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
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1.13.12.19
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1-aminocyclopropane-1-carboxylic
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2og-feii
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syringae
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climacteric
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carnation
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dianthus
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photoautotrophic
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biotechnology
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agriculture
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synthesis
- 1.13.12.19
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1-aminocyclopropane-1-carboxylic
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2og-feii
- syringae
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climacteric
- carnation
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dianthus
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photoautotrophic
- biotechnology
- agriculture
- synthesis
Reaction
Synonyms
2-oxoglutarate-Fe(II) oxygenase, 2OG-Fe(II) oxygenase, EFE, ethylene forming enzyme, ethylene-forming enzyme, More, PsEFE
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming)
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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
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site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene
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F283Y
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site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production
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H309Q
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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R171A
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site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene
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V196F
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site-directed mutagenesis, the mutant is expressed in inclusion bodies
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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
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
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
H233A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I254M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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
site-directed mutagenesis, the mutant does not produce ethylene
R171A
site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene
a loop deletion mutant is inactive
additional information
construction of a glycogen-synthesis knockout mutant (DELTAglgC) to raise the intracellular amounts of the key Efe substrate, 2-oxoglutarate, from which ethylene is formed. Introduction of the ethylene biosynthetic pathway in mutant DELTAglgC. Under nitrogen limiting conditions, the glycogen knockout strain has increased intracellular 2-oxoglutarate levels, but the ethylene production is lower in the mutant strain than in the wild-type strain
additional information
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construction of a glycogen-synthesis knockout mutant (DELTAglgC) to raise the intracellular amounts of the key Efe substrate, 2-oxoglutarate, from which ethylene is formed. Introduction of the ethylene biosynthetic pathway in mutant DELTAglgC. Under nitrogen limiting conditions, the glycogen knockout strain has increased intracellular 2-oxoglutarate levels, but the ethylene production is lower in the mutant strain than in the wild-type strain
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additional information
introduction of a gene encoding a chimeric protein consisting of EFE and beta-glucuronidase GUS into the tobacco genome using a binary vector which directs expression of the EFE-GUS fusion protein under the control of constitutive promoter of cauliflower mosaic virus 35S RNA
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
additional information
a loop deletion mutant is inactive