Amino Acid Sequences for TEM, SHV and OXA Extended-Spectrum and Inhibitor Resistant ß-Lactamases

These tables grew out of an attempt to standardize the nomenclature for the growing number of TEM ß-lactamases and the intent to make it easier for investigators to discover if particular amino acid substitutions had been described before (1). To the TEM table we have added tables for SHV and OXA enzymes with extended-spectrum or other properties and have provided references to sources for sequence information. As of May, 2001, we have added a listing for other rapidly growing enzyme groups, including OXA-, CTX-M-, CMY-, IMP-, VIM-, KPC-, GES-, PER-, and VEB- types. Additional data about AmpC-type ß-lactamases can be found in (2). A web site for OKP-, OXY-, and LEN- ß-lactamases can be found at http://www.pasteur.fr/recherche/genopole/PF8/betalact_en.html. More references about the ß-lactamases themselves can be found in reviews by Bush, Jacoby, & Medeiros (3), Livermore (4), Bradford (5), Jacoby & Munoz-Price (6), and Paterson & Bonomo (7). Structural considerations have been reviewed by Knox (8). Residue numbering for TEM and SHV enzymes follows Ambler et al. (9). More on ß-lactamase nomenclature can be found in (10).

To qualify for a new number the enzyme must have been found in nature and not created in the laboratory. The amino acid sequence of the native enzyme and not merely the nucleotide sequence should be unique. Changes in the promoter sequence do not qualify as new derivatives. Substitutions in the signal sequence do not alter the mature protein but since they may provide a useful epidemiological marker and have already been used to define new varieties, such changes are considered valid. We will accept any amino acid alteration as defining a new variety, even if no functional change is currently evident, since most enzymes will have been sequenced because of a change in properties and an effect on interaction with a future substrate or inhibitor is always possible. We will also assign numbers sequentially independent of ß-lactamase properties. Application for a new enzyme number can be made to either of us. With the investigator's permission the new sequence can be made public before publication so that the information is available without delay.

The TEM and SHV tables can be downloaded as Excel files by clicking on the Excel logo next to the table title.

1. Bush, K. and G. Jacoby. Nomenclature of TEM ß-lactamases. 1997. J. Antimicrob. Chemother. 39:1-3.

2. Philippon, A, G. Arlet, G.A. Jacoby. 2002. Plasmid-determined AmpC-type ß-lactamases. Antimicrob Agents Chemother. 46:1-11.

3. Bush, K., G.A. Jacoby, and A.A. Medeiros. 1995. A functional classification scheme for ß-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.

4. Livermore, D. M. 1995. ß-Lactamases in laboratory and clinical relevance. Clin. Microbiol. Rev. 8:557-584.

5. Bradford, P. A. 2001. Extended-spectrum ß-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat. Clin. Microbiol. Rev. 14:933-951.

6. Jacoby, G.A., and Munoz-Price, L.S. 2005. The new ß-lactamases. New Engl. J. Med. 352:380-391.

7. Paterson, D. L., and R. A. Bonomo. 2005. Extended-spectrum ß-lactamases: a clinical update. Clin. Microbiol. Rev. 18:657-686.

8. Knox, J.R. 1995. Extended-spectrum and inhibitor-resistant TEM-type ß-lactamases: mutation, specificity, and three-dimensional structure. Antimicrob. Agents Chemother. 39:2593-2601.

9. Ambler, R.P., A.F.W. Coulson, J.-M. Frère, J.-M. Ghuysen, B. Joris, M. Forsman, R.C. Levesque, G. Tiraby, and S.G. Waley. 1991. A standard numbering scheme for the class A ß-lactamases. Biochem. J. 276:269-272.

10. Jacoby, G.A. ß-Lactamase nomenclature. 2006. Antimicrob Agents Chemother 50:1123-1129.

Click here for the TEM Extended-Spectrum and Inhibitor Resistant ß-Lactamases table

	SHV Extended-Spectrum and Inhibitor Resistant ß-Lactamases