Information on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethylene-forming)

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The expected taxonomic range for this enzyme is: Pseudomonas syringae

EC NUMBER
COMMENTARY
1.13.12.19
-
RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate dioxygenase (ethylene-forming)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate + O2 = ethylene + 3 CO2 + H2O
show the reaction diagram
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-
-
-
PATHWAY
KEGG Link
MetaCyc Link
ethylene biosynthesis II (microbes)
-
ethylene biosynthesis IV
-
ethylene biosynthesis V
-
ethylene forming enzyme
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SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming)
This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.11.34, 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 ethylene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethylene and succinate is 2:1.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ethylene-forming enzyme
P32021
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene is encoded by an indigenous plasmid, designated pPSP1; pv. phaseolicola PK2
UniProt
Manually annotated by BRENDA team
pv. phaseolicola PK2
UniProt
Manually annotated by BRENDA team
pv. phaseolicola PK2, enzyme catalyzes the formation of ethylene and succinate from 2-oxoglutarate, reactions of EC 1.13.12.19 and EC 1.14.11.34
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
show the reaction diagram
P32021
enzyme is highly specific for substrate 2-oxoglutarate
-
-
?
2-oxoglutarate + O2
ethylene + ?
show the reaction diagram
P32021
presence of oxygen is essential for the ethylene forming reaction by EFE
-
-
?
additional information
?
-
P32021
enzyme catalyzes the formation of ethylene and succinate from 2-oxoglutarate, at a molar ratio of 2:l, reactions of EC 1.13.12.19 and EC 1.14.11.34. In the main reaction, 2-oxoglutarate is dioxygenated to produce one molecule of ethylene and three molecules of carbon dioxide. In the sub-reaction, both 2-oxoglutarate and L-arginine are mono-oxygenated to yield succinate plus carbon dioxide and L-hydroxyarginine, respectively, the latter being further transformed to guanidine and L-delta-pyrroline-5-carboxylate. Dual-circuit mechanism for the entire reaction is proposed, in which the binding of L-arginine and 2-oxoglutarate in a Schiff-base structure generates a common intermediate for two reactions
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-
-
additional information
?
-
P32021
presence of 2-oxoglutarate, L-arginine, Fe2+ and oxygen is essential for the enzymic reaction
-
-
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
at the active site, enzyme acts as a bidentate ligand and it forms a complex with Fe2+. The Fe2+ is further coordinated to a tridentate Schiff base of 2-oxoglutarate and L-arginine, whose terminal carboxylate and guanidino groups are trapped by binding sites I and II on the enzyme, respectively
Fe2+
P32021
required, KM value 0.059 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,5-Dihydroxy-1,3-benzene disulfonic acid
P32021
1 mM, 0.8% residual activity
5,5'-dithio-bis(2-nitrobenzoate)
P32021
1 mM, 0.7% residual activity
CoCl2
P32021
1 mM, 20% residual activity
CuSO4
P32021
1 mM, 50% residual activity
EDTA
P32021
1 mM, 1% residual activity
H2O2
P32021
1 mM, 0.7% residual activity
MnCl2
P32021
1 mM, 6% residual activity
n-propyl gallate
P32021
1 mM, 1% residual activity
Sodium azide
P32021
1 mM, 90% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
D-Arginine
P32021
3% of the activity with L-arginine
L-arginine
P32021
highly specific for cofactor L-arginine, KM value 0.018 mM
L-canavanine sulfate
P32021
7% of the activity with L-arginine
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.006
-
2-oxoglutarate
-
mutant H305Q, pH 8.0, 25C
0.007
-
2-oxoglutarate
-
mutant H168Q, pH 8.0, 25C; mutant H284Q, pH 8.0, 25C
0.008
-
2-oxoglutarate
-
mutant H335Q, pH 8.0, 25C
0.01
-
2-oxoglutarate
-
mutant H309Q, pH 8.0, 25C
0.011
-
2-oxoglutarate
-
mutant H169Q, pH 8.0, 25C
0.013
-
2-oxoglutarate
-
wild-type, pH 8.0, 25C
0.015
-
2-oxoglutarate
-
mutant H116Q, pH 8.0, 25C
0.019
-
2-oxoglutarate
P32021
pH 8.0, 25C
0.033
-
2-oxoglutarate
-
mutant H268Q, pH 8.0, 25C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.009
-
2-oxoglutarate
-
mutant H268Q, pH 8.0, 25C
0.01
-
2-oxoglutarate
-
mutant H284Q, pH 8.0, 25C
0.012
-
2-oxoglutarate
-
mutant H116Q, pH 8.0, 25C
0.015
-
2-oxoglutarate
-
mutant H168Q, pH 8.0, 25C
0.017
-
2-oxoglutarate
-
mutant H309Q, pH 8.0, 25C
0.047
-
2-oxoglutarate
-
mutant H169Q, pH 8.0, 25C
0.2
-
2-oxoglutarate
-
mutant H305Q, pH 8.0, 25C
0.3
-
2-oxoglutarate
-
mutant H335Q, pH 8.0, 25C
0.5
-
2-oxoglutarate
-
wild-type, pH 8.0, 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.27
-
2-oxoglutarate
-
mutant H268Q, pH 8.0, 25C
2883
0.8
-
2-oxoglutarate
-
mutant H116Q, pH 8.0, 25C
2883
1.43
-
2-oxoglutarate
-
mutant H284Q, pH 8.0, 25C
2883
1.67
-
2-oxoglutarate
-
mutant H309Q, pH 8.0, 25C
2883
2.14
-
2-oxoglutarate
-
mutant H168Q, pH 8.0, 25C
2883
4.24
-
2-oxoglutarate
-
mutant H169Q, pH 8.0, 25C
2883
33.3
-
2-oxoglutarate
-
mutant H305Q, pH 8.0, 25C
2883
37.5
-
2-oxoglutarate
-
mutant H335Q, pH 8.0, 25C
2883
38.5
-
2-oxoglutarate
-
wild-type, pH 8.0, 25C
2883
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
660
-
P32021
pH 8.0, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
P32021
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
P32021
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
P32021
isoelectric focusing
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36000
-
P32021
gel filtration
36000
-
P32021
gel fitlration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
P32021
1 * 39444, calculated, 1 * 42000, SDS-PAGE
monomer
P32021
1 * 42000, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
P32021
stable below
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
from cell-free extract
P32021
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Nicotiana tabacum
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H116Q
-
kcat value decreases to 2.4% of wild-type. Mutant is more thermolabile than wild-type
H168Q
-
kcat value decreases to 3% of wild-type. Mutant is more thermolabile than wild-type
H169Q
-
kcat value decreases to 9.3% of wild-type. Mutant is more thermolabile than wild-type
H189Q
-
complete loss of activity
H233Q
-
complete loss of activity
H268Q
-
kcat value decreases to 1.8% of wild-type
H284Q
-
kcat value decreases to 2% of wild-type. Mutant is more thermolabile than wild-type
H305Q
-
kcat value decreases to 40% of wild-type
H309Q
-
kcat value decreases to 3.3% of wild-type. Mutant is more thermolabile than wild-type
H335Q
-
kcat value decreases to 60% of wild-type
additional information
-
introduction of a gene encoding a chimeric protein consisting of EFE and beta-glucuronidase GUS into the tobacco genome using a binary vector which directs expression of the EFE-GUS fusion protein under the control of constitutive promoter of cauliflower mosaic virus 35S RNA
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
introduction of a gene encoding a chimeric protein consisting of EFE and beta-glucuronidase GUS into the tobacco genome using a binary vector which directs expression of the EFE-beta-glucuronidase fusion protein under the control of constitutive promoter of cauliflower mosaic virus 35S RNA. Transgenic plants produce ethylene at consistently higher rates than the untransformed plant, and their beta-glucuronidase activities are expressed in different tissues. A significant dwarf morphology observed in the transgenic tobacco displaying the highest ethylene production resembles the phenotype of a wild-type plant exposed to excess ethylene