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The metallo-ß-lactamases have been further divided by Bush into subgroups based on amino acid sequence identity: the Ba enzymes share a >23% sequence identity, require 2 Zn(II) ions for full activity, prefer penicillins and cephalosporins as substrates, and are represented by metallo-ß-lactamase CcrA from Bacteroides fragilis, the Bb enzymes share a 11% sequence identity with the Ba enzymes, require only 1 Zn(II) ion for full activity, prefer carbapenems as substrates, and are represented by the metallo-ß-lactamase imiS from Aeromonas sobria, and the Bc enzymes have only 9 conserved residues with the other metallo-ß-lactamases, require 2 Zn(II) ions for activity, contain a different metal binding motif than the other metallo-ß-lactamases, prefer penicillins as substrates, and are represented by the metallo-ß-lactamase L1 from Stenotrophomonas maltophilia [ 9 ] .
When the cephalosporins were used as substrates, the S224A and S224K mutants exhibited 2- to 4-fold changes in K m values (Table 3).
On the other hand, the S224D mutant exhibited 3- to 50-fold higher K m values and 2- to 20-fold lower k cat values for the cephalosporins tested.
When cephalosporins were used as substrates, the Y228A and Y228F mutants exhibited K m values that were 6- to 45-fold higher than those observed for wild-type L1 (Table 3).
The Tyr228 mutants exhibited < 4-fold change in k cat values for the cephalosporins tested (Table 3), suggesting that Tyr228 is not playing a large role in catalysis.
When the cephalosporins were used as substrates for the F158A mutant, the K m values observed were 7- to 31-fold higher than those determined for wild-type L1, and surprisingly, the k cat values were 2- to 31-fold higher than those exhibited by wild-type L1 (Table 3).
The F158A mutant exhibited higher K m values when using the cephalosporins as substrates, suggesting an interaction of the cephalosporins' substituents with the phenylalanine on the loop that extends over the active site.
Beta-lactamases have been widely investigated for their role in the metabolism of antibiotics including cephalosporins and penicillins.
Due to the slow non-enzymatic degradation of the cephalosporins in solution [ 39 ] , the ratio of toxicity of cephalosporin-containing prodrugs to their corresponding free drugs is generally not very high.
The use of cephalosporins in our study was less than that reported in the literature [ 20 21 ] .
The isolated organisms are becoming resistant to the commonly used antibiotics and cephalosporins may have to be prescribed in resistant cases.
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