1.13.12.19: 2-oxoglutarate dioxygenase (ethene-forming)
This is an abbreviated version!
For detailed information about 2-oxoglutarate dioxygenase (ethene-forming), go to the full flat file.
Word Map on EC 1.13.12.19
-
1.13.12.19
-
1-aminocyclopropane-1-carboxylic
-
2og-feii
-
syringae
-
climacteric
-
carnation
-
dianthus
-
photoautotrophic
-
biotechnology
-
agriculture
-
synthesis
- 1.13.12.19
-
1-aminocyclopropane-1-carboxylic
-
2og-feii
- syringae
-
climacteric
- carnation
-
dianthus
-
photoautotrophic
- biotechnology
- agriculture
- synthesis
Reaction
Synonyms
2-oxoglutarate-Fe(II) oxygenase, 2OG-Fe(II) oxygenase, EFE, ethylene forming enzyme, ethylene-forming enzyme, More, PsEFE
ECTree
Advanced search results
General Information
General Information on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
metabolism
physiological function
additional information
emzyme PsEFE should be regarded as a hybrid of subgroups I and II, in terms of its classification
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
evolution
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases, overview
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases,overview
evolution
-
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
-
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
-
-
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
-
analysis enzyme EFE reaction and cellular carbon flux, overview
-
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
physiological function
-
in the presence of O2, the enzyme catalyzes ethylene formation from the substrates 2-oxoglutarate and L-arginine
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
physiological function
the ethylene-forming enzyme (Efe) from Pseudomonas syringae pv. phaseolicola PK2 (the Kudzu strain) catalyzes the conversion of the ubiquitous tricarboxylic acid cycle intermediate 2-oxoglutarate into ethylene
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
-
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
-
physiological function
-
the ethylene-forming enzyme (Efe) from Pseudomonas syringae pv. phaseolicola PK2 (the Kudzu strain) catalyzes the conversion of the ubiquitous tricarboxylic acid cycle intermediate 2-oxoglutarate into ethylene
-
three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
additional information
three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand