重组Penicillin-binding蛋白1A (His tag)

补充信息

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Penicillin-binding protein 1A (PBP 1A) also known as PBP1a is an enzyme important for bacterial cell wall biosynthesis. It plays an essential role in the synthesis of peptidoglycan a vital polymer that provides structural strength to the bacterial cell wall. PBP 1A is expressed in the cytoplasmic membrane of many bacteria including E. coli and other Gram-negative bacterial species. It has a molecular mass of about 87 kDa and has transpeptidase activity which links the peptide chains of the peptidoglycan helping to maintain cell wall integrity and shape.

Biological function summary

PBP 1A acts in the later stages of bacterial cell wall synthesis. It catalyzes the cross-linking of peptidoglycan chains which is an important process for bacterial growth and division. PBP 1A is part of a complex that includes multiple penicillin-binding proteins working together to ensure the proper formation and remodeling of the cell wall during cell division. The enzyme is central to these processes making it a target for beta-lactam antibiotics which aim to inhibit its activity disrupting bacterial cell wall synthesis and ultimately leading to cell death.

Pathways

The involvement of PBP 1A in peptidoglycan biosynthesis places it within the bacterial cell wall synthesis pathway an essential process for bacterial viability. PBP 1A functions alongside other PBPs such as PBP 1B 2 and 3 which coordinate to complete the peptidoglycan layer. Additionally PBP 1A interacts with other proteins like MurG and FtsI that participate in the assembly and elongation of the bacterial cell wall integrating it into the greater peptidoglycan assembly pathway.

PBP 1A is significant due to its role in antibiotic resistance. Beta-lactam antibiotics like penicillins and cephalosporins target PBPs to inhibit cell wall synthesis. Mutations or overexpression of PBP 1A can lead to antibiotic resistance presenting challenges in treating bacterial infections such as pneumonia and sepsis. This resistance is often linked to alterations in other PBPs such as PBP 2a in methicillin-resistant Staphylococcus aureus (MRSA) further complicating therapy and requiring alternative treatment strategies.