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Information on EC 1.13.12.19 - 2-oxoglutarate dioxygenase (ethene-forming)
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1.13.12.19 2-oxoglutarate dioxygenase (ethene-forming)IUBMB Comments
This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 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 ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
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Word Map
- 1.13.12.19
-
1-aminocyclopropane-1-carboxylic
-
2og-feii
- syringae
-
climacteric
- carnation
-
dianthus
-
photoautotrophic
- biotechnology
- agriculture
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ethylene forming enzyme, 2og-fe(ii) oxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate-Fe(II) oxygenase
2OG-Fe(II) oxygenase
EFE
ethylene forming enzyme
ethylene-forming enzyme
additional information
ethylene-forming enzyme
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
-
-
-
-
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
reaction mechanism, overview
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2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
reaction mechanism, overview
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
reaction mechanism, overview
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
reaction mechanism, overview
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
mechanism of ethylene formation, and two-pathway reaction mechanism of EFE, structure-function relationship
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
Pseudomonas syringae ethylene-forming enzyme reveal a branched mechanism. In one branch, an apparently typical 2-oxoglutarate oxygenase reaction to give succinate, carbon dioxide, and sometimes pyrroline-5-carboxylate occurs, reaction of EC 1.13.11.34. Alternatively, Grob-type oxidative fragmentation of a 2-oxoglutarate-derived intermediate occurs to give ethylene and carbon dioxide, EC 1.13.12.19. Fragmentation to give ethylene is promoted by binding of L-arginine in a nonoxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene, relative to succinate formation. Induced fit reaction mechanism, detailed overview
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
mechanism of ethylene formation, and two-pathway reaction mechanism of EFE, structure-function relationship
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-
2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
reaction mechanism, overview
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-
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PATHWAY SOURCE
PATHWAYS
-
, ,
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SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethene-forming)
This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 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 ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + O2
ethylene + ?
presence of oxygen is essential for the ethylene forming reaction by EFE
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
2-oxoglutarate + O2
ethene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethene + 3 CO2 + H2O
in the other reaction [EC 1.14.20.7, 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. An iron(IV)-oxo intermediate initiates L-arginine oxidation but not ethylene production by the 2-oxoglutarate-dependent oxygenase, ethylene-forming enzyme
-
-
?
2-oxoglutarate + O2
ethene + 3 CO2 + H2O
in the other reaction [EC 1.14.20.7, 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 reaction mechanism of the enzyme (EFE) is studied with QM/MM methods. Based on the results, a branched pathway for the enzyme that can lead either to ethylene or to succinate via L-Arg hydroxylation is proposed. After formation of the Fe-O2 species, the nucleophilic attack of distal oxygen on the keto carbon of 2-oxoglutarate is accompanied by the breaking of the C1-C2 bond in 2-oxoglutarate, leading to an FeII-peroxysuccinate complex with a dissociated CO2. This FeII-peroxysuccinate species serves as the branch point intermediate in the dual transformations by EFE. It can proceed in two directions. In one branch, the subsequent O-O bond cleavage generates the succinate-bound FeIV-oxo intermediate. Next a nearby water molecule binds to the iron to form a hexacoordinated FeIV-oxo intermediate. Hydrogen atom abstraction from L-Arg, hydroxyl radical rebound, and elimination of guanidine from the hydroxylated L-Arg product complete the cycle. This represents the well-established mechanism for substrate oxidation by Fe/2OG oxygenases. Alternatively, starting from FeII-peroxysuccinate, the CO2 insertion into the Fe-O bond gives a peroxic anhydride species. Further steps, including the water binding, O-O bond cleavage, intermolecular proton transfer, and two consecutive C-C bond breaking steps, result in the formation of ethylene. According to the proposed reaction mechanism of EFE, a competition between the CO2 insertion and the O-O bond cleavage from the branch point intermediate governs the product selectivity. The calculated reaction barriers show a preference for the CO2 insertion reaction
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
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-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
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-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
ethylene forming reaction
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-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
the enzyme is dependent on 2-oxoglutarate
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
ethylene forming reaction
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-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
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-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
enzyme is highly specific for substrate 2-oxoglutarate
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-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34, reaction, mechanism of the two reaction catalyzed at the same time, overview. Enzyme EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34, reaction, mechanism of the two reaction catalyzed at the same time, overview. Enzyme EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
additional information
?
-
cf. EC 1.14.11.34, reaction via 5-hydroxyarginine. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylene production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated
-
-
?
additional information
?
-
Pseudomonas syringae ethylene-forming enzyme reveal a branched mechanism. In one branch, an apparently typical 2-oxoglutarate oxygenase reaction to give succinate, carbon dioxide, and sometimes pyrroline-5-carboxylate occurs, reaction of EC 1.13.11.34. Alternatively, Grob-type oxidative fragmentation of a 2-oxoglutarate-derived intermediate occurs to give ethylene and carbon dioxide, EC 1.13.12.19. Fragmentation to give ethylene is promoted by binding of L-arginine in a nonoxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene, relative to succinate formation. Role for Tyr192 in catalysis, substrate binding structures, structure-function analysis, overview
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-
?
additional information
?
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substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg
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-
?
additional information
?
-
cf. EC 1.14.11.34, reaction via 5-hydroxyarginine. Selected L-Arg derivatives induce ethylene formation without undergoing hydroxylation, demonstrating that ethylene production and L-Arg hydroxylation activities are not linked. Enzyme EFE utilizes the alternative 2-oxo acid 2-oxoadipate as a cosubstrate (forming glutaric acid) during the hydroxylation of L-Arg, with this reaction unlinked from ethylene formation. The amount of ethylene produced is more than twice the levels of succinate, L-DELTA1-pyrroline-5-carboxylate, or guanidine generated
-
-
?
additional information
?
-
substrate binding structures, crystal structure analysis, overview. In all cases of bound 2-oxoglutarate, the carboxylate distal to the metal is stabilized by a salt bridge with R277, and the carboxylate coordinating the metal is stabilized by hydrogen bonds with R171. The C1-carboxylate oxygen of 2-oxoglutarate binds approximately trans to the distal H268 and the C2-oxo oxygen binds opposite D191. L-Arg binds near, but does not coordinate, the metal center in EFE-Mn-2OG-L-Arg
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
presence of 2-oxoglutarate, L-arginine, Fe2+ and oxygen is essential for the enzymic reaction
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
2-oxoglutarate + O2
ethene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
-
-
-
?
2-oxoglutarate + O2
ethylene + 3 CO2 + H2O
-
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
-
cf. EC 1.14.11.34
-
-
?
3 2-oxoglutarate + L-arginine + 3 O2
2 C2H4 + succinate + 7 CO2 + 3 H2O + guanidine + L-DELTA1-pyrroline-5-carboxylate
cf. EC 1.14.11.34
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
dependent on, required for catalysis
Fe2+
dependent on, required for catalysis. The overall metal-binding mode of PsEFE is relatively typical for 2OG oxygenases, with the metal coordinated by His189 (C terminus of DSBH II), Asp191 (loop linking DSBH II and III), and His268 (N-terminus of DSBH VII)
Fe2+
dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
Fe2+
non-heme Fe(II)-dependent ethylene-forming enzyme, the metal ion is hexa-coordinated
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+
-
the nonheme iron(II) oxygenase catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinate and CO2 to generate a highly reactive iron species that hydroxylates a specific alkane C-H bond, in this case targeting L-arginine (Arg) for hydroxylation
Fe2+
dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,5-dihydroxy-1,3-benzene disulfonic acid
1 mM, 0.8% residual activity
N-oxalylglycine
an unreactive 2-oxoglutarate analogue, enzyme binding structure analysis, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arginine
highly specific for cofactor L-arginine, KM value 0.018 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
over 50% of maximal activity within this range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
gene is encoded by an indigenous plasmid, designated pPSP1; pv. phaseolicola PK2
UniProt
brenda
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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
emzyme PsEFE should be regarded as a hybrid of subgroups I and II, in terms of its classification
evolution
enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases
evolution
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases, overview
evolution
the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases,overview
evolution
-
ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily
-
evolution
-
enzyme EFE is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. It contains a double-stranded beta-helix (DSBH, also known as the jellyroll or cupin fold) core typically found in members of the Fe(II)/2OG-dependent oxygenases
-
metabolism
-
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
analysis enzyme EFE reaction and cellular carbon flux, overview
metabolism
-
analysis enzyme EFE reaction and cellular carbon flux, overview
-
physiological function
a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
physiological function
-
in the presence of O2, the enzyme catalyzes ethylene formation from the substrates 2-oxoglutarate and L-arginine
physiological function
the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2OG to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation
physiological function
the ethylene-forming enzyme (Efe) from Pseudomonas syringae pv. phaseolicola PK2 (the Kudzu strain) catalyzes the conversion of the ubiquitous tricarboxylic acid cycle intermediate 2-oxoglutarate into ethylene
physiological function
-
the enzyme is reported to simultaneously catalyze the conversion of 2OG into ethylene plus three CO2 and the Cdelta hydroxylation of L-arginine (L-Arg) while oxidatively decarboxylating 2OG to form succinate and carbon dioxide. The enzyme produces ethylene, a gas that is widely used as a building block in the production of various plastics, detergents, surfactants, antifreeze, solvents, and other important industrial materials. And ethylene is a plant hormone that plays an important role in growth and development. The ethylene-forming reaction is not intrinsically linked to L-Arg hydroxylation
-
physiological function
-
a non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme, EFE converts 2-oxoglutarate into ethylene plus three CO2 molecules while also catalyzing the C5 hydroxylation of L-arginine driven by the oxidative decarboxylation of 2-oxoglutarate to form succinate and CO2
-
physiological function
-
the ethylene-forming enzyme (Efe) from Pseudomonas syringae pv. phaseolicola PK2 (the Kudzu strain) catalyzes the conversion of the ubiquitous tricarboxylic acid cycle intermediate 2-oxoglutarate into ethylene
-
additional information
three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
additional information
three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand
Show AA Sequence and Transmembrane Helices (2077 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
39370
recombinant detagged enzyme, gel filtration
42000
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