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Literature summary for 1.13.12.19 extracted from

  • Martinez, S.; Fellner, M.; Herr, C.Q.; Ritchie, A.; Hu, J.; Hausinger, R.P.
    Structures and mechanisms of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme Substrate binding creates a twist (2017), J. Am. Chem. Soc., 139, 11980-11988 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.12.19

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes Pseudomonas savastanoi pv. phaseolicola

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structure of the enzyme in complex with several ligands, detailed overview Pseudomonas savastanoi pv. phaseolicola

Protein Variants

Protein Variants Comment Organism
A198V site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene Pseudomonas savastanoi pv. phaseolicola
A281V site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
F283A site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production Pseudomonas savastanoi pv. phaseolicola
F283R site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production Pseudomonas savastanoi pv. phaseolicola
F283V site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production Pseudomonas savastanoi pv. phaseolicola
F283Y site-directed mutagenesis, replacing F283 by tryptophan, tyrosine, arginine, alanine, and valine leads to the near elimination of ethylene production Pseudomonas savastanoi pv. phaseolicola
H116Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
H169Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
H233Q site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
H284Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
H309Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
R171A site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene Pseudomonas savastanoi pv. phaseolicola
R277A site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola
V196F site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola

Inhibitors

Inhibitors Comment Organism Structure
N-oxalylglycine
-
 Pseudomonas savastanoi pv. phaseolicola

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ non-heme Fe(II)-dependent ethylene-forming enzyme, the metal ion is hexa-coordinated Pseudomonas savastanoi pv. phaseolicola

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Pseudomonas savastanoi pv. phaseolicola P32021
-
-
Pseudomonas savastanoi pv. phaseolicola PK2 P32021
-
-

Reaction

Reaction Comment Organism Reaction ID
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O mechanism of ethylene formation, and two-pathway reaction mechanism of EFE, structure-function relationship Pseudomonas savastanoi pv. phaseolicola
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + O2
-
 Pseudomonas savastanoi pv. phaseolicola ethylene + 3 CO2 + H2O
-
 ?
2-oxoglutarate + O2 ethylene forming reaction Pseudomonas savastanoi pv. phaseolicola ethylene + 3 CO2 + H2O
-
 ?
2-oxoglutarate + O2
-
 Pseudomonas savastanoi pv. phaseolicola PK2 ethylene + 3 CO2 + H2O
-
 ?
2-oxoglutarate + O2 ethylene forming reaction Pseudomonas savastanoi pv. phaseolicola PK2 ethylene + 3 CO2 + H2O
-
 ?
3 2-oxoglutarate + L-arginine + 3 O2 cf. EC 1.14.11.34, reaction, mechanism of the two reaction catalyzed at the same time, overview. Enzyme EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2 Pseudomonas savastanoi pv. phaseolicola 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
 ?
3 2-oxoglutarate + L-arginine + 3 O2 cf. EC 1.14.11.34, reaction, mechanism of the two reaction catalyzed at the same time, overview. Enzyme EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2 Pseudomonas savastanoi pv. phaseolicola PK2 2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
 ?
additional information substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg Pseudomonas savastanoi pv. phaseolicola ?
-
 ?
additional information substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg Pseudomonas savastanoi pv. phaseolicola PK2 ?
-
 ?

Synonyms

Synonyms Comment Organism
EFE
-
 Pseudomonas savastanoi pv. phaseolicola
ethylene-forming enzyme
-
 Pseudomonas savastanoi pv. phaseolicola

General Information

General Information Comment Organism
evolution enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases Pseudomonas savastanoi pv. phaseolicola
physiological function a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2 Pseudomonas savastanoi pv. phaseolicola