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Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like peptidoglycan layer outside the plasma membrane, the rigid cell wall characteristic of most bacteria. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is an oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by peptidoglycan production. Peptidoglycan hydrolysis and synthesis are two processes that must occur in order for cells to grow and multiply, a technique carried out in three stages: clipping of current material, insertion of new material, and re-crosslinking of existing material to new material.
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N-Acetylmuramic acid is an organic compound with the chemical formula C
11H
19NO
8. It is a monomer of peptidoglycan in most bacterial cell walls, which is built from alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid, cross-linked by oligopeptides at the lactic acid residue of MurNAc.
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In enzymology, a UDP-N-acetylmuramate—L-alanine ligase is an enzyme that catalyzes the chemical reaction
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In enzymology, a UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase (EC 2.3.2.10) is an enzyme that catalyzes the chemical reaction
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminoheptanedioate gamma-ligase (ADP-forming). This enzyme catalyses the following chemical reaction
Cyanophycin synthase (L-aspartate-adding) is an enzyme with systematic name cyanophycin:L-aspartate ligase (ADP-forming). This enzyme catalyses the following chemical reaction
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase is an enzyme with systematic name UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:D-lysine alpha-ligase (ADP-forming). This enzyme catalyses the following chemical reaction
References
- ↑ Deva T, Baker EN, Squire CJ, Smith CA (December 2006). "Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)". Acta Crystallogr. D. 62 (Pt 12): 1466–74. doi:10.1107/S0907444906038376. PMID 17139082.
- ↑ Perdih A, Kotnik M, Hodoscek M, Solmajer T (July 2007). "Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD". Proteins. 68 (1): 243–54. doi:10.1002/prot.21374. PMID 17427948. S2CID 11577329.
- ↑ Boniface A, Bouhss A, Mengin-Lecreulx D, Blanot D (June 2006). "The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity". J. Biol. Chem. 281 (23): 15680–6. doi: 10.1074/jbc.M506311200 . PMID 16595662.
- ↑ Longenecker KL, Stamper GF, Hajduk PJ, Fry EH, Jakob CG, Harlan JE, Edalji R, Bartley DM, Walter KA, Solomon LR, Holzman TF, Gu YG, Lerner CG, Beutel BA, Stoll VS (December 2005). "Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure". Protein Sci. 14 (12): 3039–47. doi:10.1110/ps.051604805. PMC 2253247 . PMID 16322581.
- ↑ Smith CA (September 2006). "Structure, function and dynamics in the mur family of bacterial cell wall ligases". J. Mol. Biol. 362 (4): 640–55. doi:10.1016/j.jmb.2006.07.066. PMID 16934839.
- ↑ Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W (May 1998). "Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)". Eur. J. Biochem. 254 (1): 154–9. doi: 10.1046/j.1432-1327.1998.2540154.x . PMID 9652408.
