Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.19 A198V site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 A281V site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 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
1.13.12.19 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
1.13.12.19 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
1.13.12.19 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
1.13.12.19 H116Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 H169Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 H233Q site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 H284Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 H309Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 R171A site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 R277A site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 V196F site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 A198V the mutant shows about 60% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 A198V site-directed mutagenesis, the mutant produces large amounts of L-DELTA1-pyrroline-5-carboxylate but very little ethylene Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 A218R inactive Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 A218V the mutant shows about 3% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 A281V site-directed mutagenesis, the mutant produces low levels of products in comparison to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 E213A the mutant shows about 90% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 E213A/E215A the mutant shows about 5% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 E215A the mutant shows about 5% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 E285A the mutant shows about 10% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 E285Q the mutant shows about 25% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 F283A the mutant shows about 20% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 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
1.14.20.7 F283R the mutant shows about 20% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 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
1.14.20.7 F283V the mutant shows about 20% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 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
1.14.20.7 F283W the mutant shows about 20% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 F283Y inactive Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 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
1.14.20.7 F310R the mutant shows about 3% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 F310W the mutant shows about 30% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 H116Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 H169Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 H233Q site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 H284Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 H309Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 L73K the mutant shows about 60% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 L73R the mutant shows about 40% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 R171A site-directed mutagenesis, the mutant is soluble, it produces no detectable ethylene Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 R184A the mutant shows about 75% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 R277A site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 S81R the mutant shows about 5% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 S81Y the mutant shows about 5% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 V196F inactive Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 V196F site-directed mutagenesis, the mutant is expressed in inclusion bodies Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 V196R inactive Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 Y306A the mutant shows about 3% of wild type activity Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 Y306F the mutant shows about 5% of wild type activity Pseudomonas savastanoi pv. phaseolicola

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.12.19 N-oxalylglycine
-
 Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 N-oxalylglycine
-
 Pseudomonas savastanoi pv. phaseolicola

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.19 2-oxoglutarate + O2 Pseudomonas savastanoi pv. phaseolicola
-
 ethylene + 3 CO2 + H2O
-
 ?
1.13.12.19 2-oxoglutarate + O2 Pseudomonas savastanoi pv. phaseolicola PK2
-
 ethylene + 3 CO2 + H2O
-
 ?
1.14.20.7 2-oxoglutarate + L-arginine + O2 Pseudomonas savastanoi pv. phaseolicola
-
 succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
 ?
1.14.20.7 2-oxoglutarate + L-arginine + O2 Pseudomonas savastanoi pv. phaseolicola
-
 succinate + CO2 + 5-hydroxy-L-arginine
-
 ?
1.14.20.7 2-oxoglutarate + O2 Pseudomonas savastanoi pv. phaseolicola
-
 ethylene + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.19 Pseudomonas savastanoi pv. phaseolicola P32021
-
-
1.13.12.19 Pseudomonas savastanoi pv. phaseolicola PK2 P32021
-
-
1.14.20.7 Pseudomonas savastanoi pv. phaseolicola P32021
-
-
1.14.20.7 Pseudomonas savastanoi pv. phaseolicola PK2 P32021
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.12.19 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
1.14.20.7 L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O two-pathway reaction mechanism of EFE, structure-function relationship Pseudomonas savastanoi pv. phaseolicola
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.19 2-oxoglutarate + O2
-
 Pseudomonas savastanoi pv. phaseolicola ethylene + 3 CO2 + H2O
-
 ?
1.13.12.19 2-oxoglutarate + O2 ethylene forming reaction Pseudomonas savastanoi pv. phaseolicola ethylene + 3 CO2 + H2O
-
 ?
1.13.12.19 2-oxoglutarate + O2
-
 Pseudomonas savastanoi pv. phaseolicola PK2 ethylene + 3 CO2 + H2O
-
 ?
1.13.12.19 2-oxoglutarate + O2 ethylene forming reaction Pseudomonas savastanoi pv. phaseolicola PK2 ethylene + 3 CO2 + H2O
-
 ?
1.13.12.19 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
-
 ?
1.13.12.19 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
-
 ?
1.13.12.19 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 ?
-
 ?
1.13.12.19 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 ?
-
 ?
1.14.20.7 2-oxoglutarate + L-arginine + O2
-
 Pseudomonas savastanoi pv. phaseolicola succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
-
 ?
1.14.20.7 2-oxoglutarate + L-arginine + O2
-
 Pseudomonas savastanoi pv. phaseolicola succinate + CO2 + 5-hydroxy-L-arginine
-
 ?
1.14.20.7 2-oxoglutarate + O2
-
 Pseudomonas savastanoi pv. phaseolicola ethylene + CO2
-
 ?
1.14.20.7 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
-
 ?
1.14.20.7 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 ?
-
 ?
1.14.20.7 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

EC Number Synonyms Comment Organism
1.13.12.19 EFE
-
 Pseudomonas savastanoi pv. phaseolicola
1.13.12.19 ethylene-forming enzyme
-
 Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 EFE
-
 Pseudomonas savastanoi pv. phaseolicola
1.14.20.7 ethylene-forming enzyme
-
 Pseudomonas savastanoi pv. phaseolicola

General Information

EC Number General Information Comment Organism
1.13.12.19 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
1.13.12.19 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
1.14.20.7 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
1.14.20.7 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