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1.7.2.3: trimethylamine-N-oxide reductase

This is an abbreviated version!
For detailed information about trimethylamine-N-oxide reductase, go to the full flat file.

Word Map on EC 1.7.2.3

Reaction

trimethylamine
+ 2 (ferricytochrome c)-subunit +
H2O
=
Trimethylamine N-oxide
+ 2 (ferrocytochrome c)-subunit + 2 H+

Synonyms

EC 1.6.6.9, More, reductase, trimethylamine N-oxide, TMAO reductase, TOR, TorA, TorD, torECA gene product, TorECAD, TorZ, trimethylamine N-oxide reductase, trimethylamine oxide reductase

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.2 With a cytochrome as acceptor
                1.7.2.3 trimethylamine-N-oxide reductase

Specific Activity

Specific Activity on EC 1.7.2.3 - trimethylamine-N-oxide reductase

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.096
-
anaerobic growth conditions, grown without trimethylamine N-oxide
0.13
-
periplasmic fraction
0.163
-
microaerobic growth conditions, grown without trimethylamine N-oxide
0.25
-
aerobic growth conditions, grown with trimethylamine N-oxide
0.374
-
anaerobic growth conditions, grown with trimethylamine N-oxide
0.41
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, formate as electron donor
0.56
-
microaerobic growth conditions, grown with trimethylamine N-oxide
0.66
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, FMN or vitamin K5 as electron donor
1.29
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, formate as electron donor
1.56
-
wild-type strain, formate as electron donor
10.2
-
purified enzyme
105
-
purified enzyme, with trimethylamine N-oxide as substrate
11.2
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, methyl viologen as electron donor
1350
-
crude extract of mutant strain lacking the TorD protein
1720
-
crude extract of wild-type strain
1810
-
crude extract of mutant strain lacking the TorD protein but complemented by pTorD
2.63
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, vitamin K5 as electron donor
250
-
purified enzyme
3.73
-
wild-type strain, vitamin K5 as electron donor
3.77
-
mutants, which reduce little or no trimethylamine N-oxide in vivo, but their extracts retain full capacity to reduce it with methyl viologen, FMN as electron donor
320
-
30 mM trimethylamine N-oxide, cell free extract, anaerobic conditions
33
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of 2-hydroxypyridine N-oxide
34
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM
35
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of tetramethylenesulfoxide
36
-
purified enzyme, assay performed in 100 mM phosphate buffer, pH 6.8 with a trimethylamine N-oxide concentration 0.5 mM and a concentration 20 mM of picolinic acid N-oxide or a concentration 20 mM of dimethylsulfoxide
4.31
-
mutants partially defective in trimethylamine N-oxide reductase activity, which lack the inducible enzyme but retain the constitutive activity, methyl viologen as electron donor
4.7
-
wild-type strain, FMN as electron donor
41
-
purified tungsten-substituted enzyme
70
-
30 mM trimethylamine N-oxide, cell free extract, aerobic conditions
9.92
-
wild-type strain, methyl viologen as electron donor
additional information