A Tyrosine Residue Along with a Glutamic Acid of the Omega-Like Loop Governs the Beta-Lactamase Activity of MSMEG_4455 in Mycobacterium smegmatis

• Published in: The Protein Journal Vol. 36; no. 3; pp. 220 - 227
• Main Authors: Bansal, Ankita, Kar, Debasish, Pandey, Satya Deo, Matcha, Ashok, Kumar, N. Ganesh, Nathan, Soshina, Ghosh, Anindya S.
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2017; Springer; Springer Nature B.V
• Subjects: Alanine; Analysis; Animal Anatomy; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Beta lactamases; beta-Lactamases - chemistry; beta-Lactamases - genetics; Biochemistry; Bioorganic Chemistry; Carbenicillin; Chemistry; Chemistry and Materials Science; Drug resistance in microorganisms; E coli; Enzymatic activity; Escherichia coli; Glutamate; Glutamic acid; Glutamic Acid - chemistry; Glutamic Acid - genetics; Histology; Hydrogen bonds; Hydrolysis; Minimum inhibitory concentration; Morphology; Mycobacterium smegmatis - enzymology; Mycobacterium smegmatis - genetics; Organic Chemistry; Penicillin; Phenols; Phenylalanine; Protein Structure, Secondary; Structure-function relationships; Ticarcillin; Tyrosine; Tyrosine - chemistry; Tyrosine - genetics; Beta-lactamase; Mycobacterium; Site-directed mutagenesis; Penicillinase

Mycobacterial beta-lactamases are involved in exerting beta-lactam resistance, though many of these proteins remain uncharacterized. Here, we have characterized MSMEG_4455 of Mycobacterium smegmatis as a beta-lactamase using molecular, biochemical and mutational techniques. To elucidate its nature i...