Amino acid catabolism and urea cycle.pptx

HashimBashir1 43 views 20 slides May 04, 2024
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About This Presentation

Citric acid is a versatile organic acid found in many fruits, especially citrus fruits like lemons, oranges, limes, and grapefruits. Its chemical formula is C6H8O7, and it's classified as a weak acid. Citric acid has a wide range of applications, from food and beverage production to household cl...


Slide Content

Amino acid catabolism

In animals, amino acids undergo oxidative degradation in three different metabolic circumstances During the normal synthesis and degradation of cellular proteins, some are not needed for new protein synthesis. ingested amino acids exceed the body’s needs; amino acids cannot be stored During starvation or in uncontrolled diabetes mellitus: carbohydrates unavailable or not properly utilized

Under all these metabolic conditions, amino acids lose their amino groups to form α - keto acids provide three- and four-carbon units that can be converted by gluconeogenesis into glucose, the fuel for brain, skeletal muscle, and other tissues The α -keto acids undergo oxidation to CO 2 and H 2 O

Metabolic Fates of Amino Groups Amino acids derived from dietary protein are the source of most amino groups Most amino acids are metabolized in the liver Some of the ammonia generated in this process is recycled and used in a variety of biosynthetic pathways the excess is either excreted directly or converted to urea or uric acid for excretion Excess ammonia generated in other tissues travels to the liver (amino groups) for conversion to the excretory form.

Glutamate and glutamine act as a kind of general collection point for amino groups In the cytosol of hepatocytes, amino groups from most amino acids are transferred to α - ketoglutarate to form glutamate, which enters mitochondria to form NH 4 + ammonia generated in most other tissues is converted to the amide nitrogen of glutamine, which passes to the liver, then into liver mitochondria

In skeletal muscle, excess amino groups are generally transferred to pyruvate to form alanine, which transport amino groups to the liver.

Pyridoxal Phosphate Participates in the Transfer of α -Amino Groups to α - Ketoglutarate in liver, removal of the α -amino groups, promoted by enzymes called aminotransferases or transaminases. This is to collect the amino groups from many different amino acids in the form of L-glutamate The prosthetic group is pyridoxal phosphate (PLP), the coenzyme form of pyridoxine , or vitamin B6 Pyridoxal phosphate functions as an intermediate carrier of amino groups at the active site of minotransferases

Glutamate Releases Its Amino Group As Ammonia in the Liver In hepatocytes, glutamate is transported from the cytosol into mitochondria for oxidative deamination by L-glutamate dehydrogenase It is the only enzyme that can use either NAD + or NADP + The α - ketoglutarate formed from glutamate deamination can be used in the citric acid cycle and for glucose synthesis

Urea Cycle

Link b/w Urea Cycle and kreb cycle