Article
A putative low-molecular-mass penicillin-binding protein (PBP) of Mycobacterium smegmatis exhibits prominent physiological characteristics of DD-carboxypeptidase and beta-lactamase.
Microbiology (Reading, England) - 1 May 2015
Bansal Ankita, Kar Debasish, Murugan Rajagopal A, Mallick Sathi, Dutta Mouparna, Pandey Satya Deo, Chowdhury Chiranjit, Ghosh Anindya S
Abstract excerpt
DD-carboxypeptidases (DD-CPases) are low-molecular-mass (LMM) penicillin-binding proteins (PBPs) that are mainly involved in peptidoglycan remodelling, but little is known about the dd-CPases of mycobacteria. In this study, a putative DD-CPase of Mycobacterium smegmatis, MSMEG_2433 is characterized. The gene for the membrane-bound form of MSMEG_2433 was cloned and expressed in Escherichia coli in its active form,...
Topics
- Acetylation
- Amino Acid Motifs
- Conserved Sequence
- Dipeptidases
- Enzyme Activation
- Gene Expression
- Genetic Complementation Test
- Hydrolysis
- Microbial Sensitivity Tests
- Models, Molecular
- Molecular Weight
- Mutation