Download Free Medical Protein Metabolism PowerPoint Presentation

Protein Metabolism PowerPoint Presentation

DOWNLOAD MEDICAL POWERPOINT PRESENTATION

About This Presentation

Description : Check out this medical presentation on Alanine Aminotransferase (alanine transaminase), which is titled "Protein Metabolism", to know about the summary of protein digestion in the human body and the possible fates for amino acid degradation products.

Tags : Alanine Aminotransferase, alanine transaminase, Protein Metabolism, protein digestion, amino acid degradation products

Published on : Jul 05, 2021 | Views : 4379 | Downloads : 13

Shareable Url :

Embed Code :

Comment

Transcript

Slide 1-

Protein Metabolism
Slide 2-

Protein Digestion Protein breakdown begins in the stomach. No protein hydrolyzing enzymes are found in saliva. Hydrolysis (10% of peptide bonds) & denaturization by pepsin enzyme & HCl acid produce short chain polypeptides in the stomach. Trypsin, chymotrypsin, & carboxypeptidase from Pancreatic juices, and Aminopeptidase from cells in the small intestine Brush Zone create “free” amino acids.
Slide 3-

Free amino acids are absorbed thru intestinal wall via active transport. Enter bloodstream and are brought to cells. The total supply of free amino acids available is called: the Amino Acid Pool. 3 sources of “free” amino acids: Dietary protein breakdown Biosynthesis of amino acids in the Liver Protein turnover (I prefer apple turnovers) Protein turnover is the breakdown & re-synthesis of body protein: Old tissues Damage Recycling enzymes & hormones
Slide 4-

Summary of protein digestion in the human body.Possible fates for amino acid degradation products.
Slide 5-

Transamination and Oxidative Deamination: Two steps in degrading amino acids 1) remove -amino group 2) breakdown & process carbon skeleton Release of an amino group is also two steps: 1) Transamination 2) Oxidative deamination
Slide 6-

Central role of glutamate: Amino acids: Glutamate, aspartate, alanine & glutamine present in higher concentrations in mammalian cells. Have metabolic functions as well as roles in proteins. Glutamate is the most important, metabolically.
Slide 7-

Some transaminases are used for diagnosing disorders: enzyme alanine aminotransferase Escapes in large amounts from dead or dying liver tissue. Measured in blood samples for diagnostic purposes.
Slide 8-

Transaminase enzyme aspartate aminotransferase very active enzyme inside heart cells. Also escapes in large amounts from dead or dying heart tissues & enters bloodstream. Measured in blood for diagnosing myocardial infarction.
Slide 9-

Trans-deamination (sum it up) Most transaminases share a common substrate and product (oxoglutarate and glutamate) with the enzyme glutamate dehydrogenase. This permits a combined N excretion pathway for individual amino acids: "trans-deamination.” Glutamate has a central role in the overall control of nitrogen metabolism. a.k.a.-ketoglutarate
Slide 10-

Oxidative Deamination The glutamate produced from the transamination step is then deaminated by oxidative deamination using the enzyme glutamate dehydrogenase: And away I go! Recycles back to a ketodiacid & releases ammonia
Slide 11-

Glutamate dehydrogenase [GluDH] will reversibly convert glutamate to -ketoglutarate and -ketoglutarate to glutamate. Deamination reaction uses NAD+ reverse reaction uses NADPH Uses both NAD+ and NADPH – how to regulate it?
Slide 12-

Urea cycle: Ammonium salts (NH4+) are toxic compounds. Oxidative deamination converting glutamate to -ketoglutarate is an easily shifted equilibrium reaction. Ammonium ions building up favors the synthesis of excessive amounts of glutamate, decreasing the Krebs cycle intermediate -ketoglutarate. This in turn decreases ATP production, and that affects the nervous system. The answer is Urea:
Slide 13-

The inputs to the urea cycle are NH3, CO2 and aspartic acid and ATP. The outputs are urea, ADP and fumaric acid. The carbonyl group of urea is derived from CO2 Ammonia contributes one of the amine groups on urea
Slide 14-

The four-step urea cycle in which carbamoyl phosphate is converted to urea.
Slide 15-

The nitrogen content of the various compounds that participate in the urea cycle. Does it remind you of the Krebs cycle in any way?
Slide 16-

Fumarate from the urea cycle enters the Krebs cycle. Aspartate produced from oxaloacetate of the Krebs cycle enters the urea cycle. Oxaloacetate has 4 potential fates: transamination; conversion to glucose; formation of citrate; conversion to pyruvate
Slide 17-

Summary: Transamination takes off amine groups from amino acids and forms glutamate (ionized glutamic acid) Amine groups form ammonia when removed in deamination This combines with CO2 & Aspartate. Forms urea, Arginine, & Fumarate
Slide 18-

Alternative methods of nitrogen excretion Aquatic species excrete free ammonia through gills. Terrestrial critters produce Urea - very soluble - still needs water for removal via kidneys. Imposes a minimum daily water requirement. Spiders excrete guanine, 5 nitrogen atoms in a small molecule.
Slide 19-

Reptiles & birds excrete uric acid – very insoluble purine compound – forms supersaturated solutions. Concentrated urine, supersaturated with uric acid, goes from cloaca into hindgut – uric acid crystalizes & water is reabsorbed. In humans uric acid deposits crystals & causes gout.
Slide 20-

Processing Amino Acid Carbon Skeletons Transamination or Oxidative deamination both produce -keto acids Degradation of these carbon skeletons may take several different pathways: Amino acid C skeletons that degrade to form a Krebs cycle intermediate can then be used to make glucose via gluconeogenesis. These are called Glucogenic Amino Acids. Amino acid C skeletons that degrade to form acetyl CoA or Acetoacetyl CoA can form fatty acids or ketone bodies. These are called Ketogenic Amino Acids.
Slide 21-

F ates of C skeletons of 20 amino acids. Two are ketogenic: leucine & lysine. Nine are glucogenic. Nine are both because they form pyruvate or have two different degradation products.
Slide 22-

Amino Acid Biosynthesis Essential amino acids can be made by plants & bacteria in 7 to 10 steps. We obtain these amino acids by eating plants. 11 Non-essential amino acids synthesized in 1 to 3 steps. Use glycolysis intermediates: 3-phosphoglycerate & pyruvate Krebs cycle intermediates: Oxaloacetate & a-ketoglutarate
Slide 23-

Starting materials for biosynthesis of 11 nonessential amino acids: 1 step, 2 steps, or 3 steps Alanine, aspartate, & glutamate use transamination
Slide 24-

Phenylalanine & tyrosine degradation: Degradation of phenylalanine starts with conversion to tyrosine catalyzed by phenylalanine hydroxylase. Fumarate & acetoacetate are formed. Fumarate is converted to oxaloacetate for TCA cycle & acetoacetate is converted to acetyl CoA.
Slide 25-

Phenylketonuria (PKU): Defective phenylalanine hydroxylase – phenylalanine accumulates in body. Phenylalanine is transaminated to phenylpyruvate. Accumulation of phenylpyruvate leads to severe mental retardation in infants. Persons suffering from phenylketonuria should not consume foods containing high levels of phenylalanine, such as aspartame.
Slide 26-

Hemoglobin catabolism Red blood cells contain oxygen carrying pigments of a conjugated protein: Protein part is Globin Non-protein prosthetic group is Heme Heme contains four pyrrole (tetrapyrrole) groups held together by an iron atom Old red blood cells degraded in the spleen. Globin is hydrolyzed into amino acids. Iron atom stored in a protein (ferritin) Tetrapyrrole degraded to bile pigments
Slide 27-

Formation of Bile Pigments Heme Biliverdin Uses molecular O2, loses 1 C as CO which fuses to 1% of hemoglobin. Fe3+ grabbed by ferritin to make new hemoglobin Ring opens up
Slide 28-

Central methylene bridge of Biliverdin is reduced creating Bilirubin. Bilirubin found to be the major antioxidant in blood
Slide 29-

Bilirubin transported to liver. Becomes more water soluble with attachment of glucoronide sugars to propionate side chains. (Glucose + COO- group attached to 6th C) Solubilized bilirubin is excreted in Bile.
Slide 30-

Intestinal bacteria help change Bilirubin into Stercobilin and urobilin for excretion.
Slide 31-

Jaundice: when bilirubin accumulates in the blood. Spleen is degrading heme, but liver isn’t removing the products. Changing color of a bruise shows dominant degradation product of heme: either biliverdin or bilirubin
Slide 32-

Follow each pathway to its various products. All are highly inter-related.
Slide 33-

ATP production
Slide 34-

The human body’s response to feasting.
Slide 35-

The human body’s response to fasting Remember: the Brain uses Glucose or Ketone bodies for fuel.
Slide 36-

The human body’s response to starvation Everything is used to feed the brain Glucose or Ketone bodies.
Slide 37-

Review: can you… Describe the steps in Protein digestion & absorption Explain how Amino Acids are utilized in the body Explain Transamination and Oxidative De-amination Describe The Urea Cycle – purpose and steps Describe how a.a. Carbon Skeletons are processed Define and explain Amino Acid Biosynthesis. Describe the chemical composition of urine. Explain the relationship and importance of Arginine, Citrulline, and Nitric Oxide. Give a detailed description of Hemoglobin Catabolism Give an overview of the interrelationships among Carbohydrate, Lipid, and Protein Metabolic Pathways.