What is H_3N^+ -CH(CH_3)-COO^-? A. leucine B. alanine C. glycine D. cysteine E.

Question

What is H_3N^+ -CH(CH_3)-COO^-? A. leucine B. alanine C. glycine D. cysteine E. pymvate The amino acid residue in chymotrupsin responsible for covalent catelysis is: A. ala B. cys C.asp. D. his E.ser The catalytic cofactor in carbonic anhydrase is: A. Fe B. NADH C. ATP D. PLP E. Zn Which of the following is an aspartatyl protease? A. HIV protease B. chymotrypsin C. trypsin D. carbonic anhydrase E. malate dehydrogenase How does NMP kinase or hexokinase prevent hydrolysis of substrate during ? A. lock and key fit B. activation energy barrier C. induced fit D. water Which is an example of covalent modification of a protein. A. binding an iron ion B. glycation C. binding Acetyl CoA D. water salvation

Explanation / Answer

Answer:

11). B. Alanin

12). E. Ser

Explanation:

Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate. Along with histidine 57 and aspartic acid 102, this serine residue constitutes the catalytic triad of the active site.

13). E. Zn

Explanation:

Zn++ is the cofactor of carboninc anhydrase

14). A. HIV protease

Explanation:

The HIV protease is an example of the aspartyl protease. This protease is a dimer which consists of identical subunits. As a member of the aspartyl protease family, it contains two aspartic acid residues symmetrically located at the bottom of the binding pocket.

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