Beta-alanine
From Wikipedia, the free encyclopedia
 |
|
|
Beta-alanine |
|
| Systematic (IUPAC) name | |
| 3-aminopropanoic acid | |
| Identifiers | |
| PubChem | 239 |
| Chemical data | |
| Formula | C3H7NO2 |
| Mol. weight | 89.093 |
| SMILES | C(CN)C(=O)O |
| Complete data | |
In biochemistry, beta-alanine is the only naturally occurring beta amino acid, which are amino acids in which the amino group is at the β-position from the carboxylate group (i.e., two atoms away, see Figure 1). The IUPAC name for β-alanine would be 3-aminopropionic acid. Unlike its normal counterpart, L-α-alanine, β-alanine has no chiral center.
β-alanine is not used in the biosynthesis of any major proteins or enzymes. It is formed in vivo by the degradation of dihydrouracil and carnosine. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (Vitamin B-5) which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid.
Even though much weaker than glycine(and thus with a debated role as a physiological transmitter), beta alanine is an agonist next in activity to the cognate ligant glycine itself, for strychnine-sensitive inhibitory glycine receptors (GlyRs) (the agonist order: glycine>>b-alanine>taurine>>lalanine, l-serine>proline).[1]
[edit] References
- ^ Encyclopedia of Life Sciences Amino Acid Neurotransmitters Jeremy M Henley, University of Bristol, Bristol, UK Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved. DOI: 10.1038/npg.els.0000010 Article Online Posting Date: April 19, 2001
[edit] External links
 |
This biochemistry article is a stub. You can help Wikipedia by expanding it. |
