Journal article

Publication year: 2003

Pages: 284-288

Journal: FEBS Letters

Volume number: 554

Issue number: 3

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/S0014-5793(03)01146-3

Publisher: Wiley

Abstract: 
Recombinant Plasmodium falciparum glyoxalase (PfGlx 1) was characterized as monomeric Zn2+-containing en zyme of 44 kDa. The K-M value of the methylglyoxal-glutathione adduct is 77 +/- 15 muM, the k(cat) value being 4000 min(-1) at 25degreesC and pH 7.0. PfGlx I consists of two halves, each of which is homologous to the small 2-domain glyoxalase I of man. Both parts of the pfglx I gene were overexpressed; the C-terminal half of PfGlx I was found to be a stable protein and formed an enzymatically active dimer. These results support the hypothesis of domain-swapping and subunit fusion as mechanisms in glyoxalase I evolution. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Harvard Citation style: Iozef, R., Rahlfs, S., Chang, T., Schirmer, H. and Becker, K. (2003) Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion, FEBS Letters, 554(3), pp. 284-288. https://doi.org/10.1016/S0014-5793(03)01146-3

APA Citation style: Iozef, R., Rahlfs, S., Chang, T., Schirmer, H., & Becker, K. (2003). Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion. FEBS Letters. 554(3), 284-288. https://doi.org/10.1016/S0014-5793(03)01146-3