The Enzyme Database

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EC 2.7.1.192     
Accepted name: protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N-acetyl-D-muramate[side 1] = [protein]-L-histidine + N-acetyl-D-muramate 6-phosphate[side 2]
Other name(s): murP (gene name); N-acetylmuramic acid PTS permease; EIINAcMur; Enzyme IINAcMur
Systematic name: protein-Nπ-phospho-L-histidine:N-acetyl-D-muramate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Dahl, U., Jaeger, T., Nguyen, B.T., Sattler, J.M. and Mayer, C. Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid. J. Bacteriol. 186 (2004) 2385–2392. [DOI] [PMID: 15060041]
[EC 2.7.1.192 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.192]
 
 
EC 2.7.1.221     
Accepted name: N-acetylmuramate 1-kinase
Reaction: ATP + N-acetyl-D-muramate = ADP + N-acetyl-α-D-muramate 1-phosphate
Glossary: N-acetyl-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose
Other name(s): amgK (gene name)
Systematic name: ATP:N-acetyl-D-muramate 1-phosphotransferase
Comments: The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491–493. [DOI] [PMID: 23831760]
[EC 2.7.1.221 created 2017]
 
 
EC 3.1.3.105     
Accepted name: N-acetyl-D-muramate 6-phosphate phosphatase
Reaction: N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-muramate + phosphate
Other name(s): mupP (gene name)
Systematic name: N-acetyl-D-muramate 6-phosphate phosphohydrolase
Comments: The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Borisova, M., Gisin, J. and Mayer, C. The N-acetylmuramic acid 6-phosphate phosphatase MupP completes the Pseudomonas peptidoglycan recycling pathway leading to intrinsic fosfomycin resistance. mBio 8 (2017) e00092-17. [DOI] [PMID: 28351914]
[EC 3.1.3.105 created 2017]
 
 


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