N-acetylmuramic acid 6-phosphate etherase

N-acetylmuramic acid 6-phosphate etherase (EC 4.2.1.126, MurNAc-6-P etherase, MurQ) is an enzyme with systematic name (R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming). This enzyme catalyses the following chemical reaction

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate

\rightleftharpoons

N-acetylmuramate 6-phosphate + H₂O

This enzyme is required for the utilization of anhydro-N-acetylmuramic acid in some Pseudomonadota.

References

Jaeger T, Arsic M, Mayer C (August 2005). "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"". The Journal of Biological Chemistry. 280 (34): 30100–6. doi:10.1074/jbc.m502208200. PMID 15983044.
Uehara T, Suefuji K, Valbuena N, Meehan B, Donegan M, Park JT (June 2005). "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate". Journal of Bacteriology. 187 (11): 3643–9. doi:10.1128/jb.187.11.3643-3649.2005. PMC 1112033. PMID 15901686.
Uehara T, Suefuji K, Jaeger T, Mayer C, Park JT (February 2006). "MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall". Journal of Bacteriology. 188 (4): 1660–2. doi:10.1128/jb.188.4.1660-1662.2006. PMC 1367226. PMID 16452451.
Hadi T, Dahl U, Mayer C, Tanner ME (November 2008). "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling". Biochemistry. 47 (44): 11547–58. doi:10.1021/bi8014532. PMID 18837509.
Jaeger T, Mayer C (March 2008). "N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism". Cellular and Molecular Life Sciences. 65 (6): 928–39. doi:10.1007/s00018-007-7399-x. PMC 11131651. PMID 18049859.

External links

N-acetylmuramic+acid+6-phosphate+etherase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 4.2.1