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Escherichia coli K-12 substr. MG1655 Enzyme: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase



Gene: murD Accession Numbers: EG10620 (EcoCyc), b0088, ECK0089

Regulation Summary Diagram: ?

Summary:
UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) catalyzes the addition of the second amino acid to the peptide moiety of the monomer unit of peptidoglycan. There are estimated to be less than 1000 copies of MurD in the cell [PratvielSosa91].

The reaction mechanism and specific inhibitors of the enzyme have been studied [Vaganay96, Tanner96, Gegnas98, Horton03, Strancar06]. In vitro in the absence of D-glutamate, MurD can catalyze the formation of p4A from ATP via an acyl phosphate intermediate [Bouhss99].

Crystal structures of the enzyme alone and in complex with substrates, product or inhibitors have been solved, and a catalytic mechanism involving an acyl phosphate intermediate was deduced [Bertrand97, Bertrand99, Bertrand00, Kotnik07]. Results from site-directed mutagenesis of conserved amino acid residues within the active site correlated with their assigned function based on the crystal structures [Bouhss99a]. The K198 residue is present as a carbamate derivative [Bertrand99]; the modification is important for catalytic activity [Dementin01].

Molecular dynamics simulations were performed to provide insight into structural changes during substrate binding and transition into the active conformation [Perdih07]. Three reaction paths to the formation of the tetrahedral reaction intermediate have been investigated by hybrid QM/MM molecular modeling [Perdih09].

murD is an essential gene [Baba06], and is therefore an antibacterial drug target. Novel inhibitors of MurD activity have been identified [Frlan08, Bratkovic08, Sink08, Humljan08, Tomasic09, Simcic09, Kristan09, Sova09, Zidar10, Sosi11, Tomasic11, Tomaši11, Barreteau12].

Reviews: [El03, Typas12]

Gene Citations: [Vicente98, MenginLecreulx98, Hara97]

Locations: cytosol

Map Position: [97,087 -> 98,403] (2.09 centisomes)
Length: 1317 bp / 438 aa

Molecular Weight of Polypeptide: 46.974 kD (from nucleotide sequence), 50 kD (experimental) [MenginLecreulx89 ]

pI: 4.2 [PratvielSosa91]

Unification Links: ASAP:ABE-0000318 , CGSC:30450 , DIP:DIP-10279N , EchoBASE:EB0615 , EcoGene:EG10620 , EcoliWiki:b0088 , Mint:MINT-1269366 , ModBase:P14900 , OU-Microarray:b0088 , PortEco:murD , PR:PRO_000023315 , Pride:P14900 , Protein Model Portal:P14900 , RefSeq:NP_414630 , RegulonDB:EG10620 , SMR:P14900 , String:511145.b0088 , UniProt:P14900

Relationship Links: InterPro:IN-FAMILY:IPR004101 , InterPro:IN-FAMILY:IPR005762 , InterPro:IN-FAMILY:IPR013221 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR23135:SF2 , PDB:Structure:1E0D , PDB:Structure:1EEH , PDB:Structure:1UAG , PDB:Structure:2JFF , PDB:Structure:2JFG , PDB:Structure:2JFH , PDB:Structure:2UAG , PDB:Structure:2UUO , PDB:Structure:2UUP , PDB:Structure:2VTD , PDB:Structure:2VTE , PDB:Structure:2WJP , PDB:Structure:2X5O , PDB:Structure:2XPC , PDB:Structure:2Y1O , PDB:Structure:2Y66 , PDB:Structure:2Y67 , PDB:Structure:2Y68 , PDB:Structure:3UAG , PDB:Structure:4UAG , Pfam:IN-FAMILY:PF02875 , Pfam:IN-FAMILY:PF08245

In Paralogous Gene Group: 32 (3 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
GO:0008360 - regulation of cell shape Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01a]
GO:0009252 - peptidoglycan biosynthetic process Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06]
GO:0051301 - cell division Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0071555 - cell wall organization Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0008764 - UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, PratvielSosa91]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, PratvielSosa91]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell structure murein
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)

Essentiality data for murD 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 ? 17-Jul-2013 by Keseler I , SRI International


Enzymatic reaction of: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Synonyms: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase, UDP-N-acetylmuramoylalanine-D-glutamate ligase, D-glutamate-adding enzyme

EC Number: 6.3.2.9

D-glutamate + UDP-N-acetylmuramoyl-L-alanine + ATP <=> UDP-N-acetylmuramoyl-L-alanyl--D-glutamate + ADP + phosphate + H+

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 2]:

In Pathways: peptidoglycan biosynthesis I (meso-diaminopimelate containing) , UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-DAP-containing)

Summary:
A range of closely related analogs of D-glutamate has been tested as substrates or inhibitors of the enzyme [PratvielSosa94].

Cofactors or Prosthetic Groups [Comment 3]: K+ [Walsh99, PratvielSosa91], Mg2+ [Walsh99, PratvielSosa91]

Inhibitors (Unknown Mechanism): DDP-N-acetylmuramoyl-L-alanyl-D-glutamate [Michaud87] , UDP-N-acetylmuramoyl-L-alanyl--D-glutamate [Michaud87] , phosphate [PratvielSosa91]

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-glutamate
67.0
[Kristan09, BRENDA14]
D-glutamate
55.0
[PratvielSosa91]
ATP
95.0
[Kotnik07, BRENDA14]
ATP
106.0
[Kristan09, BRENDA14]
ATP
138.0
[PratvielSosa91]
UDP-N-acetylmuramoyl-L-alanine
7.5
[PratvielSosa91]

pH(opt): 8.8 [BRENDA14, Auger98], 8.9 [BRENDA14, PratvielSosa91], 9.4 [BRENDA14, Bouhss99a], 8.9-9.2 [PratvielSosa91]


Sequence Features

Feature Class Location Common Name Citations Comment State
Cleavage-of-Initial-Methionine 1  
[PratvielSosa91]
   
Chain 2 -> 438  
[UniProt09]
UniProt: UDP-N-acetylmuramoylalanine--D-glutamate ligase;
 
Sequence-Conflict 28  
[MenginLecreulx90, UniProt10a]
Alternate sequence: R → A; UniProt: (in Ref. 2; CAA35611);
 
Nucleotide-Phosphate-Binding-Region 112 -> 118  
[UniProt10]
UniProt: ATP; Non-Experimental Qualifier: potential;
 
Sequence-Conflict 174  
[MenginLecreulx90, UniProt10a]
Alternate sequence: A → T; UniProt: (in Ref. 2; CAA35611);
 
Modified-Residue 198 carbamoylated lysine residue
[Dementin01]
  Modified
Sequence-Conflict 276 -> 277  
[MenginLecreulx90, UniProt10a]
Alternate sequence: AL → RV; UniProt: (in Ref. 2; CAA35611);
 


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0088 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10620; confirmed by SwissProt match.


References

Auger98: Auger G, Martin L, Bertrand J, Ferrari P, Fanchon E, Vaganay S, Petillot Y, van Heijenoort J, Blanot D, Dideberg O (1998). "Large-scale preparation, purification, and crystallization of UDP-N-acetylmuramoyl-L-alanine: D-glutamate ligase from Escherichia coli." Protein Expr Purif 13(1);23-9. PMID: 9631510

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

Barreteau12: Barreteau H, Sosič I, Turk S, Humljan J, Tomašić T, Zidar N, Herve M, Boniface A, Peterlin-Mašič L, Kikelj D, Mengin-Lecreulx D, Gobec S, Blanot D (2012). "MurD enzymes from different bacteria: evaluation of inhibitors." Biochem Pharmacol 84(5);625-32. PMID: 22705647

Bertrand00: Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O (2000). ""Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase." J Mol Biol 301(5);1257-66. PMID: 10966819

Bertrand97: Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O (1997). "Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli." EMBO J 16(12);3416-25. PMID: 9218784

Bertrand99: Bertrand JA, Auger G, Martin L, Fanchon E, Blanot D, Le Beller D, van Heijenoort J, Dideberg O (1999). "Determination of the MurD mechanism through crystallographic analysis of enzyme complexes." J Mol Biol 289(3);579-90. PMID: 10356330

Bouhss99: Bouhss A, Dementin S, van Heijenoort J, Parquet C, Blanot D (1999). "Formation of adenosine 5'-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli." FEBS Lett 453(1-2);15-9. PMID: 10403366

Bouhss99a: Bouhss A, Dementin S, Parquet C, Mengin-Lecreulx D, Bertrand JA, Le Beller D, Dideberg O, van Heijenoort J, Blanot D (1999). "Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D-glutamate ligase (MurD)." Biochemistry 38(38);12240-7. PMID: 10493791

Bratkovic08: Bratkovic T, Lunder M, Urleb U, Strukelj B (2008). "Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis." J Basic Microbiol 48(3);202-6. PMID: 18506905

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

Dementin01: Dementin S, Bouhss A, Auger G, Parquet C, Mengin-Lecreulx D, Dideberg O, van Heijenoort J, Blanot D (2001). "Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as established by chemical rescue experiments." Eur J Biochem 268(22);5800-7. PMID: 11722566

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

El03: El Zoeiby A, Sanschagrin F, Levesque RC (2003). "Structure and function of the Mur enzymes: development of novel inhibitors." Mol Microbiol 47(1);1-12. PMID: 12492849

Frlan08: Frlan R, Kovac A, Blanot D, Gobec S, Pecar S, Obreza A (2008). "Design and synthesis of novel N-benzylidenesulfonohydrazide inhibitors of MurC and MurD as potential antibacterial agents." Molecules 13(1);11-30. PMID: 18259126

Gegnas98: Gegnas LD, Waddell ST, Chabin RM, Reddy S, Wong KK (1998). "Inhibitors of the bacterial cell wall biosynthesis enzyme MurD." Bioorg Med Chem Lett 8(13);1643-8. PMID: 9873406

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."

Hara97: Hara H, Yasuda S, Horiuchi K, Park JT (1997). "A promoter for the first nine genes of the Escherichia coli mra cluster of cell division and cell envelope biosynthesis genes, including ftsI and ftsW." J Bacteriol 179(18);5802-11. PMID: 9294438

Horton03: Horton JR, Bostock JM, Chopra I, Hesse L, Phillips SE, Adams DJ, Johnson AP, Fishwick CW (2003). "Macrocyclic inhibitors of the bacterial cell wall biosynthesis enzyme MurD." Bioorg Med Chem Lett 13(9);1557-60. PMID: 12699754

Humljan08: Humljan J, Kotnik M, Contreras-Martel C, Blanot D, Urleb U, Dessen A, Solmajer T, Gobec S (2008). "Novel naphthalene-N-sulfonyl-D-glutamic acid derivatives as inhibitors of MurD, a key peptidoglycan biosynthesis enzyme." J Med Chem 51(23);7486-94. PMID: 19007109

Kotnik07: Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Herve M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T (2007). "Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase." J Mol Biol 370(1);107-15. PMID: 17507028

Kristan09: Kristan K, Kotnik M, Oblak M, Urleb U (2009). "New high-throughput fluorimetric assay for discovering inhibitors of UDP-N-acetylmuramyl-L-alanine: D-glutamate (MurD) ligase." J Biomol Screen 14(4);412-8. PMID: 19403924

MenginLecreulx89: Mengin-Lecreulx D, Parquet C, Desviat LR, Pla J, Flouret B, Ayala JA, van Heijenoort J (1989). "Organization of the murE-murG region of Escherichia coli: identification of the murD gene encoding the D-glutamic-acid-adding enzyme." J Bacteriol 171(11);6126-34. PMID: 2681153

MenginLecreulx90: Mengin-Lecreulx D, van Heijenoort J (1990). "Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli." Nucleic Acids Res 18(1);183. PMID: 2129548

MenginLecreulx98: Mengin-Lecreulx D, Ayala J, Bouhss A, van Heijenoort J, Parquet C, Hara H (1998). "Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes." J Bacteriol 180(17);4406-12. PMID: 9721276

Michaud87: Michaud C, Blanot D, Flouret B, Van Heijenoort J (1987). "Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli K12." Eur J Biochem 1987;166(3);631-7. PMID: 3301347

Perdih07: Perdih A, Kotnik M, Hodoscek M, Solmajer T (2007). "Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD." Proteins 68(1):243-54. PMID: 17427948

Perdih09: Perdih A, Hodoscek M, Solmajer T (2009). "MurD ligase from E. coli: Tetrahedral intermediate formation study by hybrid quantum mechanical/molecular mechanical replica path method." Proteins 74(3);744-59. PMID: 18704940

PratvielSosa91: Pratviel-Sosa F, Mengin-Lecreulx D, van Heijenoort J (1991). "Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli." Eur J Biochem 1991;202(3);1169-76. PMID: 1765076

PratvielSosa94: Pratviel-Sosa F, Acher F, Trigalo F, Blanot D, Azerad R, van Heijenoort J (1994). "Effect of various analogues of D-glutamic acid on the D-glutamate-adding enzyme from Escherichia coli." FEMS Microbiol Lett 115(2-3);223-8. PMID: 7908001

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Simcic09: Simcic M, Hodoscek M, Humljan J, Kristan K, Urleb U, Kocjan D, Grdadolnik SG (2009). "NMR and molecular dynamics study of the binding mode of naphthalene-N-sulfonyl-D-glutamic acid derivatives: novel MurD ligase inhibitors." J Med Chem 52(9);2899-908. PMID: 19358612

Sink08: Sink R, Kovac A, Tomasic T, Rupnik V, Boniface A, Bostock J, Chopra I, Blanot D, Masic LP, Gobec S, Zega A (2008). "Synthesis and biological evaluation of N-acylhydrazones as inhibitors of MurC and MurD ligases." ChemMedChem 3(9);1362-70. PMID: 18651694

Sosi11: Sosič I, Barreteau H, Simčič M, Sink R, Cesar J, Zega A, Grdadolnik SG, Contreras-Martel C, Dessen A, Amoroso A, Joris B, Blanot D, Gobec S (2011). "Second-generation sulfonamide inhibitors of D-glutamic acid-adding enzyme: activity optimisation with conformationally rigid analogues of D-glutamic acid." Eur J Med Chem 46(7);2880-94. PMID: 21524830

Sova09: Sova M, Kovac A, Turk S, Hrast M, Blanot D, Gobec S (2009). "Phosphorylated hydroxyethylamines as novel inhibitors of the bacterial cell wall biosynthesis enzymes MurC to MurF." Bioorg Chem 37(6);217-22. PMID: 19804894

Strancar06: Strancar K, Blanot D, Gobec S (2006). "Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD." Bioorg Med Chem Lett 16(2);343-8. PMID: 16271472

Tanner96: Tanner ME, Vaganay S, van Heijenoort J, Blanot D (1996). "Phosphinate Inhibitors of the D-Glutamic Acid-Adding Enzyme of Peptidoglycan Biosynthesis." J Org Chem 61(5);1756-1760. PMID: 11667046

Tomasic09: Tomasic T, Zidar N, Rupnik V, Kovac A, Blanot D, Gobec S, Kikelj D, Masic LP (2009). "Synthesis and biological evaluation of new glutamic acid-based inhibitors of MurD ligase." Bioorg Med Chem Lett 19(1);153-7. PMID: 19014883

Tomasic11: Tomasic T, Zidar N, Sink R, Kovac A, Blanot D, Contreras-Martel C, Dessen A, Muller-Premru M, Zega A, Gobec S, Kikelj D, Masic LP (2011). "Structure-based design of a new series of D-glutamic acid based inhibitors of bacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD)." J Med Chem 54(13);4600-10. PMID: 21591605

Tomaši11: Tomašić T, Kovač A, Simčič M, Blanot D, Grdadolnik SG, Gobec S, Kikelj D, Peterlin Mašič L (2011). "Novel 2-thioxothiazolidin-4-one inhibitors of bacterial MurD ligase targeting D-Glu- and diphosphate-binding sites." Eur J Med Chem 46(9);3964-75. PMID: 21703731

Typas12: Typas A, Banzhaf M, Gross CA, Vollmer W (2012). "From the regulation of peptidoglycan synthesis to bacterial growth and morphology." Nat Rev Microbiol 10(2);123-36. PMID: 22203377

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.

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."

Vaganay96: Vaganay S, Tanner ME, van Heijenoort J, Blanot D (1996). "Study of the reaction mechanism of the D-glutamic acid-adding enzyme from Escherichia coli." Microb Drug Resist 2(1);51-4. PMID: 9158722

Vicente98: Vicente M, Gomez MJ, Ayala JA (1998). "Regulation of transcription of cell division genes in the Escherichia coli dcw cluster." Cell Mol Life Sci 54(4);317-24. PMID: 9614967

Walsh99: Walsh AW, Falk PJ, Thanassi J, Discotto L, Pucci MJ, Ho HT (1999). "Comparison of the D-glutamate-adding enzymes from selected gram-positive and gram-negative bacteria." J Bacteriol 181(17);5395-401. PMID: 10464212

Zidar10: Zidar N, Tomasic T, Sink R, Rupnik V, Kovac A, Turk S, Patin D, Blanot D, Contreras Martel C, Dessen A, Muller Premru M, Zega A, Gobec S, Peterlin Masic L, Kikelj D (2010). "Discovery of novel 5-benzylidenerhodanine and 5-benzylidenethiazolidine-2,4-dione inhibitors of MurD ligase." J Med Chem 53(18);6584-94. PMID: 20804196

Other References Related to Gene Regulation

Eraso14: Eraso JM, Markillie LM, Mitchell HD, Taylor RC, Orr G, Margolin W (2014). "The Highly Conserved MraZ Protein Is a Transcriptional Regulator in Escherichia coli." J Bacteriol 196(11);2053-66. PMID: 24659771

Gohler11: Gohler AK, Kokpinar O, Schmidt-Heck W, Geffers R, Guthke R, Rinas U, Schuster S, Jahreis K, Kaleta C (2011). "More than just a metabolic regulator - elucidation and validation of new targets of PdhR in Escherichia coli." BMC Syst Biol 5(1);197. PMID: 22168595

Ishino89: Ishino F, Jung HK, Ikeda M, Doi M, Wachi M, Matsuhashi M (1989). "New mutations fts-36, lts-33, and ftsW clustered in the mra region of the Escherichia coli chromosome induce thermosensitive cell growth and division." J Bacteriol 171(10);5523-30. PMID: 2676977


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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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