Distinct roles of galactose-1P in galactose-mediated growth arrest of yeast deficient in galactose-1P uridylyltransferase (GALT) and UDP-galactose 4′-epimerase (GALE)
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منابع مشابه
Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.
UDP-galactose 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose metabolism. Within recent years the enzyme from Escherichia coli has been studied extensively by both biochemical and X-ray crystallographic techniques. One of several key features in the catalytic mechanism of the enzyme involves the putative rotation of a 4'-ketopyranose intermedia...
متن کاملThe molecular architecture of galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae.
The metabolic pathway by which beta-D-galactose is converted to glucose 1-phosphate is known as the Leloir pathway and consists of four enzymes. In most organisms, these enzymes appear to exist as soluble entities in the cytoplasm. In yeast such as Saccharomyces cerevisiae, however, the first and last enzymes of the pathway, galactose mutarotase and UDP-galactose 4-epimerase, are contained with...
متن کاملUDP-galactose 4-epimerase from Kluyveromyces fragilis: equilibrium unfolding studies.
UDP-galactose 4-epimerase from yeast (Kluyveromyces fragilis) is a homodimer of total molecular mass 150 kDa having possibly one mole of NAD/dimer acting as a cofactor. The molecule could be dissociated and denatured by 8 M urea at pH 7.0 and could be functionally reconstituted after dilution with buffer having extraneous NAD. The unfolded and refolded equilibrium intermediates of the enzyme be...
متن کاملUDP-galactose 4-epimerase from Escherichia coli: equilibrium unfolding studies.
UDP-galactose 4-epimerase from Escherichia coli is a homodimer of 39 kDa subunit with non-covalently bound NAD acting as cofactor. The enzyme can be reversibly reactivated after denaturation and dissociation using 8 M urea at pH 7.0. There is a strong affinity between the cofactor and the refolded molecule as no extraneous NAD is required for its reactivation. Results from equilibrium denaturat...
متن کاملUDP-galactose 4' epimerase (GALE) is essential for development of Drosophila melanogaster.
UDP-galactose 4' epimerase (GALE) catalyzes the interconversion of UDP-galactose and UDP-glucose in the final step of the Leloir pathway; human GALE (hGALE) also interconverts UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine. GALE therefore plays key roles in the metabolism of dietary galactose, in the production of endogenous galactose, and in maintaining the ratios of key substrates for ...
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ژورنال
عنوان ژورنال: Molecular Genetics and Metabolism
سال: 2008
ISSN: 1096-7192
DOI: 10.1016/j.ymgme.2007.09.012