L-Proline

L-Proline is an amino acid that is used in the biosynthesis of protein. It is non-essential in humans, meaning the body can synthesize it from glutamic acid. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG).

Structure

L-Proline is unique among the 20 protein-forming amino acids because the amino group is secondary. The distinctive cyclic structure of proline's side chain locks its phi angle at approximately -75°, giving proline an exceptional conformational rigidity compared to other amino acids. Hence, proline loses less conformational entropy upon folding, which may account for its higher prevalence in the secondary structural elements of proteins.

Biosynthesis

In humans, L-Proline is synthesized from glutamate. This reaction is catalyzed by the enzyme glutamate 5-kinase at the expense of ATP. The subsequent steps are catalyzed by glutamate-5-semialdehyde dehydrogenase and pyrroline-5-carboxylate reductase.

Function

L-Proline plays important roles in the body. It is essential for the synthesis of collagen, the most abundant protein in mammals, used in the formation of skin, connective tissue, and bone. It is also involved in the maintenance of muscle tissue, wound healing, and the body's immune response.

Dietary sources

L-Proline is found in meat, dairy products, and eggs. It can also be synthesized by the body from other amino acids, so it is not essential in the diet.

See also

• Amino acid
• Protein biosynthesis
• Collagen

L-Proline Resources
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