please help me explain why is the answer like that for the role of pepsin in protein digestion. explain the peptide bonds and amino acid on the answer
please help me explain why is the answer like that for the role of pepsin in protein digestion. explain the peptide bonds and amino acid on the answer
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Question
please help me explain why is the answer like that for the role of pepsin in protein digestion.
explain the peptide bonds and amino acid on the answer
![Role of pepsin
Pepsin is the most important enzyme in protein digestion. Proteins are broken down
into smaller peptides and amino acids that can be absorbed more easily in the small
intestine. Specific cells within the gastric lining, known as chief cells, release pepsin in
an inactive form, or zymogen form, called pepsinogen. Pepsin functions by cleaving
peptide bonds present in the proteins. Specifically, it cleaves the peptide bonds in the
amino-terminal side of the aromatic amino acid residues which include tyrosine,
tryptophan and phenylalanine. Pepsin can hydrolyze many proteins except, keratin,
spongins or other low molecular weight peptides.
Pepsin is found in : In the gastric chief cells of the stomach lining](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0f226175-9846-4bf7-95c1-61f56233ada1%2F036c75da-81d0-4e37-8e74-445ce3557ff6%2Fags0c9q_processed.png&w=3840&q=75)
Transcribed Image Text:Role of pepsin
Pepsin is the most important enzyme in protein digestion. Proteins are broken down
into smaller peptides and amino acids that can be absorbed more easily in the small
intestine. Specific cells within the gastric lining, known as chief cells, release pepsin in
an inactive form, or zymogen form, called pepsinogen. Pepsin functions by cleaving
peptide bonds present in the proteins. Specifically, it cleaves the peptide bonds in the
amino-terminal side of the aromatic amino acid residues which include tyrosine,
tryptophan and phenylalanine. Pepsin can hydrolyze many proteins except, keratin,
spongins or other low molecular weight peptides.
Pepsin is found in : In the gastric chief cells of the stomach lining
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