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 ACCESSION NO.
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
2-oxoglutarate-dependent ethylene/succinate-forming enzyme
-
-
2-oxoglutarate-dependent oxygenase-type ethylene-forming-enzyme
-
-
ethylene forming enzyme
-
-
ethylene-forming enzyme
P32021
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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 ACCESSION NO.
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-pyrrolidine-5-carboxylate + H2O
show the reaction diagram
P32021
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
-
-
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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 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 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+
P32021
required, KM value 0.059 mM
Fe2+
-
dependent on
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,5-dihydroxy-l,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
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
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 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