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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Iozef R,Rahlfs S,Chang T,Schirmer H,Becker Kdoi
10.1016/s0014-5793(03)01146-3keywords:
subject
Has Abstractpub_date
2003-11-20 00:00:00pages
284-8issue
3eissn
0014-5793issn
1873-3468pii
S0014579303011463journal_volume
554pub_type
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