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Posttranslational Modification
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4.1.1.33
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intracellular glycosylation does not contribute to the difference between the 45000 MW form and the 37000 MW form of the enzyme
4383
4.1.1.33
side-chain modification
subunits of the enzyme homodimer are connected via an intersubunit disulfide bond between the Cys210 residues. When mutagenesis replaces the disulfide-forming cysteine residue with serine, the thermostability of the enzyme is significantly lowered. In the presence of 2-mercaptoethanol, the wild-type enzyme is less stable to heat. The disulfide bond is predominantly formed in the cells
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734098
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