4S)-2-chloro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + methyl (5S,6R)-2-chloro-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
methyl 2-fluorobenzoate + NADH + H+ + O2
methyl (3S,4S)-2-fluoro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + methyl (5S,6R)-5,6-dihydroxy-2-fluorocyclohexa-1,3-dienecarboxylate + NAD+
-
-
-
-
?
methyl 2-iodobenzoate + NADH + H+ + O2
methyl (3S,4S)-3,4-dihydroxy-2-iodocyclohexa-1,5-diene-1-carboxylate + methyl (5S,6R)-5,6-dihydroxy-2-iodocyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
methyl p-nitrophenyl sulfide + O2
methyl p-nitrophenyl sulfoxide
-
-
86% S-enantiomer
?
methyl p-tolyl sulfide + O2
cis-1,2-dihydroxy-3-methyl-6-methylthiocyclohexa-3,5-diene
-
-
-
?
n-propyl 2-bromobenzoate + NADH + H+ + O2
propyl (3S,4S)-2-bromo-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + propyl (5S,6R)-2-bromo-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
n-propyl 2-chlorobenzoate + NADH + H+ + O2
propyl (3S,4S)-2-chloro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + propyl (5S,6R)-2-chloro-5,6-dihydroxycyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
n-propyl 2-fluorobenzoate + NADH + H+ + O2
propyl (3S,4S)-2-fluoro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + n-propyl (5S,6R)-5,6-dihydroxy-2-fluorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
n-propyl 2-iodobenzoate + NADH + H+ + O2
propyl (3S,4S)-3,4-dihydroxy-2-iodocyclohexa-1,5-diene-1-carboxylate + propyl (5S,6R)-5,6-dihydroxy-2-iodocyclohexa-1,3-diene-1-carboxylate + NAD+
-
-
-
-
?
p-methoxyphenyl methyl sulfide + O2
p-methoxyphenyl methyl sulfoxide
-
-
32% S-enantiomer
?
phenol + NADH + H+ + O2
(1S,2R)-cyclohexa-3,5-diene-1,2,4-triol + (2S)-cyclohexa-3,5-diene-1,1,2-triol + NAD+
-
-
-
-
?
phenylcyclohexane + NADH + O2
(1S,2R)-3-(1-cyclohexyl)-3,5-cyclohexadiene-1,2-diol + ?
-
-
-
?
propargyl 2-bromobenzoate + NADH + H+ + O2
prop-2-yn-1-yl (3S,4S)-2-bromo-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + propargyl (5S,6R)-5,6-dihydroxy-2-bromocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
propargyl 2-chlorobenzoate + NADH + H+ + O2
prop-2-yn-1-yl (3S,4S)-2-chloro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + propargyl (5S,6R)-5,6-dihydroxy-2-chlorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
propargyl 2-fluorobenzoate + NADH + H+ + O2
prop-2-yn-1-yl (3S,4S)-2-fluoro-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylate + propargyl (5S,6R)-5,6-dihydroxy-2-fluorocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
propargyl 2-iodobenzoate + NADH + H+ + O2
prop-2-yn-1-yl (3S,4S)-3,4-dihydroxy-2-iodocyclohexa-1,5-diene-1-carboxylate + propargyl (5S,6R)-5,6-dihydroxy-2-iodocyclohex-1,3-dienecarboxylate + NAD+
-
-
-
-
?
propyl phenyl sulfide + NADH + O2
(R)-propyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
propylbenzene + NADH + H+ + O2
(1S,2R)-3-propylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
propylbenzene + NADH + H+ + O2
cis-(1S,2R)-3-propylcyclohexa-3,5-diene-1,2-diol + cis-(1S,2R)-3-[(1R)-1-hydroxypropyl]cyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
styrene + NADH + H+ + O2
cis-2,3-dihydroxy-1-vinylcyclohexa-4,6-diene + (R)1-phenyl-1,2-ethanediol + NAD+
-
-
-
-
?
toluene + NADH + H+ + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
trans-1,4-dichloro-2-butene + NADH + O2
1,4-dichloro-2-butanone + NAD+
-
18% of the activity with toluene
-
?
trans-1-bromo-1-propene + NADH + O2
?
-
3% of the activity with toluene
-
-
?
trans-1-chloro-1-propene + NADH + O2
?
-
4% of the activity with toluene
-
-
?
trichloroethylene + NADH + O2
?
-
trichloroethylene degradation is mediated by the former degradation of toluene, benzene or cumene
-
-
?
trichloroethylene + O2 + NADPH
formate + glyoxylate + NADP+
-
-
formate accounts for 47% of the trichloroethylene oxidized, glyoxylate accounts for 17% of the trichloroethylene oxidized. Both carbon atoms give rise to formic acid
?
trifluoromethylbenzene + NADH + H+ + O2
(1S,2R)-3-(trifluoromethyl)cyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
3-cresol + NADH + H+ + O2
?
-
activity in strain UV4formation of the corresponding cis-diol and catechol
-
-
?
3-cresol + NADH + H+ + O2
?
-
activity in strain UV4, 3-cresol is a better substrate than 2-cresol
-
-
?
4-chloroaniline + NADH + H+ + O2
4-chlorocatechol + 2-amino-5-chlorophenol + NAD+
-
-
-
-
?
4-chloroaniline + NADH + H+ + O2
4-chlorocatechol + 2-amino-5-chlorophenol + NAD+
-
degradation rates in decreasing order: 4-chloroaniline, 3-chloroaniline, 2-chloroaniline, 3,4-dichloroaniline
toluene dioxygenase catalyzes both 1,2- and 2,3-dioxygenation of 4-chloroaniline
-
?
benzene + NADH + O2
benzene dihydrodiol + NAD+
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
ethylbenzene + NADH + O2
?
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
indane + NADH + O2
(-)-(1R)-indanol + NAD+
-
monooxygenase reaction of toluene dioxygenase
84% enantiomeric excess of (-)-(1R)-indanol, 70% of the oxygen in 1-indanol is derived from water
?
indane + NADH + O2
(-)-(1R)-indanol + NAD+
-
biotransformation with intact cells
+ indan-1-one
?
methyl phenyl sulfide + NADH + O2
(R)-methyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
methyl phenyl sulfide + NADH + O2
(R)-methyl phenyl sulfoxide + ?
-
-
more than 98% R-enantiomer
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
440335, 440336, 440337, 440338, 440339, 440340, 440341, 440342, 440343, 440344, 440345, 440346, 440347, 440348, 440349, 440350, 440351, 657604, 658332, 658336, 659826, 660044, 660050, 671081, 677654, 677655, 678835, 678837
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
E. coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits about 20% more activity towards toluene than the wild-type enzyme
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
initial enzyme of toluene catabolism
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
enzyme is involved in meta pathway for catechol degradation
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
xylene + NADH + O2
?
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
additional information
?
-
-
the oxygen atom in methyl phenyl sulfoxide is derived exclusively from dioxygen
-
-
?
additional information
?
-
-
the NADH-ferredoxinTOL reductase component catalyzes the NADH-dependent reduction of 2,6-dichloroindophenol, nitroblue tetrazolium and ferricyanide. NADPH is inactive
-
-
?
additional information
?
-
-
screening of substituted arenes containing remote chiral centers as substrates, enantiomers are indiscriminately processed to diastereomeric pairs
-
-
?
additional information
?
-
-
the purified alpha-subunit of oxygenase component is reduced by NADH and catalytic amounts of reductaseTOL and ferredoxinTOL. Reduced alpha-subunit can not oxidize toluene and catalysis is strictly dependent on the presence of beta-subunit
-
-
?
additional information
?
-
-
enzyme catalyzes monooxygenation and dioxygenation of aliphatic olefins
-
-
?
additional information
?
-
-
a high number of 2- or 3-substituted thiophenes were tested as substrates and were found to be metabolized
-
-
?
additional information
?
-
-
catechol and 3-methylcatechol are no substrates
-
-
?
additional information
?
-
-
the enzyme is organized in a multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system. The TDO system is composed of a reductase, TDO-R, a Rieske [2Fe2S] ferredoxin, TDO-F, and a terminal dioxygenase, TDO-O, overview. TDO-F shuttles electrons from NADH via a flavin in TDO-R to TDO-O, which catalyzes the enantioselective addition of dioxygen to the aromatic nucleus to form cis-(1R,2S)-dihydroxy-3-methylcyclohexa-3,5-diene
-
-
?
additional information
?
-
-
TodS exhibits basal autophosphorylation activity that increases in the presence of toluene and is translated as an increase in the rate of transphosphorylation of TodT
-
-
?
additional information
?
-
-
enzyme active site structure, the orientation of the toluene substrate in the active site is consistent with the regiospecificity of oxygen incorporation seen in the product formed, overview
-
-
?
additional information
?
-
-
the dioxygenase catalyzes the formation of cyclohexenone cis-diols, and o-quinol dimers from phenols via cis-dihydrodiol intermediate, substrate specificity and formed products, stereospecificity, overview
-
-
?
additional information
?
-
-
TodT-P is the active form of the response regulator that induces RNA polymerase to transcribe from the PtodX promoter
-
-
?
additional information
?
-
-
toluene dioxygenase catalyzes the stereospecific synthesis of cis-dihydrodiol metabolites from 2-substituted naphthalene substrates, assignments of absolute configurations and conformations from circular dichroism and optical rotation measurements, overview
-
-
?
additional information
?
-
-
dioxygenase-catalysed cis-dihydroxylation of meta-substituted phenols to yield cyclohexenone cis-diol and derived enantiopure cis-triol metabolites, overview. Formation of enantiopure cyclohexenone cis-diol metabolites and binding interactions of the m-phenol substrates at the active site of toluene dioxygenase, overview. Product analysis by NMR
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
toluene + NADH + H+ + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
3-cresol + NADH + H+ + O2
?
-
activity in strain UV4formation of the corresponding cis-diol and catechol
-
-
?
4-xylene + NADH + H+ + O2
4-xylenol + NAD+ + H2O
-
activity in strain 39/D
-
-
?
benzene + NADH + O2
benzene dihydrodiol + NAD+
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
ethylbenzene + NADH + O2
?
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
toluene + NADH + H+ + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
xylene + NADH + O2
?
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
initial enzyme of toluene catabolism
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
enzyme is involved in meta pathway for catechol degradation
-
-
?
toluene + NADH + O2
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
involved in the conversion of aromatic compounds to their corresponding catechols
-
-
?
additional information
?
-
-
the enzyme is organized in a multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system. The TDO system is composed of a reductase, TDO-R, a Rieske [2Fe2S] ferredoxin, TDO-F, and a terminal dioxygenase, TDO-O, overview. TDO-F shuttles electrons from NADH via a flavin in TDO-R to TDO-O, which catalyzes the enantioselective addition of dioxygen to the aromatic nucleus to form cis-(1R,2S)-dihydroxy-3-methylcyclohexa-3,5-diene
-
-
?
additional information
?
-
-
TodS exhibits basal autophosphorylation activity that increases in the presence of toluene and is translated as an increase in the rate of transphosphorylation of TodT
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
NADH-ferredoxinTOL reductase component contains 1 mol of noncovalently bound FAD per mol of protein
FAD
-
NADH-ferredoxinTOL reductase component is a flavoprotein that contains one mol of FAD per mol of enzyme. Km: 2.5 nM
NADH
-
-
440331, 440332, 440334, 440335, 440336, 440337, 440338, 440339, 440340, 440341, 440342, 440343, 440344, 440345, 440346, 440347, 440348, 440349, 440350, 440351, 440352, 657604, 658332, 658336, 659826, 660044, 660050, 671081, 676278, 676283, 677654, 677655, 678835, 678837, 681364, 681757, 697293, 741558, 742285, 742927, 743115, 743138, 743391
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Iron
-
iron-sulfur protein contains 2 gatom of iron and 2 gatom of acid-labile sulfur per mol of protein
Iron
-
ferredoxinTOL component of the toluene dioxygenase contains 2 gatoms each of iron and acid-labile sulfur which appear to be organized as a single [2Fe-2S]cluster
Iron
-
the oxygenase component contains 4-6 iron atoms per holoenzyme, the ferredoxin component contains one [2Fe-s2S] cluster of the Rieske type
Iron
-
the catalytic subunit contains a Rieske [2Fe2S] cluster and mononuclear iron at the active site. The iron is not strongly bound and is easily removed during enzyme purification
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values of the NADH-ferredoxinTOL reductase component: 0.0046 mM for cytochrome and 0.0105 mM for NADH
-
additional information
additional information
-
thermodynamic characterization of the molecular interactions between TodT and the C-TodT protein with individual TodT boxes
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
-
expression of genes encoding toluene dioxygenase complex todC1C2BA in Escherichia coli results in the ability to degrade 4-chloroaniline
metabolism
-
TodS and TodT proteins form a highly specific two-component regulatory system that controls the expression of genes involved in the degradation of toluene, benzene, and ethylbenzene via the toluene dioxygenase pathway
metabolism
-
the enzyme is involved in aromatic hydroxylation and mineralization pathways converting arenes into cis-dihydrodiols, overview
metabolism
-
the TodS/TodT two-component system of Pseudomonas putida regulates the expression of the toluene dioxygenase, tod, operon for the metabolism of toluene, benzene, and ethylbenzene, overview. The TodT protein is the cognate response regulator that activates transcription of the toluene dioxygenase, TOD, pathway genes at the PtodX promoter, expression from PtodS is under catabolite control, detailed overview
metabolism
the native glycerol dehydrogenase in Escherichia coli is identified as the main responsible enzyme for catechol generation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14700
-
ferredoxinTOL component of the toluene dioxygenase, equilibrium sedimentation
15300
-
alpha2beta2, 2 * 46000 + 2 * 15300, oxygenase component of toluene dioxygenase
15500
-
1 * 15500, ferredoxinTOL component of the toluene dioxygenase, SDS-PAGE
46000
additional information
46000
-
1 * 46000, NADH-ferredoxinTOL reductase component, SDS-PAGE
46000
-
alpha2beta2, 2 * 46000 + 2 * 15300, oxygenase component of toluene dioxygenase
additional information
-
three-component enzyme: 1. reductaseTOL, 2. ferredoxinTOL, 3. a complex iron-sulfur protein
additional information
-
the enzyme system consists of monomeric reductaseTOL and ferredoxinTOL and a dimeric terminal oxygenase
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
-
enzyme is a heterohexamer containing a catalytic and a structural subunit type, consists of three domains: an FAD-binding domain, an NADH-binding domain and a C-terminal domain
monomer
tetramer
-
alpha2beta2, 2 * 46000 + 2 * 15300, oxygenase component of toluene dioxygenase
additional information
monomer
-
1 * 15500, ferredoxinTOL component of the toluene dioxygenase, SDS-PAGE
monomer
-
1 * 46000, NADH-ferredoxinTOL reductase component, SDS-PAGE
additional information
-
the enzyme system consists of monomeric reductaseTOL, a ferredoxinTOL and a dimeric terminal oxygenase
additional information
-
in TodT, the C-terminal domain has about 65 amino acids and contains a helix-turn-helix domain
additional information
-
the enzyme is organized in a multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
TodS exhibits basal autophosphorylation activity that increases in the presence of toluene and is translated as an increase in the rate of transphosphorylation of TodT, TodT phosphorylation occurs only with the folded protein by the TodS sensor kinase, binding site analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop and sitting drop vapour diffusion method using 40% (w/v) polyethylene glycol 600, 0.1 M sodium citrate pH 6.1 and 20-50 mM Fe(NH4)2(SO4)
-
purified recombinant enzyme system components, hanging-drop or sitting-drop vapour diffusion method, from 1.4 M ammonium sulfate, 0.1 M HEPES, pH 7.7. TDO-F crystallized in 38% PEG 8000, 0.1 M MES pH 6.1 or 37% PEG 8000, 0.1 M MES, pH 5.8. Apo-TDO-O crystallizes in 40% w/v PEG 600, 0.1 M sodium citrate, pH 5.8. Cocrystallization experiments with Fe(NH4)2(SO4)2 and toluene were performed under strict anaerobic conditions in 40% w/v PEG 600, 0.1 M sodium citrate pH 6.1, 20-50 mM Fe(NH4)2(SO4)2 and 20 mM toluene, X-ray diffraction structure determinhation and analysis at 1.2-3.2 A resolution, molecular replacement, structure modelling, overview
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D219A
-
mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
E214A
-
mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
F366
-
the mutant shows strongly reduced activity compared to the wild type enzyme
H222A
-
mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
H228A
-
mutation at alpha-subunit of oxygenase component completely abolishes toluene dioxygenase activity, mutation completely eliminates formation of cis-toluene dihydrodiol
I324F
-
the mutant shows reduced activity compared to the wild type enzyme
T365N
-
the mutant shows slightly reduced activity compared to the wild type enzyme
Y221A
-
mutation at alpha-subunit of oxygenase component, 42% of the activity of the wild-type enzyme, formation of cis-toluene dihydrodiol is reduced
Y266A
-
mutation at alpha-subunit of oxygenase component, 12% of the activity of the wild-type enzyme, formation of cis-toluene dihydrodiol is reduced
additional information
additional information
-
Escherichia coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits 5.6times higher activity towards 4-picoline and about 20% more activity towards toluene than the wild-type enzyme
additional information
-
mutants SP6-1A, SP6-1G, and SP14-4H (created by error-prone PCR mutagenesis) show decreased 1-indenol production in comparison to the wild type enzyme
additional information
-
mutations in the different TodT boxes affect TodT binding to the mutant promoters, overview
additional information
-
introduction of a plasmid containing the entire tod operon todC1C2BADE to Pseudomonas putida T57 to enhance its ability to degrade 4-chloroaniline. The resulting strain shows 250-fold higher 4-chloroaniline degradation activity the parental strain. The recobinant strain degrades 2-chloroaniline, 3-chloroaniline, and 3,4-dichloroaniline as well as 3-chloroaniline, but not 3,5-dichloroaniline
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, ferredoxinTOL component of the toluene dioxygenase, stable for over 10 weeks
-
-20°C, purified NADH-ferredoxinTOL reductase component is stable for two weeks
-
0-4°C, ferredoxinTOL component of the toluene dioxygenase, stable for up to 72 h
-
0-4°C, purified NADH-ferredoxinTOL reductase component is stable for up to 30 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rapid purification of oxygenase component from a polyol-responsive monoclonal antibody
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-overexpression of TDO-F, TDO-R, TDO-O and apo-TDO-O in Escherichia coli
-
expression into Escherichia coli BW25113 DELTAgldA. A strongly regulated toluene dioxygenase plasmid system for the dearomatizing cis-1,2-dihydroxylation of benzene is developed. Escherichia coli BW25113 DELTAgldA strain harboring pBAD18-TDO system is a suitable platform for the production of the valuable compound cis-1,2-dihydrocatechol (DHC) at gram scale
expression of genes encoding toluene dioxygenase complex todC1C2BA in Escherichia coli
-
expression of mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding Thr
-
expression of wild-type TodT, C-terminal part of TodT, and TodT mutants in Escherichia coli strain BL21(DE3). Genes todS and todT are transcribed from a single promoter called PtodX once the response regulator TodT is phosphorylated by the TodS sensor kinase in response to pathway substrates
-
genes encoding the three components of the toluene dioxygenase overproduced in Escherichia coli JM109: 1. the reductaseTOL - tolA, 2. the ferredoxinTOL and 3. the two subunits of the terminal dioxygenase - todC1C2
-
genes todC1C2BA, expression of the enzyme components todC1, C2, B, and A in Escherichia coli strain JM109 and in Rhodococcus opacus strain B-4. In Escherichia coli JM109, the yield of hydroxylated monoaromatics decreased with increasing substrate hydrophobicity, while in Rhodococcus opacus B-4, high performance in the hydroxylation of monoaromatics occurs, irrespective of substrate hydrophobicity.
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the todST operon is transcribed from a main promoter and that the +1 initiation point is located 31 nucleotides upstream from the A of the first ATG codon and is preceded by a -10/-35 canonical promoter. Expression from PtodS is under catabolite control, and in cells growing with glucose, the level of expression from this promoter is reduced, which in turn translates to low levels of the TodS/TodT regulators and results in a decrease of transcription from the PtodX promoter. The main underlying regulatory mechanisms of the tod structural genes are at the levels of catabolite repression control from PtodS and transcription activation, mediated by the TodT response regulator through a regulatory cascade in which the effector enhances autophosphorylation of TodS by ATP, with subsequent transphosphorylation of TodT
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
whole cell bioassay for the detection of benzene, toluene, ethyl benzene, and xylenes (BTEX)
degradation
-
stable isotopes could serve as a diagnostic for detecting aerobic biodegradation of TCE by toluene oxygenases at contaminated sites. There are no significant differences in fractionation among the enzymes toluene 3-monoxygenase, toluene 4-monooxygenase, and toluene 2,3-dioxygenase for compounds trichloroethene and cis-1,2-dichloroethene
synthesis
synthesis
-
screening of substituted arenes containing remote chiral centers as substrates, enantiomers are indiscriminately processed to diastereomeric pairs. Some of these new metabolites are useful as synthons for morphine synthesis
synthesis
-
a series of cis-dihydrodiol metabolites is obtained by bacterial biotransformation of the corresponding 1,4-disubstituted benzene substrates using Pseudomonas putida UV4, a source of toluene dioxygenase
synthesis
-
Pseudomonas putida KT2442 (pSPM01) harboring TDO genes can effectively biotransform a wide-range of aromatic substrates into their cis-diols
synthesis
Escherichia coli BW25113 DELTAgldA strain harboring pBAD18-TDO system is a suitable platform for the production of the valuable compound cis-1,2-dihydrocatechol at gram scale. The DHC scaffold finds extensive application in the production of a variety of fine chemicals and bioactive compounds
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Subramanian, V.; Liu, T.N.; Yeh, W.K.; Narro, M.; Gibson, D.T.
Purification and properties of NADH-ferredoxinTOL reductase. A component of toluene dioxygenase from Pseudomonas putida
J. Biol. Chem.
256
2723-2730
1981
Pseudomonas putida
Subramanian, V.; Liu, T.N.; Yeh, W.K.; Gibson, D.T.
Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography
Biochem. Biophys. Res. Commun.
91
1131-1139
1979
Pseudomonas putida
Wackett, L.P.; Kwart, L.D.; Gibson, D.T.
Benzylic monooxygenation catalyzed by toluene dioxygenase from Pseudomonas putida
Biochemistry
27
1360-1367
1988
Pseudomonas putida
Yeh, W.K.; Gibson, D.T.; Liu, T.N.
Toluene dioxygenase: a multicomponent enzyme system
Biochem. Biophys. Res. Commun.
78
401-410
1977
Pseudomonas putida
Zylstra, G.J.; Gibson, D.T.
Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli
J. Biol. Chem.
264
14940-14946
1989
Pseudomonas putida
Stephens, G.M.; Sidebotham, J.M.; Mann, N.H.; Dalton, H.
Cloning and expression in Escherichia coli of the toluene dioxygenase gene from Pseudomonas putida
FEMS Microbiol. Lett.
57
295-300
1989
Pseudomonas putida, Pseudomonas putida NCIB11767
Zylstra, G.J.; Wackett, L.P.; Gibson, D.T.
Trichloroethylene degradation by Escherichia coli containing the cloned Pseudomonas putida F1 toluene dioxygenase genes
Appl. Environ. Microbiol.
55
3162-3166
1989
Pseudomonas putida
Subramanian, V.; Liu, T.N.; Yeh, W.K.; Serdar, C.M.; Wackett, L.P.; Gibson, D.T.
Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1
J. Biol. Chem.
260
2355-2363
1985
Pseudomonas putida
Zylstra, G.J.; McCombie, W.R.; Gibson, D.T.; Finette, B.A.
Toluene degradation by Pseudomonas putida F1: genetic organization of the tod operon
Appl. Environ. Microbiol.
54
1498-1503
1988
Pseudomonas putida
Wackett, L.P.
Toluene dioxygenase from Pseudomonas putida F1
Methods Enzymol.
188
39-45
1990
Pseudomonas putida
Lange, C.C.; Wackett, L.P.
Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification
J. Bacteriol.
179
3858-3865
1997
Pseudomonas putida
Jiang, H.; Parales, R.E.; Gibson, D.T.
The alpha subunit of toluene dioxygenase from Pseudomonas putida F1 can accept electrons from reduced FerredoxinTOL but is catalytically inactive in the absence of the beta subunit
Appl. Environ. Microbiol.
65
315-318
1999
Pseudomonas putida
Lynch, N.A.; Jiang, H.; Gibson, D.T.
Rapid purification of the oxygenase component of toluene dioxygenase from a polyol-responsive monoclonal antibody
Appl. Environ. Microbiol.
62
2133-2137
1996
Pseudomonas putida
Jiang, H.; Parales, R.E.; Lynch, N.A.; Gibson, D.T.
Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites
J. Bacteriol.
178
3133-3139
1996
Pseudomonas putida
Leahy, J.G.; Olsen, R.H.
Kinetics of toluene degradation by toluene-oxidizing bacteria as a function of oxygen concentration, and the effect of nitrate
FEMS Microbiol. Ecol.
23
23-30
1997
Pseudomonas sp., Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas sp. W31, Pseudomonas fluorescens CFS215
Lee, K.; Brand, J.M.; Gibson, D.T.
Stereospecific sulfoxidation by toluene and naphthalene dioxygenases
Biochem. Biophys. Res. Commun.
212
9-15
1995
Pseudomonas putida
Li, S.; Wackett, L.P.
Trichloroethylene oxidation by toluene dioxygenase
Biochem. Biophys. Res. Commun.
185
443-451
1992
Pseudomonas putida
Resnick, S.M.; Torok, D.S.; Lee, K.; Brand, J.M.; Gibson, D.T.
Regiospecific and stereoselective hydroxylation of 1-indanone and 2-indanone by naphthalene dioxygenase and toluene dioxygenase
Appl. Environ. Microbiol.
60
3323-3328
1994
Pseudomonas putida, Pseudomonas putida F39D
Bui, V.P.; Vidar Hansen, T.; Stenstrom, Y.; Hudlicky, T.; Ribbons, D.W.
A study of substrate specificity of toluene dioxygenase in processing aromatic compounds containing benzylic and/or remote chiral centers
New J. Chem.
25
116-124
2001
Pseudomonas putida
-
Boyd, D.R.; Sharma, N.D.; Haughey, S.A.; Kennedy, M.A.; McMurray, B.T.; Sheldrake, G.N.; Allen, C.C.R.; Dalton, H.; Sproule, K.
Toluene and naphthalene dioxygenase-catalyzed sulfoxidation of alkyl aryl sulfides
J. Chem. Soc. Perkin Trans.
1
1929-1934
1998
Pseudomonas putida, Pseudomonas putida UV4
-
Bowers, N.I.; Boyd, D.R.; Sharma, N.D.; Goodrich, P.A.; Groocock, M.R.; Blacker, A.J.; Goode, P.; Dalton, H.
Stereoselective benzylic hydroxylation of 2-substituted indanes using toluene dioxygenase as biocatalyst
J. Chem. Soc. Perkin Trans.
1
1453-1462
1999
Pseudomonas putida, Pseudomonas putida UV4
-
Sakamoto, T.; Joern, J.M.; Arisawa, A.; Arnold, F.H.
Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate
Appl. Environ. Microbiol.
67
3882-3887
2001
Pseudomonas putida
Bagneris, C.; Cammack, R.; Mason, J.R.
Subtle difference between benzene and toluene dioxygenases of Pseudomonas putida
Appl. Environ. Microbiol.
71
1570-1580
2005
Pseudomonas putida
Xu, Z.; Mulchandani, A.; Chen, W.
Detection of benzene, toluene, ethyl benzene, and xylenes (BTEX) using toluene dioxygenase-peroxidase coupling reactions
Biotechnol. Prog.
19
1812-1815
2003
Pseudomonas putida
Ni, Y.; Chen, R.R.
Lipoprotein mutation accelerates substrate permeability-limited toluene dioxygenase-catalyzed reaction
Biotechnol. Prog.
21
799-805
2005
Pseudomonas putida
Kim, J.Y.; Lee, K.; Kim, Y.; Kim, C.K.; Lee, K.
Production of dyestuffs from indole derivatives by naphthalene dioxygenase and toluene dioxygenase
Lett. Appl. Microbiol.
36
343-348
2003
Pseudomonas putida
Boyd, D.R.; Sharma, N.D.; Bowers, N.I.; Boyle, R.; Harrison, J.S.; Lee, K.; Bugg, T.D.; Gibson, D.T.
Stereochemical and mechanistic aspects of dioxygenase-catalysed benzylic hydroxylation of indene and chromane substrates
Org. Biomol. Chem.
1
1298-1307
2003
Pseudomonas putida, Pseudomonas putida UV4
Boyd, D.R.; Sharma, N.D.; Gunaratne, N.; Haughey, S.A.; Kennedy, M.A.; Malone, J.F.; Allen, C.C.; Dalton, H.
Dioxygenase-catalysed oxidation of monosubstituted thiophenes: sulfoxidation versus dihydrodiol formation
Org. Biomol. Chem.
1
984-994
2003
Pseudomonas putida, Pseudomonas putida UV4
Lee, K.; Friemann, R.; Parales, J.V.; Gibson, D.T.; Ramaswamy, S.
Purification, crystallization and preliminary X-ray diffraction studies of the three components of the toluene 2,3-dioxygenase enzyme system
Acta crystallogr. Sect. F
61
669-672
2005
Pseudomonas putida
Boyd, D.R.; Sharma, N.D.; Bowers, N.I.; Dalton, H.; Garrett, M.D.; Harrison, J.S.; Sheldrake, G.N.
Dioxygenase-catalysed oxidation of disubstituted benzene substrates: benzylic monohydroxylation versus aryl cis-dihydroxylation and the meta effect
Org. Biomol. Chem.
4
3343-3349
2006
Pseudomonas putida, Pseudomonas putida UV4
Boyd, D.R.; Sharma, N.D.; Llamas, N.M.; Coen, G.P.; McGeehin, P.K.; Allen, C.C.
Chemoenzymatic synthesis of trans-dihydrodiol derivatives of monosubstituted benzenes from the corresponding cis-dihydrodiol isomers
Org. Biomol. Chem.
5
514-522
2007
Pseudomonas putida, Pseudomonas putida UV4
Ramos-Gonzalez, M.I.; Ben-Bassat, A.; Campos, M.J.; Ramos, J.L.
Genetic engineering of a highly solvent-tolerant Pseudomonas putida strain for biotransformation of toluene to p-hydroxybenzoate
Appl. Environ. Microbiol.
69
5120-5127
2003
Pseudomonas putida, Pseudomonas putida DOT-T1E
Morono, Y.; Unno, H.; Tanji, Y.; Hori, K.
Addition of aromatic substrates restores trichloroethylene degradation activity in Pseudomonas putida F1
Appl. Environ. Microbiol.
70
2830-2835
2004
Pseudomonas putida
Shingleton, J.T.; Applegate, B.A.; Baker, A.J.; Sayler, G.S.; Bienkowski, P.R.
Quantification of toluene dioxygenase induction and kinetic modeling of TCE cometabolism by Pseudomonas putida TVA8
Biotechnol. Bioeng.
76
341-350
2001
Pseudomonas putida, Pseudomonas putida TVA8
Lovanh, N.; Alvarez, P.J.
Effect of ethanol, acetate, and phenol on toluene degradation activity and tod-lux expression in Pseudomonas putida TOD102: evaluation of the metabolic flux dilution model
Biotechnol. Bioeng.
86
801-808
2004
Pseudomonas putida
Woo, H.; Sanseverino, J.; Cox, C.D.; Robinson, K.G.; Sayler, G.S.
The measurement of toluene dioxygenase activity in biofilm culture of Pseudomonas putida F1
J. Microbiol. Methods
40
181-191
2000
Pseudomonas putida
Zhang, N.; Stewart, B.G.; Moore, J.C.; Greasham, R.L.; Robinson, D.K.; Buckland, B.C.; Lee, C.
Directed evolution of toluene dioxygenase from Pseudomonas putida for improved selectivity toward cis-indandiol during indene bioconversion
Metab. Eng.
2
339-348
2000
Pseudomonas putida
Boyd, D.R.; Sharma, N.D.; Coen, G.P.; Gray, P.J.; Malone, J.F.; Gawronski, J.
Enzyme-catalysed synthesis and absolute configuration assignments of cis-dihydrodiol metabolites from 1,4-disubstituted benzenes
Chemistry
13
5804-5811
2007
Pseudomonas putida, Pseudomonas putida UV4
Ouyang, S.P.; Liu, Q.; Sun, S.Y.; Chen, J.C.; Chen, G.Q.
Genetic engineering of Pseudomonas putida KT2442 for biotransformation of aromatic compounds to chiral cis-diols
J. Biotechnol.
132
246-250
2007
Pseudomonas putida, Pseudomonas putida KT 2442
Friemann, R.; Lee, K.; Brown, E.N.; Gibson, D.T.; Eklund, H.; Ramaswamy, S.
Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system
Acta Crystallogr. Sect. D
65
24-33
2009
Pseudomonas putida
Boyd, D.R.; Sharma, N.D.; Malone, J.F.; Allen, C.C.
New families of enantiopure cyclohexenone cis-diol, o-quinol dimer and hydrate metabolites from dioxygenase-catalysed dihydroxylation of phenols
Chem. Commun. (Camb. )
2009
3633-3635
2009
Pseudomonas putida
Kwit, M.; Gawronski, J.; Boyd, D.R.; Sharma, N.D.; Kaik, M.; More O'Ferrall, R.A.; Kudavalli, J.S.
Toluene dioxygenase-catalyzed synthesis of cis-dihydrodiol metabolites from 2-substituted naphthalene substrates: assignments of absolute configurations and conformations from circular dichroism and optical rotation measurements
Chemistry
14
11500-11511
2008
Pseudomonas putida, Pseudomonas putida UV4
Hamada, T.; Maeda, Y.; Matsuda, H.; Sameshima, Y.; Honda, K.; Omasa, T.; Kato, J.; Ohtake, H.
Effect of cell-surface hydrophobicity on bacterial conversion of water-immiscible chemicals in two-liquid-phase culture systems
J. Biosci. Bioeng.
108
116-120
2009
Pseudomonas putida
Lacal, J.; Guazzaroni, M.E.; Busch, A.; Krell, T.; Ramos, J.L.
Hierarchical binding of the TodT response regulator to its multiple recognition sites at the tod pathway operon promoter
J. Mol. Biol.
376
325-337
2008
Pseudomonas putida
Busch, A.; Lacal, J.; Silva-Jimenez, H.; Krell, T.; Ramos, J.L.
Catabolite repression of the TodS/TodT two-component system and effector-dependent transphosphorylation of TodT as the basis for toluene dioxygenase catabolic pathway control
J. Bacteriol.
192
4246-4250
2010
Pseudomonas putida
Boyd, D.R.; Sharma, N.D.; Stevenson, P.J.; Blain, M.; McRoberts, C.; Hamilton, J.T.; Argudo, J.M.; Mundi, H.; Kulakov, L.A.; Allen, C.C.
Dioxygenase-catalysed cis-dihydroxylation of meta-substituted phenols to yield cyclohexenone cis-diol and derived enantiopure cis-triol metabolites
Org. Biomol. Chem.
9
1479-1490
2011
Pseudomonas putida, Pseudomonas putida UV4
Clingenpeel, S.; Moan, J.; McGrath, D.; Hungate, B.; Watwood, M.
Stable carbon isotope fractionation in chlorinated ethene degradation by bacteria expressing three toluene oxygenases
Front. Microbiol.
3
63
2012
Pseudomonas putida
Lin, T.Y.; Werther, T.; Jeoung, J.H.; Dobbek, H.
Suppression of electron transfer to dioxygen by charge transfer and electron transfer complexes in the FAD-dependent reductase component of toluene dioxygenase
J. Biol. Chem.
287
38338-38346
2012
Pseudomonas putida
Nitisakulkan, T.; Oku, S.; Kudo, D.; Nakashimada, Y.; Tajima, T.; Vangnai, A.; Kato, J.
Degradation of chloroanilines by toluene dioxygenase from Pseudomonas putida T57
J. Biosci. Bioeng.
117
292-297
2013
Pseudomonas putida, Pseudomonas putida T57
Vila, M.; Umpierrez, D.; Veiga, N.; Seoane, G.; Carrera, I.; Rodriguez Giordano, S.
Site-directed mutagenesis studies on the toluene dioxygenase enzymatic system Role of phenylalanine 366, threonine 365 and isoleucine 324 in the chemo-, regio-, and stereoselectivity
Adv. Synth. Catal.
359
2149-2157
2017
Pseudomonas putida
-
Vila, M.A.; Pazos, M.; Iglesias, C.; Veiga, N.; Seoane, G.; Carrera, I.
Toluene dioxygenase-catalysed oxidation of benzyl azide to benzonitrile mechanistic insights for an unprecedented enzymatic transformation
ChemBioChem
17
291-295
2016
Pseudomonas putida
Nitisakulkan, T.; Oku, S.; Kudo, D.; Nakashimada, Y.; Tajima, T.; Vangnai, A.; Kato, J.
Degradation of chloroanilines by toluene dioxygenase from Pseudomonas putida T57
J. Biosci. Bioeng.
117
292-297
2014
Pseudomonas putida, Pseudomonas putida T57
Vila, M.; Umpierrez, D.; Seoane, G.; Rodriguez, S.; Carrera, I.; Veiga, N.
Computational insights into the oxidation of mono- and 1,4 disubstituted arenes by the toluene dioxygenase enzymatic complex
J. Mol. Catal. B
133
5410-5419
2016
Pseudomonas putida (A5W4F2), Pseudomonas putida strain ATCC 700007 (A5W4F2)
-
Hoering, P.; Rothschild-Mancinelli, K.; Sharma, N.; Boyd, D.; Allen, C.
Oxidative biotransformations of phenol substrates catalysed by toluene dioxygenase A molecular docking study
J. Mol. Catal. B
134
396-406
2016
Pseudomonas putida, Pseudomonas putida UV4
-
Boyd, D.R.; Sharma, N.D.; Malone, J.F.; McIntyre, P.B.; McRoberts, C.; Floyd, S.; Allen, C.C.; Gohil, A.; Coles, S.J.; Horton, P.N.; Stevenson, P.J.
Toluene dioxygenase-catalyzed synthesis and reactions of cis-diol metabolites derived from 2- and 3-methoxyphenols
J. Org. Chem.
80
3429-3439
2015
Pseudomonas putida, Pseudomonas putida UV4
Froese, J.; Endoma-Arias, M.; Hudlicky, T.
Processing of o-halobenzoates by toluene dioxygenase. The role of the alkoxy functionality in the regioselectivity of the enzymatic dihydroxylation reaction
Org. Process Res. Dev.
18
801-809
2014
Pseudomonas putida
-
Wissner, J.L.; Ludwig, J.; Escobedo-Hinojosa, W.; Hauer, B.
An enhanced toluene dioxygenase platform for the production of cis-1,2-dihydrocatechol in Escherichia coli BW25113 lacking glycerol dehydrogenase activity
J. Biotechnol.
325
380-388
2021
Pseudomonas putida (A5W4F2 AND A5W4F1), Pseudomonas putida
EXTERNAL LINKS (specific for EC-Number 1.14.12.11)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
