Answer:
D. The side chains of D-Arg and D-Lys are not positioned to bind correctly at the active site
Explanation:
Stereospecificity is the ability to distinguish between stereoisomers of of a particular compound. L- and D- structures of compounds in living organisms are usually present in only one form due to stereospecificity. For example, naturally occuring amino acids in proteins are usually present as L-isomers.
Since enzyme are proteins, their active sites are composed of L-amino acid and they show stereospecificity in the reactions they catalyze. In their binding sites, only substrates complementary in structure can bind in order for catalysis to proceed. Therefore, only amino acids in the L- configuration are complementary to the active site of enzymes.
In the case of serine proteases, The side chains of -Arg and D-Lys will not be positioned properly for binding at the binding site of serine proteases, therefore, no catalysis will occur. On the other hand, L-Arg and L-Lys can bind to the catalytic site of serine proteases since they are complementary fits to the active site of the enzymes.
Answer:
A)
Explanation:
because of the polen an all that thing
Answer:
See explanation
Explanation:
In this case, we have to know where we have to do. We have to remove a "Br" and put a methyl group and for this, we need to use a Gilman reaction. (See figure 1). We have to start with <u>bromomethane</u> that reacts with Li to form <u>methyllithium</u>. Then we have to do the reaction with Copper to obtain the Gilman reagent <u>dimethylcopper</u>. Finally, we have to do the reaction with the halide <u>1-bromocyclohexene</u> to form <u>1-methylcyclohexene</u>.
See figure 1
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