EC Tree |
1. Oxidoreductases |
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases) |
1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases) |
ID: | 1.13.12.19 |
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Description: | 2-oxuglutarate dioxygenase (ethene-forming). |
Alternative Name: |
Ethylene-forming enzyme. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.13.12.19 |
BRENDA Enzyme Link: | BRENDA 1.13.12.19 |
KEGG Enzyme Link: | KEGG1.13.12.19 |
BioCyc Enzyme Link: | BioCyc 1.13.12.19 |
ExPASy Enzyme Link: | ExPASy1.13.12.19 |
EC2PDB Enzyme Link: | EC2PDB 1.13.12.19 |
ExplorEnz Enzyme Link: | ExplorEnz 1.13.12.19 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.13.12.19 |
IntEnz Enzyme Link: | IntEnz 1.13.12.19 |
MEDLINE Enzyme Link: | MEDLINE 1.13.12.19 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:31523 | 2-oxoglutarate + 2 H(+) + O2 = 3 CO2 + ethene + H2O |
RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[CH2;+0:6]-[CH2;+0:7]-[C;H0;+0:8](=[*:9])-[OH;+0:10].[H+;H0:11].[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:9]=[C;H0;+0:8]=[O;H0;+0:10].[*:5]=[C;H0;+0:4]=[O;H0;+0:13].[CH2;+0:6]=[CH2;+0:7].[OH2;+0:14] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. | Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, Morino Y, Fukuda H | 1991 Oct | 1770346 |
Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. | Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, Omata T, Inoue Y, Tanase S, Morino Y | 1992 Oct 30 | 1445325 |
Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. | Fukuda H, Ogawa T, Tazaki M, Nagahama K, Fujii T, Tanase S, Morino Y | 1992 Oct 30 | 1445291 |