1.14.13.236: toluene 4-monooxygenase
This is an abbreviated version!
For detailed information about toluene 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.236
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1.14.13.236
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hydroxylase
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diiron
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mendocina
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p-cresol
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regiospecificity
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ferredoxins
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cepacia
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rieske
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synthesis
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pickettii
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ortho-monooxygenase
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m-nitrophenol
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nitrobenzene
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2-naphthol
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3-monooxygenase
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rieske-type
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four-protein
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diferric
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o-xylene
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norcarane
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xanthobacter
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analysis
- 1.14.13.236
- hydroxylase
-
diiron
- mendocina
- p-cresol
-
regiospecificity
- ferredoxins
- cepacia
-
rieske
- synthesis
- pickettii
-
ortho-monooxygenase
- m-nitrophenol
- nitrobenzene
- 2-naphthol
-
3-monooxygenase
-
rieske-type
-
four-protein
-
diferric
- o-xylene
- norcarane
- xanthobacter
- analysis
Reaction
Synonyms
T4moD, T4moF, T4MOH, TMO, TmoA, TmoC, TmoF, toluene-4-monooxygenase system protein A, TOM, TomA3
ECTree
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General Information
General Information on EC 1.14.13.236 - toluene 4-monooxygenase
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physiological function
during reactions in the absence of substrate, wild-type toluene 4-monooxygenase hydroxylase T4moH slowly consumes O2 but only a negligible amount of H2O2 is released
physiological function
electron transfer subunit TmoF stimulates T4MO activity two- to threefold when coexpressed in Escherichia coli or Pseudomonas putida. The reductase component of the naphthalene dioxygenase system, encoded by the nahA gene of plasmid NAH7 from Pseudomonas putida G7, can largely replace the TmoF protein in stimulating T4MO activity, and TmoF can partially replace the NahA protein in forming active naphthalene dioxygenase
physiological function
proteins required for the in Vitro reconstitution of T4MO catalytic activity are a diiron hydroxylase (T4MOH), a Rieske-type ferredoxin (T4MOC), an effector protein (T4MOD), and an NADH oxidoreductase (T4MOF). The T4MOH component is composed of the tmoA, tmoB, and tmoE gene products with quaternary structure (alpha,beta,epsilon)2. T4MOH is the hydroxylase, the NADH-dependent multiple-turnover hydroxylation activity is increased by more than 100fold in the presence of T4MOC, which mediates highly specific electron transfer between T4MOF and T4MOH. T4MOD is a 11.6 kDa monomeric protein devoid of cofactors or redox-active metal ions and is also detected as a substoichiometric consitutent of the purified T4MOH. The rate of the hydroxylation reaction can be mildly stimulated by the further addition of separately purified T4MOD to the T4MOH
physiological function
-
during reactions in the absence of substrate, wild-type toluene 4-monooxygenase hydroxylase T4moH slowly consumes O2 but only a negligible amount of H2O2 is released
-
physiological function
-
proteins required for the in Vitro reconstitution of T4MO catalytic activity are a diiron hydroxylase (T4MOH), a Rieske-type ferredoxin (T4MOC), an effector protein (T4MOD), and an NADH oxidoreductase (T4MOF). The T4MOH component is composed of the tmoA, tmoB, and tmoE gene products with quaternary structure (alpha,beta,epsilon)2. T4MOH is the hydroxylase, the NADH-dependent multiple-turnover hydroxylation activity is increased by more than 100fold in the presence of T4MOC, which mediates highly specific electron transfer between T4MOF and T4MOH. T4MOD is a 11.6 kDa monomeric protein devoid of cofactors or redox-active metal ions and is also detected as a substoichiometric consitutent of the purified T4MOH. The rate of the hydroxylation reaction can be mildly stimulated by the further addition of separately purified T4MOD to the T4MOH
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physiological function
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electron transfer subunit TmoF stimulates T4MO activity two- to threefold when coexpressed in Escherichia coli or Pseudomonas putida. The reductase component of the naphthalene dioxygenase system, encoded by the nahA gene of plasmid NAH7 from Pseudomonas putida G7, can largely replace the TmoF protein in stimulating T4MO activity, and TmoF can partially replace the NahA protein in forming active naphthalene dioxygenase
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