| EC |
4.2.2.29 |
| Accepted name: |
peptidoglycan lytic transglycosylase |
| Reaction: |
a peptidoglycan chain = a peptidoglycan chain with N-acetyl-1,6-anhydromuramyl-(peptide) at the reducing end + a peptidoglycan chain with N-acetylglucosamine at the non-reducing end |
| Other name(s): |
lytic murein transglycosylase; endolytic murein transglycosylase; lytic transglycosylase; endolytic transglycosylase; MtlA; MltB; MltC; MltD; MltE; MltF; MltG; Slt; RlpA; SleB; SpoIID |
| Systematic name: |
peptidoglycan N-acetylmuramate—N-acetyl-β-D-glucosamine lyase |
| Comments: |
A group of bacterial enzymes that catalyse the non-hydrolytic cleavage of peptidoglycan (PG). The enzymes fragment the polysaccharide chain at the β-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues by an intramolecular cyclization of the N-acetylmuramyl moiety to yield a 1,6-anhydro-N-acetyl-β-D-muramyl product. Includes endolytic transglycosylase activity that fragments the glycan chain internally and exolytic transgylcosylase activity that cleaves a terminal disaccharide from the end of the glycan strand. The MtlG enzyme of Gram-negative bacteria may function to regulate glycan strand length within the PG polymer. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Holtje, J.V., Mirelman, D., Sharon, N. and Schwarz, U. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124 (1975) 1067–1076. [DOI] [PMID: 357] |
| 2. |
Yunck, R., Cho, H. and Bernhardt, T.G. Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria. Mol. Microbiol. 99 (2016) 700–718. [DOI] [PMID: 26507882] |
| 3. |
Dik, D.A., Marous, D.R., Fisher, J.F. and Mobashery, S. Lytic transglycosylases: concinnity in concision of the bacterial cell wall. Crit. Rev. Biochem. Mol. Biol. 52 (2017) 503–542. [DOI] [PMID: 28644060] |
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| [EC 4.2.2.29 created 2023] |
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