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Literature summary for 1.14.20.7 extracted from
- Overcoming substrate limitations for improved production of ethylene in E. coli (2016), Biotechnol. Biofuels, 9, 3-13 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | biological ethylene production can be achieved via expression of the ethylene-forming enzyme (EFE), found in some bacteria and fungi. It has the potential to provide a sustainable alternative to steam cracking. Ethylene is an important industrial compound for the production of a wide variety of plastics and chemicals | Pseudomonas syringae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene efe, recombinant expression in Escherichia coli strain MG1655, importance of promoter strength on the expression of enzyme EFE in Escherichia coli with stronger promoters producing elevated levels of ethylene, e.g. the Amaranthus hybridus chloroplast psbA promoter (PpsbA), expression method optimization, overview | Pseudomonas syringae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | 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 | Pseudomonas syringae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas syringae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxoglutarate + L-arginine + O2 | - |
Pseudomonas syringae | succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O | - |
? |  |
| 3 2-oxoglutarate + L-arginine + 3 O2 | cf. EC 1.13.12.19 | Pseudomonas syringae | 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EFE | - |
Pseudomonas syringae |
| ethylene-forming enzyme | - |
Pseudomonas syringae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Pseudomonas syringae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Pseudomonas syringae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in the presence of O2, the enzyme catalyzes ethylene formation from the substrates 2-oxoglutarate and L-arginine | Pseudomonas syringae |
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