Identification and characterization of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae.

@article{Sylvester2001IdentificationAC,
  title={Identification and characterization of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae.},
  author={Daniel Sylvester and Enrique L Alvarez and Aniket Patel and Kapila Ratnam and Howard Kallender and Nicola G. Wallis},
  journal={The Biochemical journal},
  year={2001},
  volume={355 Pt 2},
  pages={
          431-5
        }
}
The UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from a Gram-positive pathogen, Streptococcus pneumoniae, was identified and characterized. The enzyme from S. pneumoniae shows 31% identity with the MurB protein from Escherichia coli, and contains the catalytic residues, substrate-binding residues and FAD-binding motif identified previously in the E. coli protein. The gene was cloned into the pET28a+ expression vector, and the 34.5 kDa protein that it encodes was overexpressed in E. coli… CONTINUE READING

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