Chapter 20 Protein Metabolism

What is metabolism?

Summary of all chemical reactions to help sustain life

What is catabolism

Breaking down large molecules into smaller ones to release energy

What is Anabolism

Building new large molecules from smaller molecules

To form new molecules

What does ATP stand for

Adenosine Triphosphate

What is a ATP nucleotide molecule composted of

Adenine

Ribose

Three phosphate groups

What is a energy rich compound

Substances with structural features that are able to release energy if they get hydrolyzed

ATP turning into ADP for energy

Catabolism happens in 3 stages. What happens in stage 1

Marcomolecules, such as carb, proeins, lipids are broken down into their simpler monomers through hydrolysis reactions

Proteins - Amino Acids

Lipids - Glycerol Backbone+ Fatty Acids

Carbohydrates - Monosacchardies

What happens in stage 2 of catabolism?

Individual Monomer units get broken down thorugh specific pathways

Forms ATP

What happens in stage 3 of catabolism

This is when the Citric Acid Cycle and ETC occurs to produce massive aount of ATP

What type of digestion happens in the mouth

Mechnical digestion, marcomolcules are being physically broken down, not chemically

What enzymes are located in the stomach to help breakdown proteins

HCL and Pepsin

Pepsin is the active version of what inactive enzume that actually is in the celll walls

Pepsinogen

How is pepsinogen activated to pepsin

Food entering stomach causes pH to drop for the gastric juices

Low pH activates pepsinogen into active pepsin

What does pepsin do chemically to break down proteins

Catalyzes the hydrolys reaction to break the peptide bond holding proteins together

What specific aromatic mino acids does pepsin target?

Tryptophan, Tryosine, Phenylalanine

What specific hydrophobic amino acids does pepsin target

Methionine and Leucine

What enzymes are present in the small intestine

Trypsin, Chymotrypsin, aminoeptidase, Carboxpeptidase

In the small intestine what is trypsinogen converted to in it’s active form

Trypsingoen is converted to Trypsin

In the small intestine what is the inactive chymotrypsin converted to

Chymotrypsin

In the small intestine what do the enzymes trypsin and chymotrypsin do?

Catalyze the hydrolysis reaction of breaking the peptide bonds holding the proteins together

What type of amino acid does the small intestine enzyme Chymotrypsin attack specifically

Carboxyl group of aromatic amino acids (phenylalanine, trytrphan, and tyrosine)

What type of amino acid does the small intestine enzyme Trypsin specically react with

Barboxyl groups of basic amino acids, Lysine and Arginine

How is the innactive enzyme in pancreatic juice Procarboxypeptidase turn into the active form of carboxypeptidase

The enzyme Trypsin cleaves it, turns into active form Carboxypaptidase

What does the enzyme carbooxypeptidase do?

Catalyzes hydrolysis of peptide bonds at the Free carboxyl end of peptide chain