A Trypanothione-Dependent Glyoxalase I with a Prokaryotic Ancestry in Leishmania major

Glyoxalase I forms part of the glyoxalase pathway that detoxifies reactive aldehydes such as methylglyoxal, using the spontaneously formed glutathione hemithioacetal as substrate. All known eukaryotic enzymes contain zinc as their metal cofactor, whereas the Escherichia coli glyoxalase I contains ni...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-09, Vol.101 (36), p.13186-13191
Hauptverfasser:	Vickers, Tim J., Greig, Neil, Fairlamb, Alan H., Cerami, Anthony
Format:	Artikel
Sprache:	eng
Schlagworte:	Adducts Amino Acid Sequence Animals Biochemistry Biological Sciences Catalysis Enzyme substrates Enzymes Escherichia coli Eukaryotes Genomes Glutathione - analogs & derivatives Glutathione - physiology Lactoylglutathione Lyase - chemistry Lactoylglutathione Lyase - metabolism Leishmania infantum Leishmania major Leishmania major - enzymology Molecular Sequence Data Nickel Parasites Parasitism Pharmacology Phosphates Pyruvaldehyde - metabolism Spermidine - analogs & derivatives Spermidine - physiology Substrate Specificity Substrates Thiols Thiones Trypanosoma cruzi Zinc
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