1.14.20.7: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
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For detailed information about 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming), go to the full flat file.
Reaction
Synonyms
2-oxoglutarate-dependent ethylene/succinate-forming enzyme, 2-oxoglutarate-dependent oxygenase-type ethylene-forming-enzyme, 2-oxoglutarate-Fe(II) oxygenase, 2OG-Fe(II) oxygenase, EC 1.14.11.34, EFE, ethylene forming enzyme, ethylene-forming enzyme, More
ECTree
1.14.20.7 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)Advanced search results
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results (Engineering
Engineering on EC 1.14.20.7 - 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A199G
the mutant shows reduced activity compared to the wild type enzyme
I304N
the mutant shows reduced activity compared to the wild type enzyme
V212Y/E213S
the mutant shows reduced activity compared to the wild type enzyme
A198V
A199G
the mutant shows reduced activity compared to the wild type enzyme
A218V
the mutant shows about 3% of wild type activity
A281V
site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme
C317A
the mutant shows about 34% of wild type activity
C317S
the mutant shows about 21% of wild type activity
D191E
the D191E variant degrades L-Arg and 2-oxoglutarateto 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
E213A
the mutant shows about 90% of wild type activity
E213A/E215A
the mutant shows about 5% of wild type activity
E215A
the mutant shows about 5% of wild type activity
E235D
the mutant shows about wild type activity
E285A
the mutant shows about 10% of wild type activity
E285Q
the mutant shows about 25% of wild type activity
F175Y
the mutant shows about 18% of wild type activity
F278Y
the mutant shows about wild type activity
F283A
F283R
F283V
F283W
the mutant shows about 20% of wild type activity
F283Y
F310R
the mutant shows about 3% of wild type activity
F310W
the mutant shows about 30% of wild type activity
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
H233Q
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
the mutant shows about wild type activity
I304N
the mutant shows reduced activity compared to the wild type enzyme
I322V
the mutant shows about wild type activity
L22M
the mutant shows about wild type activity
L73K
the mutant shows about 60% of wild type activity
L73R
the mutant shows about 40% of wild type activity
R171A
R184A
the mutant shows about 75% of wild type activity
R277A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
R316A
the mutant shows about 3.7% of wild type activity
R316K
the mutant shows about 13% of wild type activity
S81R
the mutant shows about 5% of wild type activity
S81Y
the mutant shows about 5% of wild type activity
T86S
the mutant shows about 31% of wild type activity
V172T
the mutant shows about wild type activity
V196F
V212Y/E213S
the mutant shows reduced activity compared to the wild type enzyme
V270T
the mutant shows about 4.3 % of wild type activity
Y192F
the mutant shows about 5.6% of wild type activity
Y306A
the mutant shows about 3% of wild type activity
Y306F
the mutant shows about 5% of wild type activity
Y318F
the mutant shows about 65% of wild type activity
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
H284Q
kcat value decreases to 2% of wild-type. Mutant is more thermolabile than wild-type
H309Q
kcat value decreases to 3.3% of wild-type. Mutant is more thermolabile than wild-type
additional information
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improvement of ethylene forming enzyme expression in Escherichia coli, method optimization, overview. Because L-arginine is a co-substrate of 2-oxoglutarate for the production of ethylene, L-arginine availability is improved via deregulation of L-arginine biosynthesis. In Escherichia coli, arginine biosynthesis is controlled by a regulatory protein encoded by argR. Knockout of gene argR alleviates regulation of arginine biosynthesis resulting in increased arginine availability. The removal of arginine biosynthesis regulation in the DELTAargR Escherichia coli mutant strain improves production of ethylene by 36 % compared to the wild-type strain. Knockout of both small and large subunits of the native glutamate synthase (gltBD) might increase 2-oxoglutarate accumulation and production of ethylene. The removal of a third 2-oxoglutarate-consuming pathway, 2-oxoglutarate dehydrogenase (sucA), is also explored. This enzyme catalyzes the formation of succinyl-CoA and CO2 from AKG, and deletion of sucA results in increased 2-oxoglutarate levels in batch culture
A198V
the mutant shows about 60% of wild type activity
A198V
site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene
F283A
the mutant shows about 20% of wild type activity
F283A
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283R
the mutant shows about 20% of wild type activity
F283R
site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
F283V
the mutant shows about 20% of wild type activity
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
R171A
site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene
V196F
site-directed mutagenesis, the mutant is expressed in inclusion bodies
