g Gas Raising the pH from TA ees to (e) Doubling the amount of sabstr Decreasing the mount of substrate by half to as 19.ez why are irreversible enzyme inhibitors referred poisons? GROUP PROBLEMS 19.88 The adul DA of riboflavin is 1.3 mg 1f one riboflavin. 100 mL f apple juice contains O.O 4 mg of consume to how much apple juice would an adult have to obtain the RDA? residue to anoth- 19.89 The ability to change a selected amino acid by biochem- er amino acid is referred to as \"point mutation\" hydrolysis ists. Referring to the reaction for peptide bond following in Figure 19.4, speculate on the effects that the mechanism point mutations might have on the chymotrypsin to glutamate shown in Figure 19.4: serine to valine; aspartate side g go Trypsin is an enzyme that cleaves on the C-terminal or i.e., to the right of all basic amino acids in a protein peptide. (Consult Table 18.3 to identify basic amino acid Consider the following peptide. Predict the fragments th would be formed by treatment of this peptide with tryp -1 T en Glv-Arg-Ile-Met-His-Tyr-Trp- 
Serine is the part of catalytic triad that also include histidine and aspartic acid . The highly reactive seryl residue ser195 participate in charge relay network with HIs and Asp the side chain of Ser195 is hydrogen bonded to the corboxyl group of aspartate . This catalitic triad act as a charge relay sysytem.
 If there is conversion of Serine to Valine
 Then it will disturb the active side because serine is needed for the catalytic triad and missing hydroxyl group in Valine will make inactive active site.
 Where as change of aspartate to glutamate will not effect the active that much because the nature of the both amino acid is same and glutamate can also fullfill the reqirement of corboxyl group in catalytic triad. so it can effect but not like serine replacement.