Tyrosin | Introduction | History | Stucture.....

 Tyrosin | Introduction | History | Stucture.....

 Tyrosin Amino Acid

Introduction-

Tyrosin or 4-hydroxyphenylalanine is non-essential amino acid. It is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.

History-

It was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese.

 Properties :-

Chemical formula :- C₉H₁₁NO₃

Molar mass :- 181.191 g·mol−1

Solubility in water :- .0453 g/100 mL

Thermodynamic data :- Phase behaviour (solid–liquid–gas) 

Structure-

Sources-

Tyrosine, which can also be synthesized in the body from phenylalanine, is found in many high-protein food products such as chicken, turkey, fish, milk, cheese..etc

Biosynthesis-

In plants and most microorganisms, tyr is produced via prephenate, an intermediate on the shikimate pathway. Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and α-ketoglutarate.

Mammals synthesize tyrosine from the essential amino acid phenylalanine (phe), which is derived from food.

Industrial synthesis-

L-tyrosine and its derivatives are used in pharmaceuticals, dietary supplements, and food additives. Two methods were formerly used to manufacture L-tyrosine. The first involves the extraction of the desired amino acid from protein hydrolysates using a chemical approach. The second utilizes enzymatic synthesis from phenolics, pyruvate, and ammonia.

Function-

·     Proteinogenic amino acid.

·     Tyrosine has a special role by phenol functionality.

·    It occurs in proteins that are part of signal transduction processes and functions as a receiver of phosphate groups that are transferred by way of protein kinases.

·     Phosphorylation of the hydroxyl group can change the activity of the target protein, or may form part of a signaling cascade via SH2 domain binding.

·       A tyrosine residue also plays an important role in photosynthesis.

·    Chloroplasts it acts as an electron donor in the reduction of oxidized chlorophyll.

·       In this process, it loses the hydrogen atom of its phenolic OH-group.

·        This radical is subsequently reduced in the photosystem II by the four core manganese clusters.

 

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