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Literature summary for 1.14.20.7 extracted from

  • Martinez, S.; Hausinger, R.P.
    Biochemical and spectroscopic characterization of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2 (2016), Biochemistry, 55, 5989-5999 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
ascorbate required Pseudomonas savastanoi pv. phaseolicola

Cloned(Commentary)

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.031
-
2-oxoadipate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola
0.05
-
L-arginine with 2-oxoglutarate as cosubstrate, at pH 7.5 and 25°C Pseudomonas savastanoi pv. phaseolicola
0.057
-
2-oxoglutarate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola
0.071
-
L-arginine with 2-oxoadipate as cosubstrate, at pH 7.5 and 25°C Pseudomonas savastanoi pv. phaseolicola

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on, required for catalysis Pseudomonas savastanoi pv. phaseolicola

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39370
-
recombinant detagged enzyme, gel filtration Pseudomonas savastanoi pv. phaseolicola

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + L-arginine + O2 Pseudomonas savastanoi pv. phaseolicola
-
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?
2-oxoglutarate + L-arginine + O2 Pseudomonas savastanoi pv. phaseolicola PK2
-
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas savastanoi pv. phaseolicola P32021 i.e. Kudzu strain
-
Pseudomonas savastanoi pv. phaseolicola PK2 P32021 i.e. Kudzu strain
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O reaction mechanism Pseudomonas savastanoi pv. phaseolicola

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoadipate + L-arginine + O2
-
Pseudomonas savastanoi pv. phaseolicola glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?
2-oxoadipate + L-arginine + O2
-
Pseudomonas savastanoi pv. phaseolicola PK2 glutarate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?
2-oxoglutarate + L-arginine + O2
-
Pseudomonas savastanoi pv. phaseolicola succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?
2-oxoglutarate + L-arginine + O2
-
Pseudomonas savastanoi pv. phaseolicola PK2 succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
?
additional information cf. EC 1.13.12.19, ethylene production. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylen 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 1.13.12.19, ethylene production. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylen 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

Subunits Comment Organism
monomer 1 * 40000, recombinant detagged enzyme, SDS-PAGE, 1 * 39670, recombinant detagged enzyme, mass spectrometry Pseudomonas savastanoi pv. phaseolicola

Synonyms

Synonyms Comment Organism
2-oxoglutarate-Fe(II) oxygenase
-
Pseudomonas savastanoi pv. phaseolicola
2OG-Fe(II) oxygenase
-
Pseudomonas savastanoi pv. phaseolicola
EFE
-
Pseudomonas savastanoi pv. phaseolicola
ethylene-forming enzyme
-
Pseudomonas savastanoi pv. phaseolicola
More cf. EC 1.13.12.19 Pseudomonas savastanoi pv. phaseolicola

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas savastanoi pv. phaseolicola

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0042
-
2-oxoadipate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola
0.0045
-
L-arginine with 2-oxoadipate as cosubstrate, at pH 7.5 and 25°C Pseudomonas savastanoi pv. phaseolicola
0.048
-
L-arginine at pH 7.5 and 25°C Pseudomonas savastanoi pv. phaseolicola
2.067
-
2-oxoglutarate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7.5 broad optimum Pseudomonas savastanoi pv. phaseolicola

pH Range

pH Minimum pH Maximum Comment Organism
6 9 over 50% of maximal activity within this range Pseudomonas savastanoi pv. phaseolicola

General Information

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 2-oxoglutarate 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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.134
-
2-oxoadipate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola
0.97
-
L-arginine at pH 7.5 and 25°C Pseudomonas savastanoi pv. phaseolicola
36.26
-
2-oxoglutarate pH 7.5, 25°C, recombinant enzyme Pseudomonas savastanoi pv. phaseolicola