| Literature DB >> 14623080 |
Rimma Iozef1, Stefan Rahlfs, Tammy Chang, Heiner Schirmer, Katja Becker.
Abstract
Recombinant Plasmodium falciparum glyoxalase I (PfGlx I) was characterized as monomeric Zn(2+)-containing enzyme of 44 kDa. The K(M) value of the methylglyoxal-glutathione adduct is 77+/-15 microM, the k(cat) value being 4000 min(-1) at 25 degrees C 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.Entities:
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Year: 2003 PMID: 14623080 DOI: 10.1016/s0014-5793(03)01146-3
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124