Work

Arabidopsis thalianaMitochondrial Glyoxalase 2-1 Exhibits β-Lactamase Activity

Year: 2009

Type: article

Abstract: In an effort to determine the physiological role of Arabidopsis thaliana Glx2-1, we attempted to uncover a substrate for the enzyme. Glx2-1 did not effectively process 192 diverse substrates found in a commercial screen used for microorganism identification or exhibit arylsulfatase, lactonase, or phosphotriesterase activities. However, Glx2-1 does exhibit beta-lactamase activity with k(cat)/KM values from 10(3) to 10(5) M(-1) s(-1). Glx2-1 can hydrolyze cephalosporins and carbapenems, albeit with rate constants slower than those of most metallo-beta-lactamases. The potential role of a beta-lactamase in the mitochondria of plant cells is briefly discussed.

Source: Biochemistry

DOI: 10.1021/bi9010539

Authors: Pattraranee Limphong, George Nimako, Pei W. Thomas, Walter Fast, Christopher A. Makaroff, Michael W. Crowder

Institutions: Miami University, The University of Texas at Austin

Language: English

Topic: Antibiotic Resistance in Bacteria

Subfield: Molecular Medicine

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: University of Miami, National Institute of General Medical Sciences

Awards: Arabidopsis AtETHE1, A model to understand the metabolic role of ETHE1, G8150382125