Protein Denaturation Flashcards by LEA ROS MANALASTAS

Sum total of all the biochemical reactions

Metabolism

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Large biochemical molecules → smaller ones

Catabolism

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Small biochemical molecules → larger ones

Anabolism

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interconversion of chemical compounds in the body

Metabolism

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Another term for catabolism

“exergonic/exothermic”

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Another term for anabolism

“endergonic/endothermic”

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occurs at the “crossroads” of metabolism

Amphibolism

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pathways taken by individual molecules, their interrelationships

Metabolism

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Produce more energy than they consume, releasing the chemical energy stored in organic molecules

Catabolism

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Consume more energy than they produce

Anabolism

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Acts as links between the anabolic and catabolic pathways

Amphibolism

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Release energy producing reducing equivalents via the respiratory chain

Catabolism

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mechanisms that regulate the flow of metabolites through the pathways

Metabolism

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Involving oxidative reactions

Catabolism

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Consume more energy than they produce

Anabolism

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Occurs in the mitochondria

Catabolism

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Occurs in the endoplasmic reticulum

Anabolism

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Amphibolism steps

1st
breaks down metabolites (proteins, fats and carbohydrates) into smaller molecules and

2nd
produces energy - then used to synthesize more complex molecules from simple ones

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Term for protein → amino acid → new protein

Protein turnover/interconversion

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Series of consecutive biochemical reactions that convert a starting material into an end product

Metabolic Pathway

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Types of Metabolic Pathway

Linear
Cyclic
Branched

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series of reactions generates a final product

Linear Metabolic Pathway

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series of reactions regenerates the first reactant

Cyclic Metabolic Pathway

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reacting molecule (reactant) that binds to the enzyme (complex formation)

Substrate

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catalyzes the reaction by acting upon the given substrates

Enzyme

Produced when substrate binds to the enzyme Intermediate reaction species that is /are formed

Product

required by enzymes to further exert catalytic activity an organic molecule

CoEnzyme

Another term for Product

(enzyme-substrate complex)

Glutamate + Water products

a-ketoglutarate + Ammonium

a-ketoglutarate + Ammonium substrate

Glutamate + Water products

Glutamate + Water enzyme

Glutamate Dehydrogenase

Glutamate Dehydrogenase coenzyme

NAD (Nicotinamide adenine dinucleotide)

Central Metabolic Pathway Steps

Stage 1: Digestion and Hydrolysis Stage 2: Degradation Stage 3: Oxidation (citric acid cycle and electron transport)

Digestion and Hydrolysis Pathway

Large Molecules ↓ Smaller Molecules ↓ Blood Stream

Degradation Pathway

Molecules ↓ two- and three-carbon compounds

Oxidation (citric acid cycle and electron transport) Pathway

Small molecules ↓ ATP

proteins are degraded and resynthesized

Protein Turnover

Uses of Amino Acids from Amino Acid Pool

1. Protein synthesis 2. Synthesis of non-protein nitrogen-containing compounds 3. Synthesis of non-essential amino acids 4. Production of energy

- 75% of the free amino acids; replace old tissue (protein turnover) and build new tissue (growth)

Protein synthesis

Synthesis of non-protein nitrogen-containing compounds

purines and pyrimidines of nucleic acids, the heme of hemoglobin, neurotransmitters such as acetylcholine and serotonin, hormones such as insulin

Location where partial digestion by the enzyme pepsin and its acid

Stomach

Location where further protein digestion by enzymes released by the organ

Pancreas

Location where final digestion of protein to amino acids takes place mostly inside the cells of this organ

Small intestine

Location where the amino acid absorbed into the portal wein and transported to this organ where they enter the general bloodstream

liver

Location where dietary protein present in the feces

Anus

Protein Digestion in the Stomach Chemical Reactions:

A. Protein denaturation B. Protein hydrolysis

breakdown of the tertiary and secondary structure of proteins to expose them

Protein denaturation

Protein denaturation enzyme

Hydrochloric acid in gastric juice

Hydrochloric acid in gastric juice pH

(pH 1.5 to 2.0)

The cleaving into smaller peptide chains

Protein hydrolysis

HCl Activates _________ to ___________:

zymogen pepsinogen to pepsin

Pepsin affects hydrolysis of ________ of peptide bonds in proteins

10%

Digested protein by the stomach

chyme

which cells produce HCl acid in the stomach

Parietal cells

Breakdown of peptide bonds

Protein Digestion

secreted by intestinal mucosal cells

Aminopeptidase

Enzymes in pancreatic juice and neutralizes acidic chyme

Trypsin, Chymotrypsin, and Carboxypeptidase

Trypsin, Chymotrypsin, and Carboxypeptidase pH

7.0 and 8.0

Activated form Trypsinogen

Trypsin

Activated form Chymotrypsinogen

Chymotrypsin

Activates Trypsinogen

[Enteropeptidase]

Activates Chymotrypsinogen

[Trypsin]

Enzymes: that continue to break down proteins into peptides

Trypsin, Chymotrypsin, Elastase

Enzymes: splits off the amino acid at the carboxyl end of a peptide

Carboxypeptidase

Enzymes: cleaves off the amino acid at the amino end of a peptide

Aminopeptidase

Enzymes: splits dipeptides into single AA

Dipeptidase

Digest terminal peptide bonds to release amino acids

Exopeptidase

Types of exopeptidase

Aminopeptidase Carboxypeptidase

digest internal peptide bonds

Endopeptidase

Connects small intestine to the liver

Portal vein

amino acid to liver cell through ATP

Active transport

Involves only the shuffling of amino groups among the amino acids

Transamination

Protein Degradation: Chemical reactions

Transamination Oxidative Deamination

Removal of the α-amino groups – 1st step in the catabolism of most L-amino acids (liver)

Protein Degradation

Protein Degradation Mechanism:

transfer of an amino (NH2) group from an amino acid to a keto acid

Protein Degradation Enzyme:

aminotransferases or transaminases

Most amino acid product in transaminase

L-glutamate

Protein Degradation Purpose:

to collect the amino groups from many different amino acids in the form of L-glutamate: o functions as an amino group donor for biosynthetic pathways or for excretion pathways → elimination of nitrogenous waste products o Cells contain different types of aminotransferases

Intermediate carrier of amino groups at the active site of aminotransferases

Prosthetic group

Coenzyme form of pyridoxine, or vitamin B6

Pyridoxal phosphate

α-amino acid is converted → α - keto acid (used for a variety of reactions, including energy generation) with release of an ammonium ion

Oxidative Deamination

Occurs primarily in liver (hepatocytes) and kidney mitochondria and 2nd step of amino acid degradation

Oxidative Deamination

Oxidative Deamination Mechanism:

ammonium ion (NH4) is liberated from the glutamate formed by transamination

Oxidative Deamination Enzyme:

L-glutamate dehydrogenase

Oxidative Deamination Purpose:

amino group of L-glutamate molecules must be removed from glutamate to prepare them for excretion

amino acids that can become glutamate

Arginine Histidine Proline Glutamine

Glutamate turn to ___________ by glutamate dehydrogenase

α - ketoglutarate