PBP1A Protein, Mycobacterium tuberculosis

PBP1A (penicillin-binding protein 1A) is involved in cell wall formation and plays a crucial role in the synthesis of cross-linked peptidoglycan from lipid intermediates. The enzyme has a bifunctional structure. The penicillin-insensitive transglycosylase N-terminal domain is responsible for the formation of linear glycan chains, and the penicillin-sensitive transpeptidase C-terminal domain promotes the cross-linking of peptide subunits. PBP1A Protein, Mycobacterium tuberculosis is the recombinant PBP1A protein, expressed by E. coli , with tag free. The total length of PBP1A Protein, Mycobacterium tuberculosis is 430 a.a., .

PBP1A (Penicillin-Binding Protein 1A) is a crucial enzyme involved in cell wall formation in bacteria, specifically in the synthesis of cross-linked peptidoglycan from lipid intermediates. The protein exhibits a bifunctional structure with a penicillin-insensitive transglycosylase N-terminal domain responsible for the formation of linear glycan strands, and a penicillin-sensitive transpeptidase C-terminal domain that facilitates the cross-linking of peptide subunits. While PBP1A has limited peptidoglycan hydrolytic activity on its own, it plays a notable role in inhibiting the synergistic peptidoglycan hydrolysis of RipA plus RpfB.

Others

E. coli

Tag Free

P71707 (K391-P820)

887065

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.