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The V88L substitution occurred in the β-strand and low β-sheet content in the secondary structure, as evidenced by the CD analysis data. In conclusion, the V88L substitution increases the enzyme activity and decreases the protein stability.
Deciphering the Role of V88L Substitution in NDM-24 Metallo-β ... - MDPI
Compared with NDM-5 (V88L and M154L), NDM-20 (V88L, M154L, and R270H) improves the hydrolysis activity of some penicillins and cephalosporins but inhibits the activity of carbapenems, which may...
Biochemical characterization of New Delhi metallo-β-lactamase variants ...
NDM-5, -17, -20, -21 and -24 variants which contain V88L substitution (Table 1), have been reported to show improved carbapenemase activity (Hornsey et al., 2011; Liu et al., 2017; Liu et al., 2018b; Liu et al., 2018a; Liu et al., 2019).
Antimicrobial susceptibility of E. coli BL21(DE3)-DH5α carrying...
Compared to NDM-1, NDM-17 had three amino acid substitutions (V88L, M154L, and E170K) that confer significantly enhanced carbapenemase activity. Compared to NDM-5, NDM-17 had only one amino acid substitution (E170K) and slightly increased isolate resistance to carbapenem, as indicated by increased MIC values.
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