Lactamase Nomenclature
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《抗菌试剂及化学方法》
Lahey Clinic, Burlington, Massachusetts
INTRODUCTION
In the beginning, ?-lactamases were designated by the name of the strain or plasmid that produced them, a practice that persists in such enzyme names as PC1 or P99. In 1975, the application of isoelectric focusing for ?-lactamase characterization allowed many more enzymes to be distinguished (84). Subsequent ?-lactamase nomenclature has been nothing if not creative. The enzymes have been named after substrates, biochemical properties, peculiarities of sequence, location of their discovery, location of the gene on the chromosome, strains of bacteria, the patient providing a sample, and, least modestly, the investigators who described them. One enzyme has even been named by what it is not (Nmc, standing for not metalloenzyme carbapenemase) (91). Figure 1 shows the frequency with which novel enzymes have been described in the literature and reflects not only the pace of discovery and increasingly sophisticated means of differentiating ?-lactamases but also fashions in naming. Only recently have letters and not strain numbers been used consistently for designation.
In time, some ?-lactamases have become families of more or less closely related enzymes. Currently, 150 TEM, 88 SHV, 88 OXA, 53 CTX-M, 22 IMP, 12 VIM, and smaller numbers in other enzyme families have been described (http://www.lahey.org/studies). The TEM and SHV families are closely related, with individual members differing by only one to seven amino acids. Other families, for example, the CTX-M and IMP families, differ among themselves by as much as 20% in amino acid composition, while members of the OXA family can have almost 80% difference, because they have been grouped by activity on oxacillin and related substrates and not by primary structure. The Klebsiella oxytoca K1 or KOXY enzyme has also been subdivided into a growing series of OXY ?-lactamases (38).
A few enzymes have been given more than one name (Table 1). Other synonymous names undoubtedly await recognition as more bla genes are sequenced. Some enzymes were given provisional names until their sequence demonstrated them to be TEM or SHV derivatives; examples are shown in Table 1, and others can be found at http://www.lahey.org/studies.
Sometimes, one name rather than another has caught on. Thus, CTX-M (6), rather than MEN (18) or TLB (Toho-1-like ?-lactamase) (158), came to designate that family of enzymes, and the Toho enzymes have recently been assigned CTX-M numbers (http://www.lahey.org/studies). Some names lost their logic after being created but are still in use; thus, the "Pseudomonas-specific enzymes," PSE-1, PSE-2, and PSE-4, were soon found in Escherichia coli and other Enterobacteriaceae (76, 88, 123), and some CTX-M enzymes hydrolyze ceftazidime more efficiently than cefotaxime (112). For a time, plasmid-encoded ?-lactamases were designated with all capital letters and chromosomally determined enzymes with only the first letter capitalized, but this distinction no longer holds. Since DNA sequencing facilitated characterization, the pace of discovery and naming has increased further. Because the rationale for existing names has not previously been collected in one place, a list of derivations follows with apologies for any omissions (Table 2). When the derivation was not provided in the original reference, it has been checked, if possible, with the originating author.
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INTRODUCTION
In the beginning, ?-lactamases were designated by the name of the strain or plasmid that produced them, a practice that persists in such enzyme names as PC1 or P99. In 1975, the application of isoelectric focusing for ?-lactamase characterization allowed many more enzymes to be distinguished (84). Subsequent ?-lactamase nomenclature has been nothing if not creative. The enzymes have been named after substrates, biochemical properties, peculiarities of sequence, location of their discovery, location of the gene on the chromosome, strains of bacteria, the patient providing a sample, and, least modestly, the investigators who described them. One enzyme has even been named by what it is not (Nmc, standing for not metalloenzyme carbapenemase) (91). Figure 1 shows the frequency with which novel enzymes have been described in the literature and reflects not only the pace of discovery and increasingly sophisticated means of differentiating ?-lactamases but also fashions in naming. Only recently have letters and not strain numbers been used consistently for designation.
In time, some ?-lactamases have become families of more or less closely related enzymes. Currently, 150 TEM, 88 SHV, 88 OXA, 53 CTX-M, 22 IMP, 12 VIM, and smaller numbers in other enzyme families have been described (http://www.lahey.org/studies). The TEM and SHV families are closely related, with individual members differing by only one to seven amino acids. Other families, for example, the CTX-M and IMP families, differ among themselves by as much as 20% in amino acid composition, while members of the OXA family can have almost 80% difference, because they have been grouped by activity on oxacillin and related substrates and not by primary structure. The Klebsiella oxytoca K1 or KOXY enzyme has also been subdivided into a growing series of OXY ?-lactamases (38).
A few enzymes have been given more than one name (Table 1). Other synonymous names undoubtedly await recognition as more bla genes are sequenced. Some enzymes were given provisional names until their sequence demonstrated them to be TEM or SHV derivatives; examples are shown in Table 1, and others can be found at http://www.lahey.org/studies.
Sometimes, one name rather than another has caught on. Thus, CTX-M (6), rather than MEN (18) or TLB (Toho-1-like ?-lactamase) (158), came to designate that family of enzymes, and the Toho enzymes have recently been assigned CTX-M numbers (http://www.lahey.org/studies). Some names lost their logic after being created but are still in use; thus, the "Pseudomonas-specific enzymes," PSE-1, PSE-2, and PSE-4, were soon found in Escherichia coli and other Enterobacteriaceae (76, 88, 123), and some CTX-M enzymes hydrolyze ceftazidime more efficiently than cefotaxime (112). For a time, plasmid-encoded ?-lactamases were designated with all capital letters and chromosomally determined enzymes with only the first letter capitalized, but this distinction no longer holds. Since DNA sequencing facilitated characterization, the pace of discovery and naming has increased further. Because the rationale for existing names has not previously been collected in one place, a list of derivations follows with apologies for any omissions (Table 2). When the derivation was not provided in the original reference, it has been checked, if possible, with the originating author.
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