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Escherichia coli K-12 substr. MG1655 Enzyme: copper-containing amine oxidase



Gene: tynA Accession Numbers: EG13139 (EcoCyc), b1386, ECK1383

Synonyms: feaA, maoA

Regulation Summary Diagram: ?

Subunit composition of copper-containing amine oxidase = [TynA]2

Summary:
E. coli K-12 is capable of growth on phenylethylamine as the sole carbon and energy source. Phenylethylamine oxidase catalyzes the first step in the degradation pathway. This is a particular instance of a reaction catalyzed by the amine oxidase enzyme [Ferrandez97a, Parrott87]. In another instance, amine oxidase could hypothetically convert aminoacetone to methylglyoxal, similar to the eukaryotic semicarbazide-sensitive, Cu2+-dependent amine oxidases. This is predicted and discussed in pathway threonine degradation III (to methylglyoxal).

Amine oxidase catalyzes the conversion of an aliphatic amine to an aldehyde, followed by a two-electron reduction of O2 to H2O2 to regenerate the oxidized enzyme [MoenneLoccoz95]. It has been proven that the oxidase coded for by the maoA gene uses copper and topaquinone as prosthetic groups. The topaquinone is a part of the polypeptide chain [Cooper92] and is generated through the post-translational modification of a protein tyrosine residue, that occurs as a copper-dependent, probably autocatalytic reaction [MoenneLoccoz95, Hanlon95].

The enzyme has been crystallized [Roh94a] and its reaction mechanism studied by structural analysis [Wilmot97, Murray99, Wilmot99, Murray01, Mure05]. Structural studies using xenon as a probe have suggested that oxygen is likely to access the enzyme active site via a conserved β sandwich [Pirrat08]. In addition to copper at the catalytic center, there are two peripheral calcium ions bound per monomer [Parsons95]. Binding of metal ions at these peripheral sites is important for maximal enzyme activity [Smith10]. The roles of catalytically important residues such as Asp-383 and Tyr-381 have been studied by kinetic analysis using mutant enzymes [Saysell02, Kurtis11].

Under anaerobiosis, FNR activates tynA gene expression, but it is not known if this regulation is direct or indirect [Salmon03].

Gene Citations: [Steinebach96]

Locations: periplasmic space

Map Position: [1,447,100 <- 1,449,373] (31.19 centisomes)
Length: 2274 bp / 757 aa

Molecular Weight of Polypeptide: 84.379 kD (from nucleotide sequence), 80.0 kD (experimental) [Roh94 ]

Molecular Weight of Multimer: 143.0 kD (experimental) [Roh94]

Unification Links: ASAP:ABE-0004639 , CGSC:59 , DIP:DIP-11057N , EchoBASE:EB2934 , EcoGene:EG13139 , EcoliWiki:b1386 , ModBase:P46883 , OU-Microarray:b1386 , PortEco:tynA , PR:PRO_000024148 , Pride:P46883 , Protein Model Portal:P46883 , RefSeq:NP_415904 , RegulonDB:EG13139 , SMR:P46883 , String:511145.b1386 , UniProt:P46883

Relationship Links: InterPro:IN-FAMILY:IPR000269 , InterPro:IN-FAMILY:IPR012854 , InterPro:IN-FAMILY:IPR015798 , InterPro:IN-FAMILY:IPR015800 , InterPro:IN-FAMILY:IPR015801 , InterPro:IN-FAMILY:IPR015802 , InterPro:IN-FAMILY:IPR016182 , Panther:IN-FAMILY:PTHR10638 , PDB:Structure:1D6U , PDB:Structure:1D6Y , PDB:Structure:1D6Z , PDB:Structure:1DYU , PDB:Structure:1JRQ , PDB:Structure:1LVN , PDB:Structure:1OAC , PDB:Structure:1QAF , PDB:Structure:1QAK , PDB:Structure:1QAL , PDB:Structure:1SPU , PDB:Structure:2W0Q , PDB:Structure:2WGQ , PDB:Structure:2WO0 , PDB:Structure:2WOF , PDB:Structure:2WOH , Pfam:IN-FAMILY:PF01179 , Pfam:IN-FAMILY:PF02727 , Pfam:IN-FAMILY:PF02728 , Pfam:IN-FAMILY:PF07833 , Prosite:IN-FAMILY:PS01164 , Prosite:IN-FAMILY:PS01165

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0019607 - phenylethylamine catabolic process Inferred from experiment [Parrott87]
GO:0055114 - oxidation-reduction process Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Parrott87]
GO:0006559 - L-phenylalanine catabolic process Inferred by computational analysis [UniProtGOA12]
GO:0009308 - amine metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005507 - copper ion binding Inferred from experiment Inferred by computational analysis [GOA01a, Cooper92]
GO:0005509 - calcium ion binding Inferred from experiment [Parsons95]
GO:0008131 - primary amine oxidase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Parrott87]
GO:0042803 - protein homodimerization activity Inferred from experiment [Roh94]
GO:0048038 - quinone binding Inferred from experiment Inferred by computational analysis [GOA01a, Cooper92]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
GO:0052593 - tryptamine:oxygen oxidoreductase (deaminating) activity Inferred by computational analysis [GOA01]
GO:0052594 - aminoacetone:oxygen oxidoreductase(deaminating) activity Inferred by computational analysis [GOA01]
GO:0052595 - aliphatic-amine oxidase activity Inferred by computational analysis [GOA01]
GO:0052596 - phenethylamine:oxygen oxidoreductase (deaminating) activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Cooper92]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09, Azakami94]

MultiFun Terms: metabolism carbon utilization amines
metabolism carbon utilization amino acids
metabolism central intermediary metabolism threonine catabolism

Essentiality data for tynA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 16-Nov-2011 by Fulcher C , SRI International


Enzymatic reaction of: primary amine oxidase (copper-containing amine oxidase)

EC Number: 1.4.3.21

a primary amine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] <=> an aldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: phenylethylamine oxidase (copper-containing amine oxidase)

Synonyms: 2-phenylethylamine oxidase

EC Number: 1.4.3.21

2-phenylethylamine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] <=> phenylacetaldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of phenylethylamine degradation , phenylethylamine degradation I

Summary:
Purified, recombinant enzyme was shown to oxidize a variety of primary amines at differing relative rates, with tyramine (100%), phenylethylamine (96.1%) and tryptamine (88.3%) being highest. Diamines and polyamines were not oxidized [Roh94]. Note that some of the monoamine oxidase inhibitors shown here were assayed using tyramine as substrate [Roh94].

Cofactors or Prosthetic Groups: Cu2+ [Cooper92], topaquinone [Cooper92]

Inhibitors (Unknown Mechanism): pargyline [Roh94] , clorgyline [Roh94] , phenelzine [Roh94] , iproniazid [Roh94] , Hg2+ [Roh94] , hydroxylamine [Roh94] , isoniazid [Roh94] , semicarbazide [Hanlon95]


Enzymatic reaction of: aminoacetone oxidase (copper-containing amine oxidase)

EC Number: 1.4.3.21

aminoacetone[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] <=> methylglyoxal[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of threonine metabolism , threonine degradation III (to methylglyoxal)

Summary:
An early review described aminoacetone metabolism in Bacillus subtilis and Pseudomonas species and noted that "Preliminary results suggest that a number of microorganisms other than those mentioned here are capable of metabolizing aminoacetone by way of methylglyoxal." [Higgins67]. However, further description is lacking [Cooper84].


Enzymatic reaction of: amine oxidase

Synonyms: diamine oxidase, diamino oxhydrase, histiminase, amine:oxygen oxidoreductase (deaminating) (Cu containing), monoamine oxidase, aromatic amine oxidase

EC Number: 1.4.3.21

an aliphatic amine[periplasmic space] + H2O[periplasmic space] + oxygen[periplasmic space] <=> an aldehyde[periplasmic space] + ammonium[periplasmic space] + hydrogen peroxide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Alternative Substrates [Comment 5]:

Cofactors or Prosthetic Groups: topaquinone [Cooper92], Cu2+ [Cooper92]

Inhibitors (Unknown Mechanism): semicarbazide [Comment 6]


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 30
[Hanlon97, Yamashita96, Steinebach96, UniProt11a]
.
Chain 31 -> 757
[UniProt09]
UniProt: Primary amine oxidase;
Sequence-Conflict 33
[Yamashita96, UniProt10]
Alternate sequence: G → E; UniProt: (in Ref. 9; AA sequence);
Extrinsic-Sequence-Variant 42
[UniProt10]
Alternate sequence: K → E; UniProt: (in strain: W);
Extrinsic-Sequence-Variant 59
[UniProt10]
Alternate sequence: L → I; UniProt: (in strain: W);
Sequence-Conflict 248
[Azakami94a, UniProt10]
Alternate sequence: K → E; UniProt: (in Ref. 1; BAA04900);
Sequence-Conflict 258 -> 259
[Azakami94a, UniProt10]
Alternate sequence: GY → VI; UniProt: (in Ref. 1; BAA04900);
Sequence-Conflict 276
[Azakami94a, UniProt10]
Alternate sequence: I → II; UniProt: (in Ref. 1; BAA04900);
Sequence-Conflict 288
[Azakami94a, UniProt10]
Alternate sequence: A → missing; UniProt: (in Ref. 1);
Sequence-Conflict 290
[Azakami94a, UniProt10]
Alternate sequence: P → I; UniProt: (in Ref. 1);
Active-Site 413
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: probable;
Sequence-Conflict 456
[Azakami94a, UniProt10]
Alternate sequence: A → P; UniProt: (in Ref. 1; BAA04900);
Modified-Residue 496
[UniProt10]
UniProt: 2',4',5'-topaquinone;
Active-Site 496
[UniProt10]
UniProt: Schiff-base intermediate with substrate; via topaquinone;
Metal-Binding-Site 554
[UniProt10]
UniProt: Copper;
Metal-Binding-Site 556
[UniProt10]
UniProt: Copper;
Metal-Binding-Site 563
[UniProt10]
UniProt: Calcium 1;
Metal-Binding-Site 564
[UniProt10]
UniProt: Calcium 1; via carbonyl oxygen;
Metal-Binding-Site 565
[UniProt10]
UniProt: Calcium 1;
Metal-Binding-Site 603
[UniProt10]
UniProt: Calcium 2;
Sequence-Conflict 659
[Azakami94a, UniProt10]
Alternate sequence: H → D; UniProt: (in Ref. 1; BAA04900);
Metal-Binding-Site 700
[UniProt10]
UniProt: Calcium 2;
Metal-Binding-Site 702
[UniProt10]
UniProt: Calcium 2;
Metal-Binding-Site 708
[UniProt10]
UniProt: Calcium 1;
Metal-Binding-Site 709
[UniProt10]
UniProt: Calcium 1; via carbonyl oxygen;
Metal-Binding-Site 719
[UniProt10]
UniProt: Copper;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1386 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG13139.


References

Azakami94: Azakami H, Yamashita M, Roh JH, Suzuki H, Kumagai H, Murooka Y (1994). "Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli." Journal of Fermentation and Bioengineering 77(3):315-319.

Azakami94a: Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y. (1994). "Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli." J. Ferment. Bioeng., Volume 77, page(s) 315-319.

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Cooper84: Cooper RA (1984). "Metabolism of methylglyoxal in microorganisms." Annu Rev Microbiol 1984;38;49-68. PMID: 6093685

Cooper92: Cooper RA, Knowles PF, Brown DE, McGuirl MA, Dooley DM (1992). "Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12." Biochem J 1992;288 ( Pt 2);337-40. PMID: 1334402

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Ferrandez97a: Ferrandez A, Prieto MA, Garcia JL, Diaz E (1997). "Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli." FEBS Lett 1997;406(1-2);23-7. PMID: 9109378

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hanlon95: Hanlon SP, Carpenter K, Hassan A, Cooper RA (1995). "Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor." Biochem J 1995;306 ( Pt 3);627-30. PMID: 7702553

Hanlon97: Hanlon SP, Hill TK, Flavell MA, Stringfellow JM, Cooper RA (1997). "2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression." Microbiology 143 ( Pt 2);513-8. PMID: 9043126

Higgins67: Higgins IJ, Turner JM, Willetts AJ (1967). "Enzyme mechanism of aminoacetone metabolism by micro-organisms." Nature 215(5103);887-8. PMID: 4292865

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kurtis11: Kurtis CR, Knowles PF, Parsons MR, Gaule TG, Phillips SE, McPherson MJ (2011). "Tyrosine 381 in E. coli copper amine oxidase influences substrate specificity." J Neural Transm 118(7);1043-53. PMID: 21547391

MoenneLoccoz95: Moenne-Loccoz P, Nakamura N, Steinebach V, Duine JA, Mure M, Klinman JP, Sanders-Loehr J (1995). "Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy." Biochemistry 1995;34(21);7020-6. PMID: 7766611

Mure05: Mure M, Brown DE, Saysell C, Rogers MS, Wilmot CM, Kurtis CR, McPherson MJ, Phillips SE, Knowles PF, Dooley DM (2005). "Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase." Biochemistry 44(5);1568-82. PMID: 15683241

Murray01: Murray JM, Kurtis CR, Tambyrajah W, Saysell CG, Wilmot CM, Parsons MR, Phillips SE, Knowles PF, McPherson MJ (2001). "Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential." Biochemistry 40(43);12808-18. PMID: 11669617

Murray99: Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ (1999). "The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants." Biochemistry 38(26);8217-27. PMID: 10387067

Parrott87: Parrott S, Jones S, Cooper RA (1987). "2-Phenylethylamine catabolism by Escherichia coli K12." J Gen Microbiol 1987;133 ( Pt 2);347-51. PMID: 3309152

Parsons95: Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF (1995). "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution." Structure 3(11);1171-84. PMID: 8591028

Pirrat08: Pirrat P, Smith MA, Pearson AR, McPherson MJ, Phillips SE (2008). "Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway." Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 12);1105-9. PMID: 19052360

Roh94: Roh JH, Suzuki H, Azakami H, Yamashita M, Murooka Y, Kumagai H (1994). "Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12." Biosci Biotechnol Biochem 58(9);1652-6. PMID: 7765483

Roh94a: Roh JH, Suzuki H, Kumagai H, Yamashita M, Azakami H, Murooka Y, Mikami B (1994). "Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12." J Mol Biol 1994;238(4);635-7. PMID: 8176752

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Saysell02: Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF (2002). "Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue." Biochem J 365(Pt 3);809-16. PMID: 11985492

Smith10: Smith MA, Pirrat P, Pearson AR, Kurtis CR, Trinh CH, Gaule TG, Knowles PF, Phillips SE, McPherson MJ (2010). "Exploring the roles of the metal ions in Escherichia coli copper amine oxidase." Biochemistry 49(6);1268-80. PMID: 20052994

Steinebach96: Steinebach V, Benen JA, Bader R, Postma PW, De Vries S, Duine JA (1996). "Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme." Eur J Biochem 237(3);584-91. PMID: 8647101

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Wilmot97: Wilmot CM, Murray JM, Alton G, Parsons MR, Convery MA, Blakeley V, Corner AS, Palcic MM, Knowles PF, McPherson MJ, Phillips SE (1997). "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction." Biochemistry 36(7);1608-20. PMID: 9048544

Wilmot99: Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE (1999). "Visualization of dioxygen bound to copper during enzyme catalysis." Science 286(5445);1724-8. PMID: 10576737

Yamashita96: Yamashita M, Azakami H, Yokoro N, Roh JH, Suzuki H, Kumagai H, Murooka Y (1996). "maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli." J Bacteriol 178(10);2941-7. PMID: 8631685

Other References Related to Gene Regulation

Partridge09: Partridge JD, Bodenmiller DM, Humphrys MS, Spiro S (2009). "NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility." Mol Microbiol 73(4);680-94. PMID: 19656291

Zeng13: Zeng J, Spiro S (2013). "Finely tuned regulation of the aromatic amine degradation pathway in Escherichia coli." J Bacteriol 195(22);5141-50. PMID: 24013633


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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