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: Bacteria, Eukaryota

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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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
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Manually annotated by BRENDA team
isolated from Mangifera indica fruits
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Manually annotated by BRENDA team
no activity in Penicillium chrysogenum
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Manually annotated by BRENDA team
PHI26
UniProt
Manually annotated by BRENDA team
pv. phaseolicola
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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-oxoadipate + L-arginine + O2
?
show the reaction diagram
2-oxoglutarate + agmatine + O2
?
show the reaction diagram
2-oxoglutarate + L-argininamide + O2
?
show the reaction diagram
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less than 1% activity compared to L-arginine
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?
2-oxoglutarate + L-arginine + O2
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
2-oxoglutarate + L-arginine + O2
succinate + CO2 + 5-hydroxy-L-arginine
show the reaction diagram
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
2-oxoglutarate + L-canavanine + O2
?
show the reaction diagram
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less than 1% activity compared to L-arginine
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?
2-oxoglutarate + L-homoarginine + O2
?
show the reaction diagram
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less than 1% activity compared to L-arginine
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?
2-oxoglutarate + L-ornithine + O2
?
show the reaction diagram
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less than 1% activity compared to L-arginine
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?
2-oxoglutarate + Ngamma-hydroxy-L-arginine + O2
?
show the reaction diagram
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15% activity compared to L-arginine
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?
2-oxoglutarate + O2
ethylene + CO2
show the reaction diagram
additional information
?
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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
ethylene + succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
2-oxoglutarate + L-arginine + O2
succinate + CO2 + 5-hydroxy-L-arginine
show the reaction diagram
2-oxoglutarate + L-arginine + O2
succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O
show the reaction diagram
2-oxoglutarate + O2
ethylene + CO2
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
ascorbate
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
0.031
2-oxoadipate
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at pH 7.5 and 25°C
0.006 - 0.057
2-oxoglutarate
0.05 - 0.071
L-arginine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042
2-oxoadipate
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at pH 7.5 and 25°C
0.009 - 2.07
2-oxoglutarate
0.0045 - 0.048
L-arginine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 38.5
2-oxoglutarate
0.97
L-arginine
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at pH 7.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
660
pH 8.0, 25°C
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
39444
1 * 39444, calculated, 1 * 42000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with manganese and 2-oxoglutarate, with manganese and the buffer bis-Tris-propane, and in complex with iron, L-Arg, and N-oxalylglycine, sitting drop vapor diffusion method, using 17.5-25% (w/v) polyethylene glycol (PEG) 3350 and 6000
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from cell-free extract
His-Trap column chromatography
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Ni-NTA agarose column chromatography
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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
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli MG1655 cells
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expressed in Saccharomyces cerevisiae strain SCNJ03
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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
A199G
the mutant shows reduced activity compared to the wild type enzyme
E235D
the mutant shows about wild type activity
F278Y
the mutant shows about wild type activity
I254M
the mutant shows about wild type activity
I304N
the mutant shows reduced activity compared to the wild type enzyme
I322V
the mutant shows about wild type activity
L22M
the mutant shows about wild type activity
V172T
the mutant shows about wild type activity
V212Y/E213S
the mutant shows reduced activity compared to the wild type enzyme
A198V
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the mutant shows about 60% of wild type activity
A199G
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the mutant shows reduced activity compared to the wild type enzyme
A218V
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the mutant shows about 3% of wild type activity
C317A
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the mutant shows about 34% of wild type activity
C317S
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the mutant shows about 21% of wild type activity
E213A
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the mutant shows about 90% of wild type activity
E213A/E215A
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the mutant shows about 5% of wild type activity
E215A
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the mutant shows about 5% of wild type activity
E235D
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the mutant shows about wild type activity
E285A
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the mutant shows about 10% of wild type activity
E285Q
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the mutant shows about 25% of wild type activity
F175Y
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the mutant shows about 18% of wild type activity
F278Y
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the mutant shows about wild type activity
F283A
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the mutant shows about 20% of wild type activity
F283R
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the mutant shows about 20% of wild type activity
F283V
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the mutant shows about 20% of wild type activity
F283W
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the mutant shows about 20% of wild type activity
F310R
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the mutant shows about 3% of wild type activity
F310W
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the mutant shows about 30% of wild type activity
I254M
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the mutant shows about wild type activity
I304N
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the mutant shows reduced activity compared to the wild type enzyme
I322V
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the mutant shows about wild type activity
L22M
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the mutant shows about wild type activity
L73K
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the mutant shows about 60% of wild type activity
L73R
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the mutant shows about 40% of wild type activity
R184A
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the mutant shows about 75% of wild type activity
R316A
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the mutant shows about 3.7% of wild type activity
R316K
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the mutant shows about 13% of wild type activity
S81R
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the mutant shows about 5% of wild type activity
S81Y
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the mutant shows about 5% of wild type activity
T86S
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the mutant shows about 31% of wild type activity
V172T
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the mutant shows about wild type activity
V212Y/E213S
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the mutant shows reduced activity compared to the wild type enzyme
V270T
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the mutant shows about 4.3 % of wild type activity
Y192F
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the mutant shows about 5.6% of wild type activity
Y306A
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the mutant shows about 3% of wild type activity
Y306F
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the mutant shows about 5% of wild type activity
Y318F
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the mutant shows about 65% of wild type activity
A198V
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the mutant shows about 60% of wild type activity
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E213A
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the mutant shows about 90% of wild type activity
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E215A
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the mutant shows about 5% of wild type activity
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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