1.14.12.11: toluene dioxygenase

This is an abbreviated version!
For detailed information about toluene dioxygenase, go to the full flat file.

Word Map on EC 1.14.12.11

Reaction

Toluene
+
NADH
+
H+
+
O2
=
(1S,2R)-3-Methylcyclohexa-3,5-diene-1,2-diol
+
NAD+

Synonyms

ISPTOD, ISPTOL, More, oxygenase, toluene 2,3-di-, oxygenaseTOL, TDO, Tod, todC1C2BA, toluene 2,3-dioxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
                1.14.12.11 toluene dioxygenase

Engineering

Engineering on EC 1.14.12.11 - toluene dioxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
E609L
-
increased activity with all substrates
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