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Sagot :
The enzyme separase, which is kept dormant by securin until the APC/C complex degrades it, cleaves cohesin.
Discussion about the enzymes:
- At the metaphase-to-anaphase shift, the cysteine protease separase cleaves the Scc1 component of cohesin, signaling the start of chromosome segregation.
- Prior to metaphase, securin, a firmly bound protein, inhibits separase by blocking the separase enzymatic activity with a pseudosubstrate motif. Therefore, we create a technique for creating cloned, securin-free human separase in order to study the affinity and specificity, and control of separase.
- We find that the Scc1 substrate has an LPE motif that is different from the catalytic domain and necessary for quick and precise substrate breakdown that uses this enzyme. Researchers show that the retained LPE motif found in securin prevents the separase from binding to the Scc1 LPE motif.
Learn more about separase here:
https://brainly.com/question/7248007
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