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Escherichia coli K-12 substr. MG1655 Enzyme: methionine adenosyltransferase



Gene: metK Accession Numbers: EG10589 (EcoCyc), b2942, ECK2937

Synonyms: metX

Regulation Summary Diagram: ?

Subunit composition of methionine adenosyltransferase = [MetK]4
         methionine adenosyltransferase = MetK

Summary:
Methionine adenosyltransferase catalyzes the formation of the sulfonium compound S-adenosylmethionine. The reaction is unusual in that the entire tripolyphosphate chain is cleaved from the ATP molecule, and is further degraded to pyrophosphate and phosphate before the products are released [Markham80]. Due to its importance, the enzyme is a target for the development of antimicrobial and anticancer compounds.

The enzyme is a homotetramer in solution [Markham80]; the tetrameric form is required for activity [Markham88, Reczkowski95]. Various crystal structures of methionine adenosyltransferase have been solved. The enzyme is a dimer of dimers with active sites located at the dimer interfaces [Takusagawa96, Takusagawa96a, Komoto04]. A mobile loop gates access to the active site [Fu96].

Methionine adenosyltransferase requires binding of two divalent cations and one monovalent cation per subunit for full activity [Markham80, Markham81]. The binding sites have been studied [Markham84, Markham86, Zhang93, McQueney95]. The reaction proceeds by a sequential mechanism consistent with random binding of substrates and ordered product release [Markham80]. The catalytic mechanism and active site have been studied [Markham87, SchalkHihi99, Reczkowski99, McQueney00, Taylor02, Taylor99a, Taylor00]. The R244 residue plays a role in interactions with the triphosphate chain [Reczkowski98]. A novel catalytic mechanism for SAM formation has been proposed [Komoto04].

Novel inhibitors of methionine adenosyltransferase have been discovered by computational docking and were tested in vitro [Taylor09].

metK is essential for growth in E. coli [Wei02a]. The metK84 mutant has an altered promoter sequence [Wei02a] and shows a defect in cell division [Newman98]. Further studies of recruitment of cell division proteins to the septal ring in the metK84 mutant indicate that a methylation reaction is required for complete septal ring assembly [Wang05a]. Expression of methionine adenosyltransferase is regulated by MetJ [Su71]. Transcription of metK is induced upon biofilm formation [Ren04].

[Satischandran93] reported the presence of two adjacent genes encoding methionine adenosyltransferase, metK and metX; however, as noted by [Wei02a], there is no evidence for the existence of metX in the sequenced genome.

Review: [SaintGirons88]

Locations: cytosol

Map Position: [3,084,728 -> 3,085,882] (66.49 centisomes)
Length: 1155 bp / 384 aa

Molecular Weight of Polypeptide: 41.952 kD (from nucleotide sequence), 43.0 kD (experimental) [Markham80 ]

Molecular Weight of Multimer: 180.0 kD (experimental) [Markham80]

pI: 6.05

Unification Links: ASAP:ABE-0009650 , CGSC:507 , DIP:DIP-35672N , EchoBASE:EB0584 , EcoGene:EG10589 , EcoliWiki:b2942 , Mint:MINT-1233798 , OU-Microarray:b2942 , PortEco:metK , PR:PRO_000023216 , Pride:P0A817 , Protein Model Portal:P0A817 , RefSeq:NP_417417 , RegulonDB:EG10589 , SMR:P0A817 , String:511145.b2942 , UniProt:P0A817

Relationship Links: InterPro:IN-FAMILY:IPR002133 , InterPro:IN-FAMILY:IPR022628 , InterPro:IN-FAMILY:IPR022629 , InterPro:IN-FAMILY:IPR022630 , InterPro:IN-FAMILY:IPR022631 , InterPro:IN-FAMILY:IPR022636 , Panther:IN-FAMILY:PTHR11964 , PDB:Structure:1FUG , PDB:Structure:1MXA , PDB:Structure:1MXB , PDB:Structure:1MXC , PDB:Structure:1P7L , PDB:Structure:1RG9 , PDB:Structure:1XRA , PDB:Structure:1XRB , PDB:Structure:1XRC , Pfam:IN-FAMILY:PF00438 , Pfam:IN-FAMILY:PF02772 , Pfam:IN-FAMILY:PF02773 , Prosite:IN-FAMILY:PS00376 , Prosite:IN-FAMILY:PS00377

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006556 - S-adenosylmethionine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA01a, Satishchandran90a, Greene73]
GO:0033353 - S-adenosylmethionine cycle Inferred from experiment [Wei02a]
GO:0006730 - one-carbon metabolic process Inferred by computational analysis [UniProtGOA11a, GOA06]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment Inferred by computational analysis [GOA06, Markham80]
GO:0004478 - methionine adenosyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Markham80]
GO:0005515 - protein binding Inferred from experiment [Tang08a, Arifuzzaman06]
GO:0030955 - potassium ion binding Inferred from experiment [McQueney95, Markham80]
GO:0042802 - identical protein binding Inferred from experiment [Lasserre06, Takusagawa96a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07b, LopezCampistrou05, Watt07, Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism central intermediary metabolism S-adenosyl methionine biosynthesis

Essentiality data for metK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Last-Curated ? 30-Nov-2009 by Keseler I , SRI International


Enzymatic reaction of: methionine adenosyltransferase

Synonyms: S-adenosylmethionine synthetase, ATP:L-methionine S-adenosyltransferase, MAT

EC Number: 2.5.1.6

ATP + L-methionine + H2O <=> S-adenosyl-L-methionine + phosphate + diphosphate

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 for L-methionine: seleno-L-methionine [Markham80 ]

In Pathways: S-adenosyl-L-methionine cycle I , aspartate superpathway , superpathway of S-adenosyl-L-methionine biosynthesis , S-adenosyl-L-methionine biosynthesis

Cofactors or Prosthetic Groups [Markham80, Markham81, Comment 2]: K+ [Markham80], Mg2+ [Markham80]

Alternative Cofactors for K+ [Markham81 ]: ammonium , Tl+ , Cs+ , Li+ , Na+

Alternative Cofactors for Mg2+ [Markham81 ]: Mn2+ , Co2+ , Zn2+ , Cd2+ , Ni2+ , Ca2+

Cofactor Binding Comment: The enzyme has a single binding site per subunit for a monovalent cation. A divalent cation is bound to ATP during the reaction. [Markham80]

Inhibitors (Competitive): diimidotriphosphate [Reczkowski99] , S-carbamylcysteine [Markham80] , PPPi [Markham80, Comment 3] , AMPPNP [Markham80] , S-adenosyl-L-methionine [Markham80]

Inhibitors (Noncompetitive): diphosphate [Markham80] , phosphate [Markham80]

Inhibitors (Unknown Mechanism): UO2+ [McQueney95] , L-norleucine [Chattopadhyay91]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
S-adenosyl-L-methionine
4.2e-4
[Taylor02, BRENDA14]
L-methionine
92.0
[Taylor02, BRENDA14]
L-methionine
30.0, 65.0, 80.0
[LeGros00, BRENDA14]
L-methionine
80.0
[Markham80, BRENDA14]
L-methionine
110.0
1.5
[Taylor03, BRENDA14]
ATP
73.0
[Taylor02, BRENDA14]
ATP
83.0
[Taylor03, BRENDA14]
ATP
100.0
[Markham80]


Sequence Features

Feature Class Location Common Name Citations Comment
Cleavage-of-Initial-Methionine 1  
[UniProt10a]
UniProt: Removed;
Chain 2 -> 384  
[UniProt09]
UniProt: S-adenosylmethionine synthetase;
Acetylation-Modification 3  
[Zhang09a, UniProt11a]
UniProt: N6-acetyllysine.
Mutagenesis-Variant 15  
[Taylor00, UniProt11a]
Alternate sequence: H → N; UniProt: Loss of activity.
Mutagenesis-Variant 17  
[Taylor99a, UniProt11a]
Alternate sequence: D → A; UniProt: Loss of activity.
Alternate sequence: D → N; UniProt: Loss of activity.
Metal-Binding-Site 17  
[UniProt10a]
UniProt: Magnesium;
Mutagenesis-Variant 43  
[McQueney95, UniProt11a]
Alternate sequence: E → Q; UniProt: Loss of stimulation by potassium.
Alternate sequence: E → K; UniProt: Misfolding and subject to proteolytic degradation.
Metal-Binding-Site 43 K+ binding ligand
[McQueney95]
 
Sequence-Conflict 50 -> 61  
[Moore90, Markham84a, UniProt10a]
Alternate sequence: MVLVGGEITTSA → IGFSWRRNHHQRP; UniProt: (in Ref. 1 and 5);
Mutagenesis-Variant 90  
[Reczkowski95, UniProt11a]
Alternate sequence: C → S; UniProt: Decrease in the homotetramer formation capability. Enhanced thermal stability.
Alternate sequence: C → A; UniProt: Decrease in the homotetramer formation capability. Enhanced thermal stability.
Mutagenesis-Variant 119  
[Taylor99a, UniProt11a]
Alternate sequence: D → N; UniProt: Decrease of both AdoMet synthesis and AdoMet-activated tripolyphosphate hydrolysis.
Amino-Acid-Sites-That-Bind 119  
[UniProt10a]
UniProt: Methionine;
Sequence-Conflict 123 -> 133  
[Markham84a, UniProt10a]
Alternate sequence: MFGYATNETDV → DVSATQLMKPTC; UniProt: (in Ref. 1; AAA24164);
Sequence-Conflict 159 -> 161  
[Satischandran93, Markham84a, UniProt10a]
Alternate sequence: PWL → RV; UniProt: (in Ref. 1 and 2);
Mutagenesis-Variant 166  
[Taylor00, UniProt11a]
Alternate sequence: K → M; UniProt: Decrease in AdoMet synthesis.
Sequence-Conflict 172  
[Markham84a, UniProt10a]
Alternate sequence: Q → S; UniProt: (in Ref. 1; AAA24164);
Mutagenesis-Variant 239  
[Taylor99a, UniProt11a]
Alternate sequence: D → N; UniProt: Decrease in AdoMet synthesis.
Amino-Acid-Sites-That-Bind 239  
[UniProt10a]
UniProt: Methionine;
Protein-Segment 239 -> 248  
[UniProt10]
UniProt: Pyrophosphate binding; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 240  
[Reczkowski95, UniProt11a]
Alternate sequence: C → A; UniProt: Decrease in AdoMet synthesis.
Mutagenesis-Variant 245  
[Reczkowski98, UniProt11a]
Alternate sequence: R → L; UniProt: Loss of activity.
Alternate sequence: R → H; UniProt: Loss of activity.
Mutagenesis-Variant 246  
[Taylor00, UniProt11a]
Alternate sequence: K → M; UniProt: Loss of activity. modification in protein conformation.
Sequence-Conflict 252  
[Markham84a, UniProt10a]
Alternate sequence: Y → T; UniProt: (in Ref. 1; AAA24164);
Nucleotide-Phosphate-Binding-Region 260 -> 267  
[UniProt10]
UniProt: ATP; Non-Experimental Qualifier: potential;
Metal-Binding-Site 264  
[UniProt10a]
UniProt: Potassium;
Mutagenesis-Variant 266  
[Taylor00, UniProt11a]
Alternate sequence: K → M; UniProt: Unstable; trace activity.
Alternate sequence: K → A; UniProt: Loss of activity.
Mutagenesis-Variant 270  
[Taylor00, UniProt11a]
Alternate sequence: K → M; UniProt: Decrease in activity.
Mutagenesis-Variant 272  
[Taylor99a, UniProt11a]
Alternate sequence: D → A; UniProt: Loss of activity.
Alternate sequence: D → N; UniProt: Loss of activity.
Metal-Binding-Site 272  
[UniProt10a]
UniProt: Magnesium;
Sequence-Conflict 305  
[Markham84a, UniProt10a]
Alternate sequence: V → L; UniProt: (in Ref. 1; AAA24164);
Sequence-Conflict 337  
[Markham84a, UniProt10a]
Alternate sequence: R → missing; UniProt: (in Ref. 1);
Sequence-Conflict 339  
[Markham84a, UniProt10a]
Alternate sequence: Y → I; UniProt: (in Ref. 1);
Sequence-Conflict 375 -> 376  
[Satischandran93, UniProt10a]
Alternate sequence: QL → HV; UniProt: (in Ref. 2);
Sequence-Conflict 378  
[Satischandran93, UniProt10a]
Alternate sequence: R → P; UniProt: (in Ref. 2);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2942 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10589.


References

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Chattopadhyay91: Chattopadhyay MK, Ghosh AK, Sengupta S (1991). "Control of methionine biosynthesis in Escherichia coli K12: a closer study with analogue-resistant mutants." J Gen Microbiol 137(3);685-91. PMID: 2033383

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

Fu96: Fu Z, Hu Y, Markham GD, Takusagawa F (1996). "Flexible loop in the structure of S-adenosylmethionine synthetase crystallized in the tetragonal modification." J Biomol Struct Dyn 13(5);727-39. PMID: 8723769

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Greene73: Greene RC, Hunter JS, Coch EH (1973). "Properties of metK mutants of Escherichia coli K-12." J Bacteriol 115(1);57-67. PMID: 4577753

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Komoto04: Komoto J, Yamada T, Takata Y, Markham GD, Takusagawa F (2004). "Crystal structure of the S-adenosylmethionine synthetase ternary complex: a novel catalytic mechanism of S-adenosylmethionine synthesis from ATP and Met." Biochemistry 43(7);1821-31. PMID: 14967023

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

LeGros00: LeGros HL, Halim AB, Geller AM, Kotb M (2000). "Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)." J Biol Chem 275(4);2359-66. PMID: 10644686

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Markham80: Markham GD, Hafner EW, Tabor CW, Tabor H (1980). "S-Adenosylmethionine synthetase from Escherichia coli." J Biol Chem 1980;255(19);9082-92. PMID: 6251075

Markham81: Markham GD (1981). "Spatial proximity of two divalent metal ions at the active site of S-adenosylmethionine synthetase." J Biol Chem 1981;256(4);1903-9. PMID: 6257692

Markham84: Markham GD (1984). "Structure of the divalent metal ion activator binding site of S-adenosylmethionine synthetase studied by vanadyl(IV) electron paramagnetic resonance." Biochemistry 23(3);470-8. PMID: 6322838

Markham84a: Markham GD, DeParasis J, Gatmaitan J (1984). "The sequence of metK, the structural gene for S-adenosylmethionine synthetase in Escherichia coli." J Biol Chem 259(23);14505-7. PMID: 6094561

Markham86: Markham GD (1986). "Characterization of the monovalent cation activator binding site of S-adenosylmethionine synthetase by 205Tl NMR of enzyme-bound Tl+." J Biol Chem 261(4);1507-9. PMID: 3511045

Markham87: Markham GD, Parkin DW, Mentch F, Schramm VL (1987). "A kinetic isotope effect study and transition state analysis of the S-adenosylmethionine synthetase reaction." J Biol Chem 262(12);5609-15. PMID: 3553181

Markham88: Markham GD, Satishchandran C (1988). "Identification of the reactive sulfhydryl groups of S-adenosylmethionine synthetase." J Biol Chem 263(18);8666-70. PMID: 3288619

McQueney00: McQueney MS, Anderson KS, Markham GD (2000). "Energetics of S-adenosylmethionine synthetase catalysis." Biochemistry 39(15);4443-54. PMID: 10757994

McQueney95: McQueney MS, Markham GD (1995). "Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition." J Biol Chem 270(31);18277-84. PMID: 7629147

Moore90: Moore RC, Boyle SM (1990). "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli." J Bacteriol 1990;172(8);4631-40. PMID: 2198270

Newman98: Newman EB, Budman LI, Chan EC, Greene RC, Lin RT, Woldringh CL, D'Ari R (1998). "Lack of S-adenosylmethionine results in a cell division defect in Escherichia coli." J Bacteriol 180(14);3614-9. PMID: 9658005

Reczkowski95: Reczkowski RS, Markham GD (1995). "Structural and functional roles of cysteine 90 and cysteine 240 in S-adenosylmethionine synthetase." J Biol Chem 270(31);18484-90. PMID: 7629176

Reczkowski98: Reczkowski RS, Taylor JC, Markham GD (1998). "The active-site arginine of S-adenosylmethionine synthetase orients the reaction intermediate." Biochemistry 37(39);13499-506. PMID: 9753435

Reczkowski99: Reczkowski RS, Markham GD (1999). "Slow binding inhibition of S-adenosylmethionine synthetase by imidophosphate analogues of an intermediate and product." Biochemistry 38(28);9063-8. PMID: 10413480

Ren04: Ren D, Bedzyk LA, Thomas SM, Ye RW, Wood TK (2004). "Gene expression in Escherichia coli biofilms." Appl Microbiol Biotechnol 64(4);515-24. PMID: 14727089

SaintGirons88: Saint-Girons I, Parsot C, Zakin MM, Barzu O, Cohen GN (1988). "Methionine biosynthesis in Enterobacteriaceae: biochemical, regulatory, and evolutionary aspects." CRC Crit Rev Biochem 23 Suppl 1;S1-42. PMID: 3293911

Satischandran93: Satischandran C, Taylor JC, Markham GD (1993). "Isozymes of S-adenosylmethionine synthetase are encoded by tandemly duplicated genes in Escherichia coli." Mol Microbiol 1993;9(4);835-46. PMID: 8231813

Satishchandran90a: Satishchandran C, Taylor JC, Markham GD (1990). "Novel Escherichia coli K-12 mutants impaired in S-adenosylmethionine synthesis." J Bacteriol 172(8);4489-96. PMID: 2115868

SchalkHihi99: Schalk-Hihi C, Markham GD (1999). "The conformations of a substrate and a product bound to the active site of S-adenosylmethionine synthetase." Biochemistry 38(8);2542-50. PMID: 10029549

Su71: Su CH, Greene RC (1971). "Regulation of methionine biosynthesis in Escherichia coli: mapping of the metJ locus and properties of a metJ plus-metJ minus diploid." Proc Natl Acad Sci U S A 68(2);367-71. PMID: 5277087

Takusagawa96: Takusagawa F, Kamitori S, Misaki S, Markham GD (1996). "Crystal structure of S-adenosylmethionine synthetase." J Biol Chem 271(1);136-47. PMID: 8550549

Takusagawa96a: Takusagawa F, Kamitori S, Markham GD (1996). "Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution." Biochemistry 35(8);2586-96. PMID: 8611562

Tang08a: Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M (2008). "Essential role of the chaperonin folding compartment in vivo." EMBO J 27(10);1458-68. PMID: 18418386

Taylor00: Taylor JC, Markham GD (2000). "The bifunctional active site of S-adenosylmethionine synthetase. Roles of the basic residues." J Biol Chem 275(6);4060-5. PMID: 10660564

Taylor02: Taylor JC, Takusagawa F, Markham GD (2002). "The active site loop of S-adenosylmethionine synthetase modulates catalytic efficiency." Biochemistry 41(30);9358-69. PMID: 12135357

Taylor03: Taylor JC, Markham GD (2003). "Conformational dynamics of the active site loop of S-adenosylmethionine synthetase illuminated by site-directed spin labeling." Arch Biochem Biophys 415(2);164-71. PMID: 12831838

Taylor09: Taylor JC, Bock CW, Takusagawa F, Markham GD (2009). "Discovery of novel types of inhibitors of S-adenosylmethionine synthesis by virtual screening." J Med Chem 52(19);5967-73. PMID: 19739644

Taylor99a: Taylor JC, Markham GD (1999). "The bifunctional active site of s-adenosylmethionine synthetase. Roles of the active site aspartates." J Biol Chem 274(46);32909-14. PMID: 10551856

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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 the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

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

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

Wang05a: Wang S, Arends SJ, Weiss DS, Newman EB (2005). "A deficiency in S-adenosylmethionine synthetase interrupts assembly of the septal ring in Escherichia coli K-12." Mol Microbiol 58(3);791-9. PMID: 16238627

Watt07: Watt RM, Wang J, Leong M, Kung HF, Cheah KS, Liu D, Danchin A, Huang JD (2007). "Visualizing the proteome of Escherichia coli: an efficient and versatile method for labeling chromosomal coding DNA sequences (CDSs) with fluorescent protein genes." Nucleic Acids Res 35(6);e37. PMID: 17272300

Wei02a: Wei Y, Newman EB (2002). "Studies on the role of the metK gene product of Escherichia coli K-12." Mol Microbiol 43(6);1651-6. PMID: 11952912

Zhang07b: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhang09a: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Zhang93: Zhang C, Markham GD, LoBrutto R (1993). "Coordination of vanadyl(IV) cation in complexes of S-adenosylmethionine synthetase: multifrequency electron spin echo envelope modulation study." Biochemistry 32(37);9866-73. PMID: 8396974

Other References Related to Gene Regulation

Liu01: Liu R, Blackwell TW, States DJ (2001). "Conformational model for binding site recognition by the E.coli MetJ transcription factor." Bioinformatics 17(7);622-33. PMID: 11448880

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470


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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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