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1.14.12.3: benzene 1,2-dioxygenase

This is an abbreviated version!
For detailed information about benzene 1,2-dioxygenase, go to the full flat file.

Word Map on EC 1.14.12.3

Reaction

Benzene
+
NADH
+
H+
+
O2
=
cis-cyclohexa-3,5-diene-1,2-diol
+
NAD+

Synonyms

BDO, BED, benzene dioxygenase, benzene hydroxylase, More, oxygenase, benzene 1,2-di-

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
                1.14.12.3 benzene 1,2-dioxygenase

Engineering

Engineering on EC 1.14.12.3 - benzene 1,2-dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A291S
-
reduced activity with ethylbenzene
E444D
-
no effect on activity
G404D
-
reduced activity with ethylbenzene
H119C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors
H222M
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
H228C
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
H98C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors, detection of a novel EPR spectrum, the intensity of the spectrum is approximately 8% from the wild-type
I301V
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
I301V/T305S/I307L/L309V
I307L
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
I412V
-
reduced activity with ethylbenzene
K436R
-
reduced activity with ethylbenzene
L285W
-
reduced activity with ethylbenzene
L285W/A291S/G404D
-
slightly reduced activity with ethylbenzene
L28W/A291S
-
reduced activity with ethylbenzene
L309V
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
T305S
-
the mutation in the C-terminal part of subunit alpha enhances the substrate specificity for ethylbenzene, the mutant shows altered patterns of products formed from toluene and ethylbenzene, including monohydroxylated side chains
V324I/I327V
-
reduced activity with ethylbenzene
Y118S
-
the mutant alpha-subunit of the terminal dioxygenase shows an EPR spectrum of half the intensity of that of the wild-type. In the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase it shows significantly reduced activities
Y221A
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit shows significantly reduced activity
H119C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors
-
H222M
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit is unable to reconstitute dioxygenase activity
-
H98C
-
the mutant alpha-subunit of the terminal dioxygenase is unable to coordinate an EPR-detectable Rieske [2Fe-2S] cluster with the characteristic g factors, detection of a novel EPR spectrum, the intensity of the spectrum is approximately 8% from the wild-type
-
Y118S
-
the mutant alpha-subunit of the terminal dioxygenase shows an EPR spectrum of half the intensity of that of the wild-type. In the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase it shows significantly reduced activities
-
Y221A
-
in the reconstitution assay with the reductase component, the ferredoxin component and the beta-subunit of terminal dioxygenase the mutant alpha-subunit shows significantly reduced activity
-
additional information