An aspartyl protease binds the Nterminus of a polypeptide by

An aspartyl protease binds the N-terminus of a polypeptide by specifically binding its sequence: N-Met-Ala-Phe-Lys-Ala-Thr-C

An ideal inhibitor (not a drug) designed based on the hexapeptide substrate of this protease would have a molecular weight between 600 and750 g/mol.

True

False

Phosphorylation of the threonine on the substrate would likely prevent cleavage by the protease.

True

False

Solution

1)

a) True

Explanation: Aspartyl protease binding site open enough to contain as many as six or seven residue surrounding the site of cleavage.

b) False

Explanation: Thr and ser residues shown in the catalytic centre are belived by some to participate in the chemistry by hydrogen bonding to the asparates.