Presence of a plant-like glyoxalase II in Candida albicans.
Glyoxalase II from Candida albicans was purified by affinity chromatography on S-carbobenzoxyglutathione-Affi Gel 10. The enzyme was characterized and compared with the glyoxalases II from animal and plant sources. The relative molecular mass is 29 kDa, and the isoelectric point (pI) is 6.0. The acidic pI value appears to be typical for plant glyoxalase II, in contrast to the uniformly basic glyoxalase II pI values from animals. S-D-Lactoylglutathione and S-acetoacetylglutathione are the best substrates, and S-carbobenzoxyglutathione is the best inhibitor of the yeast enzyme. Glutathione derivatives with a thioether bond are not inhibitory. Glyoxalase II from Candida albicans is compared either with animal and plant enzymes.
Talesa
V
V
Department of Experimental Medicine, University of Perugia, Italy.
Rosi
G
G
Bistoni
F
F
Marconi
P
P
Norton
S J
SJ
Principato
G B
GB
D000818:Animals; D002176:Candida albicans / Q000201:enzymology*; D002846:Chromatography, Affinity; D007526:Isoelectric Point; D010944:Plants / Q000201:enzymology; D013379:Substrate Specificity; D013869:Thiolester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000099301:Hydroxyacylglutathione Hydrolase
D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase