Key result
Cysteines 41 and 390 are essential for human GlcNAc 2-epimerase activity and stability.
Why the study?
The relationship between structure and function of recombinant human renin-binding protein as a GlcNAc 2-epimerase was not fully understood, particularly the role of cysteine residues.
This study identifies specific cysteine residues critical for the enzymatic activity and stabilization of human renin-binding protein acting as GlcNAc 2-epimerase.
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Cys41/Cys390 merit priority in structural studies; leaves open in vivo roles and therapeutic targeting.
Takahashi et al. (2001) studied this question. C-terminal deletion and multi-cysteine/serine mutants of rhGlcNAc 2-epimerase vs. Wild-type enzyme was evaluated on Enzymatic activity. Mutational analysis of recombinant human GlcNAc 2-epimerase revealed that cysteines 41 and 390 are critical for enzyme activity or stabilization, whereas cysteines 125, 210, 239, and 302 are not.
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