3nia

Structural highlights

Function

BLAG2_PSEAI Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth-generation cephalosporins (PubMed:11502535, PubMed:19656947, PubMed:20696873, PubMed:21220532). Has modest carbapenem-hydrolyzing activity (PubMed:11502535, PubMed:19656947, PubMed:25485972). Has cefotaxime-hydrolyzing activity (PubMed:11502535, PubMed:19656947).^{[1] [2] [3] [4] [5]}

See Also

• Beta-lactamase 3D structures

References

1. ↑ Poirel L, Weldhagen GF, Naas T, De Champs C, Dove MG, Nordmann P. GES-2, a class A beta-lactamase from Pseudomonas aeruginosa with increased hydrolysis of imipenem. Antimicrob Agents Chemother. 2001 Sep;45(9):2598-603. PMID:11502535 doi:10.1128/AAC.45.9.2598-2603.2001
2. ↑ Frase H, Shi Q, Testero SA, Mobashery S, Vakulenko SB. Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of beta-lactamases. J Biol Chem. 2009 Oct 23;284(43):29509-13. PMID:19656947 doi:10.1074/jbc.M109.011262
3. ↑ Kotsakis SD, Miriagou V, Tzelepi E, Tzouvelekis LS. Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES β-lactamases. Antimicrob Agents Chemother. 2010 Nov;54(11):4864-71. PMID:20696873 doi:10.1128/AAC.00771-10
4. ↑ Frase H, Toth M, Champion MM, Antunes NT, Vakulenko SB. Importance of position 170 in the inhibition of GES-type β-lactamases by clavulanic acid. Antimicrob Agents Chemother. 2011 Apr;55(4):1556-62. PMID:21220532 doi:10.1128/AAC.01292-10
5. ↑ Stewart NK, Smith CA, Frase H, Black DJ, Vakulenko SB. Kinetic and Structural Requirements for Carbapenemase Activity in GES-Type beta-Lactamases. Biochemistry. 2014 Dec 22. PMID:25485972 doi:http://dx.doi.org/10.1021/bi501052t