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Type IV Galactosemia?s Structural and Molecular Biology

Samantha Banford

Type IV galactosemia is a metabolic disorder that is passed down through the family. Galactose autorotate enzyme activity decreases as a result of mutations in the GALM gene. D-galactose and a few other monosaccharides’ - and -anomers are interconverted by this enzyme. The structure of human galactose autorotate is largely composed of -sheets and is monomeric. A glutamate acting as a base and a histidine residue acting as an acid are required for the catalytic mechanism. Together, these residues break open the pyranose ring of d-galactose, allowing the monosaccharide’s first two carbon atoms to freely rotate. The hydroxyl group on carbon 1 may reverse its configuration as a result of this. Early onset cataracts are a symptom of type IV galactosemia, which is similar to type II galactosemia (galactokinase deficiency). However, as a disease that was only recently discovered, its long-term effects are unknown. It is currently unknown what kind of physiological function, if any, galactose mutarotase’s interactions with other monosaccharides play. The potential relationship with different proteins likewise require further examination.