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 hide
1.14.11.34
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RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + L-arginine + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
overall reaction
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2-oxoglutarate + L-arginine + O2 = succinate + CO2 + L-hydroxyarginine
show the reaction diagram
(1a)
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L-hydroxyarginine = guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
(1b)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene biosynthesis IV (engineered)
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ethylene forming enzyme
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from Mangifera indica fruits
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate
show the reaction diagram
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?
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
additional information
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
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 hide
LITERATURE
IMAGE
0.006 - 0.033
2-oxoglutarate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.5
2-oxoglutarate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 38.5
2-oxoglutarate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cell-free extract
recombinant enzyme
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recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H116Q
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kcat value decreases to 2.4% of wild-type. Mutant is more thermolabile than wild-type
H168Q
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kcat value decreases to 3% of wild-type. Mutant is more thermolabile than wild-type
H169Q
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kcat value decreases to 9.3% of wild-type. Mutant is more thermolabile than wild-type
H189Q
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complete loss of activity
H233Q
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complete loss of activity
H268Q
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kcat value decreases to 1.8% of wild-type
H284Q
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kcat value decreases to 2% of wild-type. Mutant is more thermolabile than wild-type
H305Q
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kcat value decreases to 40% of wild-type
H309Q
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kcat value decreases to 3.3% of wild-type. Mutant is more thermolabile than wild-type
H335Q
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kcat value decreases to 60% of wild-type