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Information on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming) and Organism(s) Pseudomonas syringae pv. pisi and UniProt Accession Q9Z3T0

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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Pseudomonas syringae pv. pisi
UNIPROT: Q9Z3T0
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The taxonomic range for the selected organisms is: Pseudomonas syringae pv. pisi
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
ethylene forming enzyme
-
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
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
show the reaction diagram
-
-
-
?
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
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EFE_PSESJ
337
0
38064
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A199G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C280F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D191A
site-directed mutagenesis, inactive mutant
E235D
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F278Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H189A
site-directed mutagenesis, inactive mutant
H233A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H268A
site-directed mutagenesis, inactive mutant
I254M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
I304N
site-directed mutagenesis, inactive mutant
I322V
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L22M
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
R236S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V172T
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
V212Y/E213S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
a loop deletion mutant is inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons with Pseudomonas digitatum and Pseudomonas chrysogenum, recombinant expression in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johansson, N.; Persson, K.; Norbeck, J.; Larsson, C.
Expression of NADH-oxidases enhances ethylene productivity in Saccharomyces cerevisiae expressing the bacterial EFE
Biotechnol. Bioprocess Eng.
22
195-199
2017
Pseudomonas savastanoi pv. phaseolicola (P32021), Pseudomonas syringae pv. pisi (Q9Z3T0)
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Manually annotated by BRENDA team