UDP-N-acetylenolpyruvoylglucosamine reductase, encoded by the gene murB, is a crucial enzyme in the peptidoglycan biosynthesis pathway of bacteria. It catalyzes the reduction of UDP-N-acetylenolpyruvoylglucosamine to UDP-N-acetylmuramic acid, a key step in forming the bacterial cell wall . In Leptospira interrogans, particularly the serogroup Icterohaemorrhagiae serovar Copenhageni, this enzyme plays a vital role in maintaining the structural integrity of the cell wall.
Peptidoglycan, also known as murein, is essential for bacterial cell wall structure, providing rigidity and strength necessary for cell growth and division . The biosynthesis pathway involves several enzymes, including MurA, MurB, MurC, MurD, MurE, and MurF. MurB specifically reduces the enolpyruvyl moiety of UDP-N-acetylenolpyruvoylglucosamine to form UDP-N-acetylmuramic acid, using NADPH as a cofactor .
Recombinant expression of Leptospira interrogans serogroup Icterohaemorrhagiae serovar Copenhageni UDP-N-acetylenolpyruvoylglucosamine reductase (murB) involves cloning the murB gene into an expression vector and expressing it in a suitable host organism. This approach allows for large-scale production of the enzyme for biochemical studies and potential applications in drug development. Given the importance of peptidoglycan in bacterial survival, enzymes like murB are attractive targets for antibacterial drugs .
While specific research findings on the recombinant Leptospira interrogans serogroup Icterohaemorrhagiae serovar Copenhageni UDP-N-acetylenolpyruvoylglucosamine reductase (murB) are scarce, studies on related enzymes and serovars provide valuable insights:
KEGG: lic:LIC_13138
STRING: 267671.LIC13138