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Pathway Description
1,6-Anhydro-N-acetylmuramic Acid Recycling
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-10-09
Last Updated: 2025-05-08
Most bacteria, including Escherichia coli, are composed of murein which protects and stabilizes the cell wall. Over half of the murein is broken down by Escherichia coli and recycled for the next generation. The main muropeptide is GlcNAc-anhydro-N-acetylmuramic acid (anhMurNAc)-l-Ala-γ-d-Glu-meso-Dap-d-Ala which enters the cytoplasm by AmpG protein. The peptide is then released from the muropeptide. 1,6-Anhydro-N-acetylmuramic acid (anhMurNAc) is recycled by its conversion to N-acetylglucosamine-phosphate (GlcNAc-P). The sugar is phosphorylated by anhydro-N-acetylmuramic acid kinase (AnmK) to produce MurNAc-P. Etherase cleaves MurNAc-P to produce N-acetyl-D-glucosamine 6-phosphate. The product can undergo further degradation or be recycled into peptidoglycan monomers. The pathway's final product is a peptidoglycan biosynthesis precursor, UDP-N-acetyl-α-D-muramate. The enzyme muropeptide ligase (mpl), attaches the recovered Ala-Glu-DAP tripeptide to the precursor UDP-N-acetyl-α-D-muramate to return to the peptide to the peptidoglycan biosynthetic pathway to synthesize the cell wall.
References
1,6-Anhydro-N-acetylmuramic Acid Recycling References
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Pubmed: 3891732
Uehara T, Suefuji K, Valbuena N, Meehan B, Donegan M, Park JT: Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J Bacteriol. 2005 Jun;187(11):3643-9. doi: 10.1128/JB.187.11.3643-3649.2005.
Pubmed: 15901686
Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. doi: 10.1093/dnares/3.3.137.
Pubmed: 8905232
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Pubmed: 16738553
Kerff F, Petrella S, Mercier F, Sauvage E, Herman R, Pennartz A, Zervosen A, Luxen A, Frere JM, Joris B, Charlier P: Specific structural features of the N-acetylmuramoyl-L-alanine amidase AmiD from Escherichia coli and mechanistic implications for enzymes of this family. J Mol Biol. 2010 Mar 19;397(1):249-59. doi: 10.1016/j.jmb.2009.12.038. Epub 2009 Dec 28.
Pubmed: 20036252
Lindquist S, Galleni M, Lindberg F, Normark S: Signalling proteins in enterobacterial AmpC beta-lactamase regulation. Mol Microbiol. 1989 Aug;3(8):1091-102. doi: 10.1111/j.1365-2958.1989.tb00259.x.
Pubmed: 2691840
Honore N, Nicolas MH, Cole ST: Regulation of enterobacterial cephalosporinase production: the role of a membrane-bound sensory transducer. Mol Microbiol. 1989 Aug;3(8):1121-30. doi: 10.1111/j.1365-2958.1989.tb00262.x.
Pubmed: 2607970
Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. doi: 10.1093/dnares/4.2.91.
Pubmed: 9205837
Souza JM, Plumbridge JA, Calcagno ML: N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization. Arch Biochem Biophys. 1997 Apr 15;340(2):338-46. doi: 10.1006/abbi.1997.9780.
Pubmed: 9143339
Ferreira FM, Mendoza-Hernandez G, Castaneda-Bueno M, Aparicio R, Fischer H, Calcagno ML, Oliva G: Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli. J Mol Biol. 2006 Jun 2;359(2):308-21. doi: 10.1016/j.jmb.2006.03.024. Epub 2006 Mar 29.
Pubmed: 16630633
Plumbridge JA: Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon. Mol Microbiol. 1989 Apr;3(4):505-15. doi: 10.1111/j.1365-2958.1989.tb00197.x.
Pubmed: 2668691
Dallas WS, Dev IK, Ray PH: The dihydropteroate synthase gene, folP, is near the leucine tRNA gene, leuU, on the Escherichia coli chromosome. J Bacteriol. 1993 Dec;175(23):7743-4. doi: 10.1128/jb.175.23.7743-7744.1993.
Pubmed: 8244950
Mengin-Lecreulx D, van Heijenoort J: Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J Bacteriol. 1993 Oct;175(19):6150-7. doi: 10.1128/jb.175.19.6150-6157.1993.
Pubmed: 8407787
Mengin-Lecreulx D, van Heijenoort J: Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J Bacteriol. 1994 Sep;176(18):5788-95. doi: 10.1128/jb.176.18.5788-5795.1994.
Pubmed: 8083170
Walker JE, Gay NJ, Saraste M, Eberle AN: DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS. Biochem J. 1984 Dec 15;224(3):799-815. doi: 10.1042/bj2240799.
Pubmed: 6395859
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0002076
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