Cathepstain X with an amino terminal amphiphilic alpha helix sequence and a carb

Question

Cathepstain X with an amino terminal amphiphilic alpha helix sequence and a carboxyl terminal KDEL.

When present in growth media, chotropic salts disupts protein folding and impair yeast growth. If cathepsain X is localized to the ER lumen, it facilitates protein folding and allows yeast to grow in the presence of these salts. Predict how expression of cathepsain X fusion protein will influence yeast growth when cells are incubated in media containing chaoptropic salts. be sure to justify your answer in the context of protein localization.

Explanation / Answer

Cathapsin X is a type of cysteine type carboxy peptidase , the enzyme catalyses the following reaction ,It causes the release of the C terimnal amino acids with braod specificity but lacks the action on the c terminal proline it shows the weak exopeptidase activity ,It is a lysosomal cysteine protease it has narrow substrate specificity .They also have the integrin mediated signal transduction integrins are heterodimeric , glycosyslated, transmemberane ahesion rceptors .The loops in the cathepsin X has the less exopeptidase activity reduce the number of the binding site ,substrate binding , the mini loop utilise the histidine residue to dcok the c terminal residue , These help in the removal of the substartye which are impure ,as they are very substarte specific which results in the cleavge of the ant chaoptropic agents which results in the growth of the yeast in the cells

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