That Roses Are A Type Of Vascular Plant

Did You Know That Roses Are A Type Of Vascular Plant?

Whether you recognize it or not, Roses are a locality of vascular plant family. When spring is on its means and also the ground is soft, it’s the right time for planting roses. Roses are a really common bloom over the years, not solely do they appear smart, however they smell wonderful too.

However, planting roses can’t be done simply anywhere or in barely any climate. they have special care and treatment. Here are some tips that you simply have to be compelled to contemplate so as to successfully grow roses:

Roses need regarding four to six hours of daylight everyday. it’d be best to plant your roses during a clear space where there aren’t too several trees or different styles of plants. the rationale behind this is often that the rose could lack daylight exposure and also the roots also are doubtless to become intertwined with the rose and throttle its growth. If you would like to switch an previous rose bush, you must take away regarding one ½ cubic feet of the previous soil and replace it with new soil in order that the newly planted rose can have contemporary soil to begin with.

When puzzling over the position of your roses you want to contemplate the sort of rose you’re planting. Place ramblers and climbers along trellises, fences and next to pergolas or arches. this is often necessary to contemplate as a result of they have area to grow freely and these positions are excellent for larger blooming roses.

Roses can look smart in island beds which might be mixed with perennials. Smaller roses create nice edging plants, that are excellent for combining in front of taller species. Dig a hole massive enough for the scale of the foundation ball, however keep in mind to loosen the soil within the bottom of the outlet. you’ll additionally add bone meal that acts as a slow acting resource of phosphorus. this may facilitate establish a healthy root growth for your roses, that is important for healthy vascular plant growth.

You should use caution when considering the planting depth as this relies on your climate. If you reside during a cooler climate, plant roses deeper, however if you would like to plant during a pot, you want to dig regarding one in. deeper than the standard potted level. Adding non vascular plants as ground cowl will add beauty to your rose garden simply.

Make sure that you simply place roses within the hole fastidiously. the outlet ought to be refilled with soil in order that the roots are lined utterly. Before you create the ultimate covering, water the rose. Then mound the soil regarding eight inches high round the base of the plant. the planet can keep the stems from drying out till the plant is totally rooted. because the leaves open, you’ll take away the surplus soil that surrounds the plant.

These some necessary tips you wish to contemplate when planting roses. it’ll be well worth the effort, as your roses can bloom fantastically.

Chromosomes Function

Chromosomes are the most important parts of the body that determine the shape, structure and character of a person. The chromosomes are made of DNA particles and protein material. There are totally 23 pairs of chromosomes in the human body responsible for various activities in the body. The last pair of chromosomes is sex chromosomes and is responsible for the determination of the gender of the baby which is the one of the primary chromosomes function. In males, the sex chromosomes are made of X and Y chromosomes and in the females both the chromosomes are X. When the X chromosome joins with the X chromosome in the female, a baby girl is born and when a Y chromosome from the male joins with the X chromosome in the female, this result in the birth of the baby boy.

Chromosomes Function
The human body is the most complex system to study and the chromosomes function are further complex. Researchers state that chromosomes are responsible to control all the activities in the human body. Chromosomes divide the cells and contain DNA and proteins. The proteins are most essential for the growth of muscles and tissues in the human body. One of the chromosomes function is protein synthesis and these chromosomes are essential to pass the genes in to the generations as a means of heredity. The structure of the DNA is in a double helix structure containing a lot of genes each resembling the characteristic feature of the entire generation of a particular heredity. This is the reason for the children to inherit the characters of the parents and the grand parents to a certain extent.

The DNA test is being conducted to identify the generation of the off spring and in a lot of police cases these type of DNA test are done. The primary chromosomes function is cell division which is essential for the reproduction, repair and smooth functioning of the body. These particles are present in all living beings in the planet and the cell division is a normal function that occurs in all living species. There are a lot of genetic disorders and syndromes that occur as a result of the improper pairing of the chromosomes. The gene mutations occur in some cases due to the alteration in the sequence of the genes of the chromosomes. Genetic engineering is a field that specializes in the treatment of the genetic disorders.

Cytoplasm Function

Cytoplasm – a mandatory part of the cells attached between the plasma membrane and the nucleus, divided into hyaloplasm (the main substance of the cytoplasm), organelles (the permanent component of the cytoplasm) and inclusion (the time components of the cytoplasm).

Cytoplasm Function
The chemical composition of the cytoplasm: the base is water (60-90% of the total mass of the cytoplasm), various organic and inorganic compounds. The cytoplasm is alkaline. A characteristic feature of the cytoplasm of eukaryotic cells is a constant movement (cycloids). It is found primarily on the movement of organelles cells, such as chloroplasts. If the motion stops the cytoplasm, the cell dies, because only by being in constant motion, it can perform all the functions – cytoplasm function.

Hyaloplasm (cytosol) is a colorless, slimy, thick and transparent colloidal solution. It is in this flow all the metabolic processes; it provides a link for the nucleus and all organelles. Depending on the predominance of hyaloplasm liquid part, or large molecules they distinguish two forms of hyaloplasm: sol – a more liquid and gel hyaloplasm – thicker hyaloplasm. Between them is possible inter transitions: gel turns into a sol and vice versa.

Cytoplasm function:

the union of all components of the cell into a single system
environment for the passage of many biochemical and physiological processes
environment for the existence and functioning of organelles.
Cell walls

Cell walls restrict eukaryotic cells. In each cell membrane can provide at least two layers. The inner layer is adjacent to the cytoplasm and presented to the plasma membrane (synonyms – plasma membrane, the cell membrane, cytoplasmic membrane), on which is formed by the outer layer. In animal cells it is thin and is called the glycocalyx (formed glycoproteins, glycolipids, lipoproteins) in the plant cell – a thick, called the cell wall (forming cellulose).

Structure of membranes

All biological membranes have a common structural characteristics and properties. Currently, generally accepted liquid-mosaic model of the membrane. The basis of the membrane lipid bilayer is formed mainly phospholipids. Phospholipids – triglycerides, in which one fatty acid residue is substituted for the remainder of phosphoric acid portion of the molecule, which is the residue of phosphoric acid, called the hydrophilic head regions, which are the remains of fatty acids – hydrophobic tails. In the membrane phospholipids are located in a very orderly: the hydrophobic tails of the molecules facing each other, and the hydrophilic heads – out to the water.

Here I am going to discuss about cytoplasm function. We all know that the body of a living creature consists of numerous and countless cells. The cell is the basic building block of the body of an animal or a plant. Each of these cells carries out numerous functions which are essential to keep us alive. Each of these cells consists upon a number of cell components and cytoplasm is one of them.

Cytoplasm is one of the very important components of a cell but before getting into the issue of cytoplasm function, it is important to have a basic knowledge on cells. The structure of the cell is an important issue as it is a crucial factor for carrying out cell operations. Each off these cells is separated from each other through a membrane called cell membrane. Cells can be categorized into tow basic categories depending upon the presence of nucleus and some other organelles. These tow categories of cell are, eukaryotic and prokaryotic. Prokaryotic cells don’t have nucleus and they are usually present in plant body where as a eukaryotic cell contains nucleus along with other cell structure components and they are usually found in animal body.

Anyway, we have spoken a lot about cells and it is time to enter into the issue of the cytoplasm. Cytoplasm is present in between the nucleus and the cell membrane, that is, it fills the gap between the cell membrane and nucleus. The liquid substance of the cytoplasm is called cytosol and another component is termed as hyaloplasm. The 80% off component of cytosol is water. The next paragraph describes the roll of cytoplasm behind cell activities.

However the structure of plant cells and that of animal cells are quite different but the role of cytoplasm is same in both cases. The main function of cytoplasm is to provide security to internal layer. The fluid acts as a shock absorber for the internal layers of the cell. The next high priority role of cytoplasm is, it preserves essential chemical substances which may be required by our body in future and acts as a medium for various essential metabolic reactions. It also allows anaerobic glycolisys and protine synthesis for our body. Cytosol helps to dissolves essential enzyme which are required to decompose various compound element into simple elements and to elevate the metabolism process. It also provides a means for exchange of various chemical substances and other essential materials in between cells which are required to keep all cells working properly.

Fatty acid oxidation

Beta oxidation is the major pathway for catabolism of fatty acids in mitochondria of cell, in which two carbons are successively removed from the carboxyl end of fatty acyl CoA producing acetyl CoA, NADH, and FADH2. The fatty acid is broken between alpha(2) and beta(2) carbon atoms – hence the name beta oxidation. It is an aerobic process requiring oxygen. Fatty acid oxidation generates large quentities of ATP.

Steps of beta oxidation of fatty acids:

Steps of beta oxidation of fatty acids

Steps of beta oxidation of fatty acids

At first, fatty acid must be converted into an active intermediate (aceyl CoA) in the cytoplasm of cell before they can be catabolized. In the presence of ATP, aceyl CoA synthetase enzyme catalyzes the conversion of fatty acid into aceyl CoA (active fatty acid). Active short chain and medium chain fatty acids (containing less than 12 carbon atoms) can enter from cytoplasm into mitochondria without difficulty, but long chain fatty acid must be bound to carnitine to penetrate the inner mitochondrial membrane and gain access to mitochondria for beta oxidation.

The first cycle of beta oxidation consists of a sequence of four reactions, which result in shortening the fatty acid chain by two carbons (for saturated fatty acid with even number of carbon atoms) or three carbons residue (for saturated fatty acid with an odd number of carbon atoms). The reactions include an oxidation that yields FADH2, a hydration reaction, a second oxidation reaction that yields NADH, and a thiolytic reaction that produces a molecule of acetyl CoA. These four reactions occur repeatately. Each cycle of reactions producing one acetyl CoA, one NADH, and one FADH2.

Energy generation from beta oxidation of fatty acids:

Energy generation from beta oxidation of fatty acids depend on the number of carbon atoms present in fatty acid. Fatty acids containing more carbon atoms generate more energy. For example, caproic acid is a 6 carbon atoms fatty acid, catabolism of one mol of caproic acid ultimately generates 44 mol of ATP.

Fatty acid oxidation disorder:

Fatty acid oxidation disorder can be produced by carnitine deficiency or genetic defects in enzymes involved in the transfer of long chain fatty acid into the mitochondria. This disorder causes cardiomyopathy and hypoketonemic hypoglycemia with coma.

Fatty acid

Fatty acid is an aliphatic carboxylic acid made up of a hydrocarbon chain with a terminal carboxyl group. Fatty acids are usually derived from fats (triglycerides). Fatty acids are important sources of fuel in the body because, when metabolized, they generate large amounts of energy. Heart muscle prefers mostly fatty acids as a source of energy. When fatty acids are not attached to other molecules, they are called free fatty acids. They leave the cell to be transported for use in another part of the body.

On the basis of saturation, fatty acids may be divided into two types –

Saturated fatty acids: Fatty acids that contain single bond in their carbon chain are called saturated fatty acids. Saturated fatty acids are harmful for our health because, they increase our serum total cholesterol and LDL cholesterol level, and increased risk of coronary heart disease.They include acetic acid, palmitic acid, butyric acid, lauric acid, capric acid, formic acid, myristic acid, and stearic acid. The main sources of saturated fatty acids are meat and dairy products, and some vegetable oils including coconut oil and palm oil. Most experts strongly advise limiting consumption of saturated fatty acids.

Unsaturated fatty acids: Fatty acids that contain one or more double bonds in their carbon chain are called unsaturated fatty acids.

Monounsaturated fatty acids: They contain one double bond. Dietary monounsaturated fatty acids are beneficial for our health because, they reduce our serum total cholesterol and LDL cholesterol, and increase HDL cholesterol, which protect against coronary heart disease. They include oleic acid, palmitoleic acid, and elaidic acid. Monounsaturated fatty acids are usually derived from vegetables and fish.

Polyunsaturated fatty acids: They contain two or more double bonds.

Polyunsaturated fatty acid Family            Source
Linoleic acid Omega-6 Corn, soyabean, peanut, and cootonseed
Alpha linolenic acid Omega-3 Linseed oil
Arachidonic acid Omega-6 Animal fat
Timnodonic acid Omega-3 Cod liver oil, mackerel oil, menhaden oil, and salmon oil
Cervonic acid Omega-3 Fish oil

Omega-6 fatty acids: The first double bond of these fatty acids begin at the sixth carbon atom. Omega-6 polyunsaturated fatty acids decrease our serum total cholesterol and LDL cholesterol, but also decrease HDL cholesterol that protect against coronary heart disease.

Omega-3 fatty acids: The first double bond of these fatty acids begin at the third carbon atom. Dietary omega-3 polyunsaturated fatty acids reduce serum triglyceride level, reduce the tendency to thrombosis by inhibiting thromboxane A2 synhesis, suppress cardiac arrhythmias, and substantially decrease the risk of cardiovascular mortality, but they have minor effect on LDL cholesterol or HDL cholesterol level.

Essential fatty acids:

Two fatty acids linoleic acid and linolenic acid are called essential fatty acids because of these fatty acids cannot be synthesized by the body and must be supplied in the diet. Linoleic acid is the precursor of arachidonic acid which is the substrate for eicosanoids synthesis. If linoleic acid is deficient in the food, arachidonic acid becomes essential. Essential fatty acids are required for fluidity of biological membrane structure and formation of eicosanoids. Essential fatty acids deficiency leads to development of scaly dermatitis, poor wound healing, hair loss, decreased vision and altered learning behaviors.

Trans fatty acids: Trans fatty acids are chemically classified as unsaturated fatty acids, but they behave more like saturated fatty acids in the body. Trans fatty acids do not found in plants, only found in small amounts in animal fats. However, trans fatty acids are produced during the hydrogenation of vegetable oils, for example, during the manufacture of margarine. Trans fatty acids rise serum LDL cholesterol and increase the rish of coronary heart disease.

Short chain fatty acids: containing 4 – 10 carbon atoms, for example, acetic acid is a short chain fatty that contain 2 carbon atoms. For oxidation of short chain fatty acids, they can enter into mitochondria without difficulty.

Long chain fatty acids: containing 11 – 24 carbon atoms, for example, stearic acid is a long chain fatty acid that contain 18 number of carbon atoms. For oxidation of long chain fatty acids, they must be bound to carnitine to penetrate the inner mitochondrial membrane and gain access to mitochondria.

Lipid Metabolism

Lipids constitute about 15-20% of the body weight. Lipids are a major source of energy for our body. Lipid metabolism is concerned mainly with the fatty acid and cholesterol. The main source of fatty acids is dietary lipids.

In the first phase of fatty acid metabolism, fatty acids are oxidized to acetyl CoA by the process of β-oxidation or esterified with glycerol, forming triglyceride, stored in the adipose tissue, serve as the body’s principal fuel reserve.

In the second phase of fatty acid metabolism, acetyl CoA synthesized by the process of β-oxidation may undergo the following fates;

(1)        Acetyl CoA is oxidized to carbon dioxide via the citric acid cycle and produces large amount of energy.

(2)        It is the precursor for the synthesis of cholesterol and other steroids.

(3)        Acetyl CoA is used to synthesis the ketone bodies in the liver that are important fuels in prolonged fasting state.

As a whole, lipid metabolism can be divided into two categories:

A) Catabolic pathway of lipid metabolism:

  • Beta-oxidation of fatty acid – Fatty acids are oxidized to acetyl CoA by the process of β-oxidation.
  • Hydrolysis of triglyceride – Triglyceride is hydrolysis into glycerol and free fatty acid.

A) Anabolic pathway of lipid metabolism:

  • Lipogenesis (Synthesis of fatty acid) – fatty acids may be synthesized from acetyl CoA derived from glucose or amino acids metabolism by the process of lipogenesis.
  • Ketogenesis (Formation of ketone bodies) – Acetyl CoA arise from β-oxidation of fatty acid is used to synthesis of ketone bodies in the liver by the process of ketogenesis.
  • Cholesterol synthesis – Cholesterol is synthesized from acetyl CoA arises from β-oxidation of fatty acid.
  • Triglyceride synthesis – Triglyceride is synthesized by the esterificaton of free fatty acids with glycerol, which is stored in the adipose tissue.
  • Steroid synthesis – Steroid is synthesized from acetyl CoA arises from β-oxidation of fatty acid.

Urea cycle

Urea is the principal disposal form of amino groups of amino acids, and about 90% of nitrogen containing compounds of urine. At first, the amino groups of amino acids are converted into glutamate by the process of transamination reaction.Then, glutamate can enter into oxidative deamination reaction, and provide ammonia. Finally, most of the toxic ammonia is converted to urea by the process of urea cycle, and excreted through the urine.

Reactions of urea cycle:

The first two reactions of cycle occur in mitochondria, whereas the remaining reactions occur in cytoplasm of cells.

(1) Synthesis of carbamoyl phosphate: Carbamoyl phosphate is formed from ammonia by the action of mitochondrial carbamoyl phosphate synthetase I. This rate limiting enzyme of urea cycle is active only in the presence of N-acetylglutamate. Two molecules of ATP are required to form carbamoyl phosphate.

(2) Formation of citrulline: The carbamoyl group of carbamoyl phosphate is transferred to ornithine, forming citrulline, catalyzed by ornithine transcarbamoylase.

(3) Formation of argininosuccinate: Argininosuccinate synthase links citrulline and aspartate via amino group of aspartate, and form argininosuccinate. The amino group of aspartate provides second nitrogen of urea. This reaction requires ATP.

Reactions of urea cycle

Reactions of urea cycle

(4) Cleavage of argininosuccinate: Argininosuccinase cleaves the argininosuccinate to arginine and fumarate. Arginine serves as the immediate precursor of urea. Fumarate is hydrated to malate, and subsequent oxidation of malate forms oxaloacetate. This oxaloacetate re-forms aspartate by the process of transamination.

(5) Cleavage of arginine releases urea: Hydrolytic cleavage of arginine, catalyzed by liver arginase, relases urea and ornithine. This reaction occurs almost exclusively in yhe liver. Ornithine, reenters liver for additional rounds of urea synthesis.

(6) Disposal of urea: From liver, urea is transported in blood to kidney, where it is filtered and excreted through the urine. A small portion of urea diffuses from blood into the intestine, and is converted to carbon dioxide (CO2) and ammonia (NH3) by bacterial urease. This NH3 is partly excreted in the feces, and is partly reabsorbed into blood.

Urea cycle regulation:

The rate limiting enzyme of urea cycle is carbamoyl phosphate synthetase I, which is active only in the presence of N-acetylglutamate. N-acetylglutamate is produced from glutamate and acetyl CoA, in a reaction for which arginine is activator. Therefore, glutamate (substrate of N-acetylglutamate) and arginine (activator of N-acetylglutamate production) are increased after intake of protein rich diet, which ultimately increased the intrahepatic concentration of N-acetylglutamate. This leads to increased rate of urea production.

Urea cycle disorder:

Urea cycle disorder is comparatively rare, but medically devastating. This disorder is associated with genetic defects in each enzyme of urea cycle, of N-acetylglutamate synthetase, and of the membrane associated ornithine transporter. All defects of urea cycle lead to ammonia intoxication. Common clinical symptoms of urea cycle disorders include vomiting, irritability, lethargy, intermittent ataxia, and mental retardation. In persons with urea cycle disorder, high protein foods should be avoided, and a frequent small low protein meals should be intake to avoid sudden rises in blood ammonia levels.

Transamination

Transamination is the conversion of one amino acid to corresponding keto acid with simultaneous conversion of another keto acid to an amino acid. In short, it is the interconversion between a pair of amino acid and a pair of ketoacid.

All amino acids except lysine, proline, hydroxyproline, and, threonine participate in transamination. Reaction of transamination is reversible and catalyzed by enzyme aminotransferases. These enzymes are found in the cytoplasm of cells throughout the body, especially in liver, kidney, muscle, and intestine. All aminotransferases require coenzyme pyridoxal phosphate (a derivative of vitamin B6) for transamination reaction.

Transamination is the first step of amino acids catabolism in which the α-amino group of amino acid is transfer to α-ketoglutarate, and form an α-keto acid and glutamate. Glutamate can be oxidatively deaminated, or used as an amino group donor in the formation of nonessential amino acids

The two most important transamination reactions are catalyzed by alanine  aminotransferase (ALT) and aspartate  aminotransferase(AST).

Alanine aminotransferase enzyme, formerly called serum glutamate pyruvate transaminase (SGPT) calalyzes the transfer of amino group of alanine to α-ketoglutarate, and form pyruvate and glutamate.

Aspartate aminotransferase enzyme, formerly called serum glutamate oxaloacetate transaminase (SGOT) calalyzes the transfer of amino group of aspartate to α-ketoglutarate, and form oxaloacetate and glutamate.

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Amino acids

Amino acids are the monomer of protein containing both amino group and carboxyl group.

Structure of amino acids:

Each amino acid has an α-amino group (- NH3+), an α-carboxyl group (- COOH), and a distinctive side chain (R- group) attached to the α-carbon atom.

Types of amino acids:

20 amino acids are necessary for human body. Of these, some can be produced by the liver – called non essential amino acids; the rest must be supplied by food – called essential amino acids.

According to nutritional value, amino acids may be classified as:

Essential amino acids – Amino acids that cannot be produced by the body but essential for growth and development of body. These amino acids must be obtained from diet. Protein containing diet including milk, egg, meat, and cheese contain all essential amino acids but grains and vegetables do not contain all the essential amino acids.

Non essential amino acids – These amino acids that can be produced by the body.

List of 20 Amino acids:

8 are essential amino acids 12 are non essential amino acids
Isoleucine Alanine
Tryptophan Asparagine
Phenylalanine Aspartate
Methionine Cysteine
Threonine Glutamate
Lysine Glycine
Leucine Proline
Valine Glutamine
Serine
Tyrosine
Arginine *
Histidine*

*Argnine and histidine are essential under specific condition.

According to the nature of their catabolic end products,  amino acids may be classified as:

Glucogenic amino acids – Amino acids whose catabolism generates pyruvate or one of the intermediates of citric acid cycle are called glucogenic or glycogenic amino acids. These intermediates can give rise to formation of glucose or glycogen in liver and glycogen in skeletal muscle by the process of gluconeogenesis.

Ketogenic amino acids – Amino acids whose catabolism generates either acetoacetate or one of its precursor (acetyl CoA or acetoacetyl CoA) are called ketogenic amino acids. Acetoacetate is one of the ketone bodies.

List of ketogenic and glucogenic amino acids:

Ketogenic Glucogenic and ketogenic  Glucogenic
Lysine Tyrosine Alanine
Leucine Isoleucine Asparagine
Tryptophan Aspartate
Phenylalanine Cysteine
Glutamate
Glutamine
Glycine
Proline
Serine
Methionine
Threonine
Arginine
Histidine
Valine

Branched chain amino acids:

The essential amino acids valine, isoleucine, and leucine are called branched chain amino acids. Branched chain amino acid refers to their chemical structure. Therapeutically, these amino acids are valuable because they pass through the liver in unchanged form and are available for cellular uptake from circulation, preferentially metabolized in muscle. Parenteral administration of branched chain amino acids is beneficial whenever catabolism due to physiological stress occurs. The skeletal muscle can be used these amino acids for energy.

Amino acids benefits:

  • Amino acids act as the building blocks of our body proteins.
  • Some amino acids participate in transmission of impulse in the nervous system.
  • These are the precuesors of hormone, purines, pyrimidines, and some vitamins like pantothenic acid ( vitamin B3) and folic acid.
  • Essential amino acids support infant growth and maintain health in adult.

Protein Metabolism

Dietary proteins are digested in the intestine and produced their constituent amino acids that are absorbed into the blood stream. Amino acids are also obtained in the blood stream from normal body protein degradation or from de novo synthesis.

Amino acids are safely locked by the α-amino group. Removal of α-amino group is essential for generating energy from amino acids, and it is an obligatory step in amino acid metabolism.

The first stage of amino acid metabolism involves the removal of the α-amino group from amino acids by transamination and subsequent deamination forming ammonia and corresponding α-ketoacid. A small portion of ammonia is excreted through the urine, but large portion is used in the formation of urea that is the most important route for removing of nitrogen from the body.

In second stage of amino acid metabolism, the α-ketoacids also called carbon skeletons of amino acids are converted into common intermediate products. These intermediate products can (1) be metabolized to carbon dioxide and water with generation of energy via citric acid cycle; (2) be used to form glucose via gluconeogenesis; or (3) synthesize ketone bodies.

Overall, protein metabolism can be divided into two categories:

A) Catabolic pathway of protein metabolism:

  • Catabolism of body protein to amino acids – our body proteins are converted to amino acids via a series of catabolic reactions.
  • Transamination and Deamination – α-amino group is removed from the amino acids by transamination and deamination, forming ammonia and corresponding α-ketoacid.
  • Catabolism of carbon skeleton of amino acid – Carbon skeleton of amino acid is catabolised into seven common intermediate products such as pyruvate, fumarate, oxaloacetate, α-ketoglutarate, acetyl CoA, acetoacetyl CoA and succinyl CoA.

B) Anabolic pathway of protein metabolism:

  • Protein synthesis – Protein is synthesized from the amino acids through a series of anabolic reactions.
  • Biosynthesis of non-essential amino acids – Non-essential amino acids are formed from the intermediates of metabolism or, from the carbon skeletons of essential amino acids.
  • Urea cycle – Most of the toxic ammonia synthesized from the deamination of amino acids in the liver are converted into non-toxic urea by the process of urea cycle. From the liver urea is transported to kidney for disposal.