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INTRODUCTION The amino acids obtained from dietary source or body protein turnover are utilized for protein

biosynthesis and the production of a wide range of nitrogen-containing compounds(creatinine, amines, porphyrinetc) Amino acid metabolism The amino acids undergo certain common reaction like transamination followed by deamination for the liberation of ammonia. The amino group of amino acids is utilized for the formation of urea which is an excretory end product of protein metabolism. The carbonskeleton of amino acids is first converted to keto acids(by transamination) which meet one or more of the following fates. 1. Utilization to generate energy. 2. used for the synthesis of glucose. 3. Diverted for the formation of fat or ketone bodies. 4. Involved in the production of non-essential amino acids.

General and specific metabolic reaction of amino acids is described as follows: TRANSAMINATION The transfer of an amino(-NH2) group from an amino acid to a keto acid is known as transamination. This process involves theinterconversion of a pair of amino acids and a pair of keto acids, catalyzed by a group of enzymes called transaminases (recently amiontransferases) Mechanism of Transamination Transamination occurs in two stages 1. Transfer of the amino group to the coenzyme pyridoxal phosphate (bound to the coenzyme) to form pyridoxaminephosphate. 2. The Amino group of pyridoxamine phosphate is then transferred to a keto acid to produce a new amino acids and enzyme with PLP is regenerated. All the transaminases require pyridoxal phosphate (PLP) , a derivative of vitamin B6. The aldehyde group of PLP is linked with amino group of lysine residue, at the active site of the enzyme forming a Schiff base (imine linkage). When an amino acid comes in contract with the enzyme, it displaces lysine and a new Schiff base linkage is formed. The amino acidPLP-schiff base tightly binds with the enzyme by non-covalent forces. Snell and Braudtein proposed a Ping Pong Bi Bi mechanism involving a series of intermediate (aldimines and ketimines) in transamination reaction.

Fig. Mechanism of transamination


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DEAMINATION Deamination means the removal of amino group from amino acid in the form of ammonia with formation of keto acid. The liver and kidney are the main sites for deamination. Deamination may be oxidative or non-oxidative.

A. Oxidative deamination: It is catalyzed by one of the following enzymes: i. ii. iii. L-amino acid oxidases D-amino acid oxidases Glutamate dehydrogenase

B.Non-oxidative deamination: It is catalyzed by one of the following enzymes: i. ii. Dehydratases Desulfhydrases

A.OXIDATIVE DEAMINATION i. L-amino acid oxidases This enzyme is present in the liver and kidney. Its activity is low. It is an aerobic dehydrogenase that needs FMN as a coenzyme. It deaminates most of the naturally occurring L-amino acid.

ii. D- amino acid oxidases D-amino acids are present in plants and bacterial cell wall. They are not used in protein biosynthesis in humans and animals. D-amino acid oxidase is present in the liver. It is an aerobic dehydrogenase.

It needs FAD as a coenzyme

iii.Glutamate dehydrogenase This enzyme is present in most tissues. It is present both in cytoplasm and mitochondria. Its activity is high It needs NAD or NADP as acoenzyme. It deaminates glutamic acid resulting in ketoglutaric acid and ammonia.

B.NON-OXIDATIVE DEAMINATION i.Dehydratase This enzyme deaminates amino acids containing hydroxyl group e.g. serine, homoserine and threonine. It needs pyridoxal phosphate as coenzyme.

ii.Desulfhydrase This enzyme deaminatessulphurcontaiing amino acid e.g. cysteine and cystine. It needs pyridoxal phosphate as a coenzyme.

Most of the naturally occurring -amino acids are catabolized by transamination with ketoglutaric acid followed by deamination of the produced glutamic acid, a condition called transdeamination.

DECARBOXYLATION Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. The reverse process, which is the first chemical step in photosynthesis, is called carboxylation, the addition of CO2 to a compound. Enzymes that catalyze decarboxylations are called decarboxylases or, the more formal term, carboxy-lyases. The term "decarboxylation" literally means removal of the COOH (carboxyl group) and its replacement with a proton. The term simply relates the state of the reactant and product. Decarboxylation is one of the oldest organic reactions, since it often entails simple pyrolysis, and volatile products distill from the reactor. Heating is required because the reaction is less favorable at low temperatures. Yields are highly sensitive to conditions. In retrosynthesis, decarboxylation reactions can be considered the opposite of homologation reactions, in that the chain length becomes one carbon shorter. Metals, especially copper compounds, are usually required because such reactions proceed via the intermediacy of metal carboxylate complexes. Simple carboxylic acids rarely undergo decarboxylation. Carboxylic acids with a carbonyl group at the 3- (or b-) position readily undergo thermal decarboxylation, e.g. derivatives of malonic acid.

Some examples of decarboxylation reactions:

UREA CYCLE The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions occurring in many animals that produces urea ((NH2)2CO) from ammonia (NH3). This cycle was the first metabolic cycle discovered (Hans Krebs and Kurt Henseleit, 1932). In mammals, the urea cycle takes place primarily in the liver, and to a lesser extent in the kidney. Urea is the chief nitrogenous waste of mammals. Most of our nitrogenous waste comes from the breakdown of amino acids. This occurs by deamination. Deamination of amino acids results in the production of ammonia (NH3). Ammonia is an extremely toxic base and its accumulation in the body would quickly be fatal. Although our bodies cannot tolerate high concentrations of urea, it is much less poisonous than ammonia. Urea is removed efficiently by the kidneys. However, the liver contains a system of carrier molecules and enzymes which quickly converts the ammonia (and carbon dioxide) into urea. This is called the urea cycle. Functions: Organisms that cannot easily and quickly remove ammonia usually have to convert it to some other substance, like urea or uric acid, which are much less toxic. Insufficiency of the urea cycle occurs in some genetic disorders (inborn errors of metabolism), and in liver failure. The result of liver failure is accumulation of nitrogenous waste, mainly ammonia, which leads to hepatic encephalopathy. Reactions: Overview of intermediates and substrates in reaction: 1) L-ornithine 2) carbamoyl phosphate 3) L-citrulline 4) argininosuccinate 5) fumarate 6) L-arginine 7) urea i. L-Asp: L-aspartate ii. CPS-1: Carbamoyl Phosphate Synthetase I iii. OTC: Ornithine transcarbamoylase iv. ASS: Argininosuccinate Synthetase v. ASL: Argininosuccinate Lyase vi. ARG1: Arginase 1

Summary of reaction:

Consumes 2 molecules of ammonia. Consumes 1 molecule of carbon dioxide. Creates 1 molecule of urea ((NH2)2CO. Regenerates a molecule of ornithine for another turn.