Information on EC 1.14.11.34 - 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.14.11.34
-
RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
overall reaction
-
-
-
2-oxoglutarate + L-arginine + O2 = succinate + CO2 + L-hydroxyarginine
show the reaction diagram
(1a)
-
-
-
L-hydroxyarginine = guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
(1b)
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene biosynthesis IV
-
-
ethylene forming enzyme
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-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 1.13.12.19, 2-oxoglutarate dioxygenase (ethylene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethylene and three molecules of carbon dioxide. The enzyme catalyses 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
COMMENTARY
LITERATURE
2-oxoglutarate-dependent ethylene/succinate-forming enzyme
-
-
2-oxoglutarate-dependent oxygenase-type ethylene-forming-enzyme
-
-
ethylene forming enzyme
-
-
ethylene-forming enzyme
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from Mangifera indica fruits
-
-
Manually annotated by BRENDA team
enzyme catalyzes the formation of ethylene and succinate from 2-oxoglutarate, reactions of EC 1.13.12.19 and EC 1.14.11.34; pv. phaseolicola PK2
UniProt
Manually annotated by BRENDA team
gene is encoded by an indigenous plasmid, designated pPSP1; pv. phaseolicola PK2
UniProt
Manually annotated by BRENDA team
pv. phaseolicola
-
-
Manually annotated by BRENDA team
pv. phaseolicola PK2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
Fusarium mangiferae, a pathogen of Mangifera indica, is associated with mango malformation disease due to its stress ethylene production via the 2-oxoglutarate-dependent oxygenase-type ethylene-forming-enzyme (EFE) pathway, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
overall reaction, enzyme is highly specific for substrate 2-oxoglutarate. Presence of 2-oxoglutarate, L-arginine, Fe2+ and oxygen is essential for the enzymic reaction
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate
show the reaction diagram
-
-
-
?
additional information
?
-
-
in a few plant pathogens ethylene is synthesized by an ethylene forming enzyme in a complex multi-step reaction utilizing 2-oxoglutarate, arginine and dioxygen as substrates, resulting in the accumulation of ethylene in the headspace of closed vessels
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
-
-
-
?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
-
in a few plant pathogens ethylene is synthesized by an ethylene forming enzyme in a complex multi-step reaction utilizing 2-oxoglutarate, arginine and dioxygen as substrates, resulting in the accumulation of ethylene in the headspace of closed vessels
-
-
-
METALS and IONS
ORGANISM
UNIPROT
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 Schiffs 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+
required, KM value 0.059 mM
Fe2+
-
dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,5-dihydroxy-1,3-benzenedisulfonic acid
1 mM, 0.8% residual activity
5,5'-dithio-bis(2-nitrobenzoate)
1 mM, 0.7% residual activity
CoCl2
1 mM, 20% residual activity
CuSO4
1 mM, 50% residual activity
EDTA
1 mM, 1% residual activity
H2O2
1 mM, 0.7% residual activity
MnCl2
1 mM, 6% residual activity
n-propyl gallate
1 mM, 1% residual activity
Sodium azide
1 mM, 90% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Arginine
3% of the activity with L-arginine
L-arginine
highly specific for cofactor L-arginine, KM value 0.018 mM
L-canavanine sulfate
7% of the activity with L-arginine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
pH 8.0, 25C
0.033
2-oxoglutarate
-
mutant H268Q, pH 8.0, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
2-oxoglutarate
Pseudomonas syringae
-
mutant H268Q, pH 8.0, 25C
0.01
2-oxoglutarate
Pseudomonas syringae
-
mutant H284Q, pH 8.0, 25C
0.012
2-oxoglutarate
Pseudomonas syringae
-
mutant H116Q, pH 8.0, 25C
0.015
2-oxoglutarate
Pseudomonas syringae
-
mutant H168Q, pH 8.0, 25C
0.017
2-oxoglutarate
Pseudomonas syringae
-
mutant H309Q, pH 8.0, 25C
0.047
2-oxoglutarate
Pseudomonas syringae
-
mutant H169Q, pH 8.0, 25C
0.2
2-oxoglutarate
Pseudomonas syringae
-
mutant H305Q, pH 8.0, 25C
0.3
2-oxoglutarate
Pseudomonas syringae
-
mutant H335Q, pH 8.0, 25C
0.5
2-oxoglutarate
Pseudomonas syringae
-
wild-type, pH 8.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
2-oxoglutarate
Pseudomonas syringae
-
mutant H268Q, pH 8.0, 25C
34
0.8
2-oxoglutarate
Pseudomonas syringae
-
mutant H116Q, pH 8.0, 25C
34
1.43
2-oxoglutarate
Pseudomonas syringae
-
mutant H284Q, pH 8.0, 25C
34
1.67
2-oxoglutarate
Pseudomonas syringae
-
mutant H309Q, pH 8.0, 25C
34
2.14
2-oxoglutarate
Pseudomonas syringae
-
mutant H168Q, pH 8.0, 25C
34
4.24
2-oxoglutarate
Pseudomonas syringae
-
mutant H169Q, pH 8.0, 25C
34
33.3
2-oxoglutarate
Pseudomonas syringae
-
mutant H305Q, pH 8.0, 25C
34
37.5
2-oxoglutarate
Pseudomonas syringae
-
mutant H335Q, pH 8.0, 25C
34
38.5
2-oxoglutarate
Pseudomonas syringae
-
wild-type, pH 8.0, 25C
34
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
gel filtration
714009, 715784
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 39444, calculated, 1 * 42000, SDS-PAGE
monomer
1 * 42000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
stable below
715784
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cell-free extract
recombinant enzyme
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
gene efe, codon optimization, gene synthesis, and construction of the self-replicating wide-host-range pDF-series vectors, recombinant expression in Synechocystis sp. strain PCC 6803, the cyanobacterial system is highly unstable resulting in rapid development of mutants that lost the capability to synthesize ethylene, N-terminally His6-tagged enzyme expression in Escherichia coli. Ethylene synthesis in Escherichia coli and Synechocystis using three different metal-inducible promoters from cyanobacteria, expression rates and genomic structure of the native metal-inducible promoter elements, method development, overview
-
ENGINEERING
ORGANISM
UNIPROT
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