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).^[1]^[2]^[3]^[4]^[5] 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 proteobacteria.

References

↑ Jaeger, T., Arsic, M. and Mayer, C. (2005). "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"". J. Biol. Chem. 280: 30100–30106. doi:10.1074/jbc.m502208200. PMID 15983044.
↑ Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. (2005). "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate". J. Bacteriol. 187: 3643–3649. doi:10.1128/jb.187.11.3643-3649.2005. PMID 15901686.
↑ Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. (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". J. Bacteriol. 188: 1660–1662. doi:10.1128/jb.188.4.1660-1662.2006. PMID 16452451.
↑ Hadi, T., Dahl, U., Mayer, C. and Tanner, M.E. (2008). "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling". Biochemistry 47: 11547–11558. doi:10.1021/bi8014532. PMID 18837509.
↑ Jaeger, T. and Mayer, C. (2008). "N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism". Cell. Mol. Life Sci. 65: 928–939. doi:10.1007/s00018-007-7399-x. PMID 18049859.

External links

N-acetylmuramic acid 6-phosphate etherase at the US National Library of Medicine Medical Subject Headings (MeSH)

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

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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