What question did this study set out to answer?

To determine how conserved nonactive-site residues adjacent to the catalytic core modulate the enzymatic activity, substrate specificity, and structural stability of OXA-232 beta-lactamase.

August 16, 2026ACS Infectious Diseases

Deciphering the Role of the Nonactive Site AncillaryResidues in Maintaining the Activity and Substrate Specificity ofthe OXA-232 β-Lactamase

View Full Paper

Ask AI

Bookmark

Authors

ATAjith TejavathIndian Institute of Technology Kharagpur BBBayomi BijuIndian Institute of Technology Kharagpur APAditya Prasad PandaIndian Institute of Technology Kharagpur

Discussion

Member takes

Implication

Biochemical study reveals that nonactive-site residues govern catalytic efficiency in OXA-232 carbapenemase, highlighting new targets for overcoming antibiotic resistance.

Key Points

To determine how conserved nonactive-site residues adjacent to the catalytic core modulate the enzymatic activity, substrate specificity, and structural stability of OXA-232 beta-lactamase.
Generated alanine substitutions at conserved nonactive-site residues (S118A, V120A, L158A, and D159A) within and adjacent to the active-site motifs and omega-loop of OXA-232.
Assessed antimicrobial susceptibility phenotypes, steady-state enzyme kinetics, circular dichroism spectroscopy, and molecular dynamics simulations on wild-type and mutant variants.
Substitutions S118A and D159A sensitized bacteria to penicillins, cephalosporins, and carbapenems, whereas V120A and L158A resulted in substrate-selective susceptibility changes.
All mutants displayed decreased catalytic efficiency compared to wild-type, with L158A and D159A showing deacylation deficiency, S118A and V120A showing acylation defects, and bicarbonate supplementation partially rescuing activity.

Cite This Study

Tejavath et al. (2026) studied this question.

synapsesocial.com/papers/6a8179bcf2fb91fc834ad033 https://doi.org/10.1021/acsinfecdis.6c00512

View Full Paper

Ask AI

Bookmark

Implication

Biochemical study reveals that nonactive-site residues govern catalytic efficiency in OXA-232 carbapenemase, highlighting new targets for overcoming antibiotic resistance.

Deciphering the Role of the Nonactive Site AncillaryResidues in Maintaining the Activity and Substrate Specificity ofthe OXA-232 β-Lactamase

Discussion

Member takes

Implication

Key Points

Cite This Study

Deciphering the Role of the Nonactive Site AncillaryResidues in Maintaining the Activity and Substrate Specificity ofthe OXA-232 β-Lactamase

Discussion

Member takes

Implication

Key Points

Cite This Study

Also Consider

Also Consider