Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ascorbate | required | Pseudomonas savastanoi pv. phaseolicola |
Cloned (Comment) | Organism |
---|---|
gene efe, large scale expression of His6-tagged enzyme in Escherichia coli strain BL21 Gold (DE3), method optimization and evaluation | Pseudomonas savastanoi pv. phaseolicola |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | dependent on, required for catalysis | Pseudomonas savastanoi pv. phaseolicola |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
39370 | - |
recombinant detagged enzyme, gel filtration | Pseudomonas savastanoi pv. phaseolicola |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutarate + O2 | Pseudomonas savastanoi pv. phaseolicola | - |
ethylene + 3 CO2 + H2O | - |
? | |
2-oxoglutarate + O2 | Pseudomonas savastanoi pv. phaseolicola PK2 | - |
ethylene + 3 CO2 + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas savastanoi pv. phaseolicola | P32021 | - |
- |
Pseudomonas savastanoi pv. phaseolicola PK2 | P32021 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21 Gold (DE3) by nickel affinity chromatography, tag cleavage by a TEV protease mutant, and another step of nickel affinity chromatography, and dialysis of the flow through | Pseudomonas savastanoi pv. phaseolicola |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutarate + O2 | - |
Pseudomonas savastanoi pv. phaseolicola | ethylene + 3 CO2 + H2O | - |
? | |
2-oxoglutarate + O2 | - |
Pseudomonas savastanoi pv. phaseolicola PK2 | ethylene + 3 CO2 + H2O | - |
? | |
additional information | cf. EC 1.14.11.34, reaction via 5-hydroxyarginine. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylene production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated | Pseudomonas savastanoi pv. phaseolicola | ? | - |
? | |
additional information | cf. EC 1.14.11.34, reaction via 5-hydroxyarginine. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylene production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated | Pseudomonas savastanoi pv. phaseolicola PK2 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 40000, recombinant detagged enzyme, SDS-PAGE, 1 * 39670, recombinant detagged enzyme, mass spectrometry | Pseudomonas savastanoi pv. phaseolicola |
Synonyms | Comment | Organism |
---|---|---|
ethylene-forming enzyme | - |
Pseudomonas savastanoi pv. phaseolicola |
More | cf. EC 1.14.11.34 | Pseudomonas savastanoi pv. phaseolicola |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas savastanoi pv. phaseolicola |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7.5 | broad optimum | Pseudomonas savastanoi pv. phaseolicola |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | over 50% of maximal activity within this range | Pseudomonas savastanoi pv. phaseolicola |
General Information | Comment | Organism |
---|---|---|
evolution | ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily | Pseudomonas savastanoi pv. phaseolicola |
physiological function | the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2OG to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation | Pseudomonas savastanoi pv. phaseolicola |