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Structure of the novel monomeric glyoxalase I from Zea mays
(Wiley Blackwell Publishing, Inc, 2015-10)
The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated ...
Mechanism of action of glycyrrhizin against Plasmodium falciparum
(Fundação Oswaldo Cruz. Instituto Oswaldo Cruz., 2021)
Metal-dependent inhibition of glyoxalase II: a possible mechanism to regulate the enzyme activity
(ElsevierNew York, 2010-07)
Glyoxalase II (GLX2, EC 3.1.2.6., hydroxyacylglutathione hydrolase) is a metalloenzyme involved in crucial detoxification pathways. Different studies have failed in identifying the native metal ion of this enzyme, which ...
Deciphering the number and location of active sites in the monomeric glyoxalase I of Zea mays
(Wiley Blackwell Publishing, Inc, 2019-08)
Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into d-lactate via a glutathione ...
A proposed reaction mechanism for maize monomeric glyoxalase I
(Sociedad Argentina de Biofísica, 2019)
Detoxification of methylglyoxal, a toxic by-product of central sugar metabolism, is a major issue for all forms of life. The glyoxalase pathway evolved to effectively convert methylglyoxal into D-lactate via a glutathione ...
Metilglioxal: uma toxina endógena?
(Sociedade Brasileira de Química, 2010-01-01)
Methylglyoxal is a very reactive α-oxoaldehyde putatively produced by glycolysis, cytochrome P450-catalyzed acetone oxidation and aminoacetone oxidation. Methylglyoxal has been pointed as a substrate for the glyoxalase ...
Metilglioxal: uma toxina endógena?
(Sociedade Brasileira de Química, 2010)
Methylglyoxal is a very reactive α-oxoaldehyde putatively produced by glycolysis, cytochrome P450-catalyzed acetone oxidation and aminoacetone oxidation. Methylglyoxal has been pointed as a substrate for the glyoxalase ...