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Information on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming) and Organism(s) Pseudomonas savastanoi pv. glycinea and UniProt Accession Q7BS32

for references in articles please use BRENDA:EC1.13.12.19
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IUBMB Comments
This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and L-hydroxyarginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.The enzymes catalyse two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
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This record set is specific for:
Pseudomonas savastanoi pv. glycinea
UNIPROT: Q7BS32
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The taxonomic range for the selected organisms is: Pseudomonas savastanoi pv. glycinea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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2-oxoglutarate
+
O2
=
ethene
+
3
CO2
+
H2O
+
=
+
3
+
Synonyms
ethylene forming enzyme, 2og-fe(ii) oxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoglutarate-Fe(II) oxygenase
-
additional information
cf. EC 1.14.11.34
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
show the reaction diagram
reaction mechanism, overview
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethene-forming)
This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and L-hydroxyarginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.The enzymes catalyse two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
show the reaction diagram
cf. EC 1.14.11.34
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
show the reaction diagram
cf. EC 1.14.11.34
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
dependent on, required for catalysis
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EFE_PSESG
350
0
39376
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene efe, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
EFE is a promising biotechnology target because the expression of a single gene is sufficient for ethylene production in the absence of toxic intermediates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eckert, C.; Xu, W.; Xiong, W.; Lynch, S.; Ungerer, J.; Tao, L.; Gill, R.; Maness, P.; Yu, J.
Ethylene-forming enzyme and bioethylene production
Biotechnol. Biofuels
7
33
2014
Penicillium digitatum, Pseudomonas savastanoi pv. glycinea (Q7BS32), Pseudomonas savastanoi pv. phaseolicola (P32021), Pseudomonas savastanoi pv. phaseolicola PK2 (P32021), Ralstonia solanacearum (Q8XPV7)
Manually annotated by BRENDA team