Why amino acid stereochemistry always L-configuration

In summary, there are many theories about why earthly amino-acids exist in the L-configuration and have not been found in D-configuration naturally. Some believe that the L configuration is the most stable, while others think that EM radiation is necessary for the D configuration to form. However, all of this is still speculation.
  • #1
Kglocc
44
0
Any known reasons, research, or theories about why earthly amino-acids exist in the L-configuration and have not been found in D-configuration naturally??
 
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  • #3
There are many theories. Who knows?

Try these tasty bits for some theories. You need to go to the library to see them, of course.

Nature 389 265 (1997)
Proc. Natl. Acad. Sci. USA 106(14) 5487 (2009)
Angew. Chem. Int. Ed. 38(23) 3418 (1999)
Chem. Rev. 98(7) 2391 (1998)
Mendeleev Commun. 13(3) 129 (2003)
Angew. Chem. Int. Ed. 41(24) 4618 (2002)
 
  • #4
Most naturally occurring amino acids are L amino acids. Proteins made from L-amino acids are called left-handed proteins. Homochirality of amino acids is important because it ensures uniformity of protein structure. In other words, proteins made of L-amino acids always fold the same way whereas proteins made from a mixture of L and D amino acids would not have the same structure. This is important for many reasons but the most important is probably recognition by enzymes.

I don't know if this is proved or just a theory
 
  • #5
Moogie said:
In other words, proteins made of L-amino acids always fold the same way whereas proteins made from a mixture of L and D amino acids would not have the same structure.

I think it depends on what you mean by "mixture of L and D amino acids". If you mean mixture in which amino acid is in the form of racemic mixture, and D and L forms are selected at random during peptide synthesis - you are probably right. If you mean mixture containing L and D amino acids, but each given amino acid has always the same conformation - you are probably wrong.

But that's just my guess.
 
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  • #6
Thanks brains, I appreciate the sources chemisttree.
I checked them all out. I had heard of the meteorite idea. But my gut was telling me that EM radiation must play a role, and now I have proper research to support.
 
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1. Why are amino acids in the L-configuration?

The L-configuration of amino acids is due to the way they are synthesized by living organisms. Amino acids are produced from their corresponding alpha-keto acids, and the enzymes responsible for this conversion only produce L-amino acids. This is a result of the specific active site of the enzyme that can only accommodate the L-form of the amino acid.

2. Can amino acids exist in other configurations?

Yes, amino acids can exist in both L- and D- configurations. D-amino acids are not commonly found in living organisms, but they can be synthesized in a laboratory. However, they are not used in protein synthesis and do not have the same biological functions as L-amino acids.

3. What is the significance of amino acid stereochemistry?

Amino acid stereochemistry is important because it determines the overall shape and structure of proteins. The L-configuration of amino acids allows for the formation of stable and functional proteins, which are essential for many biological processes in living organisms.

4. Are all amino acids in the L-configuration in proteins?

No, not all amino acids in proteins are in the L-configuration. Some amino acids, such as glycine, do not have a chiral center and therefore do not have a specific configuration. Additionally, some non-proteinogenic amino acids, such as D-amino acids, can be incorporated into proteins in small amounts, but they are not as common as L-amino acids.

5. Can amino acid stereochemistry affect the function of proteins?

Yes, amino acid stereochemistry can significantly impact the function of proteins. The specific arrangement of L-amino acids in a protein determines its overall shape, which is crucial for its function. A change in the stereochemistry of even a single amino acid can result in a misfolded protein with impaired function.

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