KEGG   ENZYME: 1.14.20.7
Entry
EC 1.14.20.7                Enzyme                                 

Name
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming);
ethene-forming enzyme;
ethylene-forming enzyme;
EFE
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and the other dehydrogenated
Sysname
L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)
Reaction(IUBMB)
L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction) [RN:R09785];
(1a) L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + 5-hydroxy-L-arginine [RN:R10081];
(1b) 5-hydroxy-L-arginine = guanidine + (S)-1-pyrroline-5-carboxylate + H2O [RN:R10082]
Reaction(KEGG)
Substrate
L-arginine [CPD:C00062];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007];
5-hydroxy-L-arginine [CPD:C20330]
Product
succinate [CPD:C00042];
CO2 [CPD:C00011];
guanidine [CPD:C17349];
(S)-1-pyrroline-5-carboxylate [CPD:C03912];
H2O [CPD:C00001];
5-hydroxy-L-arginine [CPD:C20330]
Comment
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 (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide.The enzyme catalyses 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.
History
EC 1.14.20.7 created 2011 as EC 1.14.11.34, transferred 2018 to EC 1.14.20.7
Orthology
K21815  2-oxoglutarate dioxygenase / 2-oxoglutarate/L-arginine monooxygenase/decarboxylase
Genes
XOR: XOC_2500
RSO: RSp1529(efe)
RSL: RPSI07_mp1626(efe)
RSN: RSPO_m00454(efe)
RSM: CMR15_mp30178(efe)
RSE: F504_5001
RSY: RSUY_36440(efe)
RPU: CDC45_25315
MSD: MYSTI_05925
MFB: MFUL124B02_31745
SGE: DWG14_01175(efe_2)
AMD: AMED_9132
AMN: RAM_46840
AMM: AMES_8995
AMZ: B737_8996
 » show all
Reference
1  [PMID:1770346]
  Authors
Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, Morino Y, Fukuda H
  Title
Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2.
  Journal
J Gen Microbiol 137:2281-6 (1991)
DOI:10.1099/00221287-137-10-2281
  Sequence
Reference
2  [PMID:1445291]
  Authors
Fukuda H, Ogawa T, Tazaki M, Nagahama K, Fujii T, Tanase S, Morino Y
  Title
Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae.
  Journal
Biochem Biophys Res Commun 188:483-9 (1992)
DOI:10.1016/0006-291X(92)91081-Z
  Sequence
Reference
3  [PMID:1445325]
  Authors
Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, Omata T, Inoue Y, Tanase S, Morino Y
  Title
Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2.
  Journal
Biochem Biophys Res Commun 188:826-32 (1992)
DOI:10.1016/0006-291X(92)91131-9
  Sequence
Reference
4  [PMID:28780854]
  Authors
Martinez S, Fellner M, Herr CQ, Ritchie A, Hu J, Hausinger RP
  Title
Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates a Twist.
  Journal
J Am Chem Soc 139:11980-11988 (2017)
DOI:10.1021/jacs.7b06186
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.20.7
IUBMB Enzyme Nomenclature: 1.14.20.7
ExPASy - ENZYME nomenclature database: 1.14.20.7
BRENDA, the Enzyme Database: 1.14.20.7

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