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1.13.12.19: 2-oxoglutarate dioxygenase (ethene-forming)

This is an abbreviated version!
For detailed information about 2-oxoglutarate dioxygenase (ethene-forming), go to the full flat file.

Word Map on EC 1.13.12.19

Reaction

2-oxoglutarate
+
O2
=
Ethene
+ 3 CO2 +
H2O

Synonyms

2-oxoglutarate-Fe(II) oxygenase, 2OG-Fe(II) oxygenase, EFE, ethylene forming enzyme, ethylene-forming enzyme, More, PsEFE

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
                1.13.12.19 2-oxoglutarate dioxygenase (ethene-forming)

Engineering

Engineering on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A198V
site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene
A199G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A281V
site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme
C280F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D191A
site-directed mutagenesis, inactive mutant
D191E
the D191E variant degrades L-Arg and 2-oxoglutarate to pyrroline-5-carboxylate (again detected after reduction to proline and Fmoc derivatization) and succinate nearly stoichiometrically, with only about 5% of the cosubstrate being fragmented to ethylene
E235D
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
E84D
site-directed mutagenesis, the mutant does not produce ethylene
E84Q
site-directed mutagenesis, the mutant does not produce ethylene
F278Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
F283A
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283R
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283V
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283Y
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
H116Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H169Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H189A
site-directed mutagenesis, inactive mutant
H233A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H233Q
site-directed mutagenesis, inactive mutant
H268A
site-directed mutagenesis, inactive mutant
H284Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H309Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I254M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
I304N
site-directed mutagenesis, inactive mutant
I322V
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L22M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
R171A
R171K
site-directed mutagenesis, the mutant does not produce ethylene
R236S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R277A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
R316A
site-directed mutagenesis, the mutant shows reduced ethylene production compared to the wild-type enzyme
R316K
site-directed mutagenesis, the mutant shows reduced ethylene production compared to the wild-type enzyme
V172T
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
V196F
site-directed mutagenesis, the mutant is expressed in inclusion bodies
V212Y/E213S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y172F
site-directed mutagenesis, the mutant shows reduced ethylene production compared to the wild-type enzyme
A198V
-
site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene
-
F283Y
-
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
-
H309Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
R171A
-
site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene
-
V196F
-
site-directed mutagenesis, the mutant is expressed in inclusion bodies
-
H116Q
kcat value decreases to 2.4% of wild-type. Mutant is more thermolabile than wild-type
H168Q
kcat value decreases to 3% of wild-type. Mutant is more thermolabile than wild-type
H169Q
kcat value decreases to 9.3% of wild-type. Mutant is more thermolabile than wild-type
H189Q
complete loss of activity
H233Q
complete loss of activity
H268Q
kcat value decreases to 1.8% of wild-type
H284Q
kcat value decreases to 2% of wild-type. Mutant is more thermolabile than wild-type
H305Q
kcat value decreases to 40% of wild-type
H309Q
kcat value decreases to 3.3% of wild-type. Mutant is more thermolabile than wild-type
H335Q
kcat value decreases to 60% of wild-type
A199G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C280F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D191A
site-directed mutagenesis, inactive mutant
E235D
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F278Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H189A
site-directed mutagenesis, inactive mutant
H233A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H268A
site-directed mutagenesis, inactive mutant
I254M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
I304N
site-directed mutagenesis, inactive mutant
I322V
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L22M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
R236S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V172T
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
V212Y/E213S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information