Báo cáo khoa học: UDP-galactose 4-epimerase from Kluyveromyces fragilis – catalytic sites of the homodimeric enzyme are functional and regulated
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UDP-galactose 4-epimerase fromKluyveromyces fragilisis a homodimercontaining one catalytic site and one NAD+as cofactor per subunit. One5¢-UMP, a competitive inhibitor, binds per dimer of epimerase as isolatedand causes inactivation. Addition of 0.2 mminhibitor to the enzyme in vitroleads to three sequential steps: first, the inhibitor binds to the unoccupiedsite; second, the inhibitor bound ex vivo is displaced allosterically; andfinally, both sites are occupied by the inhibitor.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: UDP-galactose 4-epimerase from Kluyveromyces fragilis – catalytic sites of the homodimeric enzyme are functional and regulated
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: UDP-galactose 4-epimerase from Kluyveromyces fragilis – catalytic sites of the homodimeric enzyme are functional and regulated
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