PMID:1512209
| Citation |
Marquardt, JL, Siegele, DA, Kolter, R and Walsh, CT (1992) Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase. J. Bacteriol. 174:5748-52 |
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| Abstract |
The Escherichia coli gene murZ, encoding the enzyme UDP-N-acetylglucosamine enolpyruvyl transferase, has been cloned and sequenced. Identified by screening an E. coli genomic library for clones that conferred phosphomycin resistance, murZ encoded a 419-amino-acid polypeptide and was mapped to 69.3 min on the E. coli chromosome. MurZ protein was purified to near homogeneity and found to have the expected UDP-N-acetylglucosamine enolpyruvyl transferase activity. Sequence analysis of the predicted product revealed 44% identity to OrfR from Bacillus subtilis (K. Trach, J.W. Chapman, P. Piggot, D. LeCoq, and J.A. Hoch, J. Bacteriol. 170:4194-4208, 1988), suggesting that orfR may also encode a UDP-N-acetylglucosamine enolpyruvyl transferase enzyme. MurZ is also homologous to the aromatic amino acid biosynthetic enzyme enolpyruvyl shikimate phosphate synthase, the other enzyme known to catalyze an enolpyruvyl transfer. |
| Links | |
| Keywords |
Alkyl and Aryl Transferases; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Base Sequence; Chromosome Mapping; Cloning, Molecular; DNA, Bacterial/genetics; Escherichia coli/genetics; Genes, Bacterial; Molecular Sequence Data; Molecular Weight; Mutagenesis, Insertional; Transferases/genetics |
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