3695-80-5

Usage

Uses

Used in Pharmaceutical Industry:
H-ALA-D-ALA-OH is used as a key component in the synthesis of antibiotics for its ability to inhibit the enzyme transpeptidase, which is crucial for the cross-linking of peptidoglycan strands in bacterial cell walls. This disruption of cell wall formation ultimately leads to bacterial cell lysis and death, making H-ALA-D-ALA-OH an important chemical in the development of antibiotic drugs targeting bacterial infections.
Used in Antibacterial Applications:
H-ALA-D-ALA-OH is employed as an antibacterial agent, particularly in the development of drugs that target bacterial infections. Its ability to inhibit the enzyme transpeptidase, which is essential for the cross-linking of peptidoglycan strands in bacterial cell walls, results in the disruption of cell wall formation and leads to bacterial cell lysis and death. This makes H-ALA-D-ALA-OH a valuable chemical in the creation of effective antibiotic treatments against various bacterial infections.

InChI:InChI=1/C6H12N2O3/c1-3(7)5(9)8-4(2)6(10)11/h3-4H,7H2,1-2H3,(H,8,9)(H,10,11)/t3?,4-/m1/s1

Upstream product

• 128982-78-5 DL-2-(2-hydroxyimino-propionylamino)-propionic acid 
• 31654-38-3 N-(2-bromo-propionyl)-alanine 
• 5625-46-7 cyclo(-DL-Ala-DL-Ala-) 
• 2392-63-4 N-pyruvoyl-alanine 
• 7732-18-5 water 
• 2835-06-5 phenylglycin 
• 7664-41-7 ammonia 
• 19245-95-5 N-[(benzyloxy)carbonyl]-L-alanyl-D-alanine 
• 64532-72-5 Z-L-Ala-D-Ala-OEt 
• 132343-11-4 Cbz-L-ala-D-ala-Cbz 
• 56-41-7 L-alanin 
• 98337-25-8 (S,S)-N,N'-bis(1-carboxyethyl)urea 
• 64-17-5 ethanol 
• 338-69-2 D-Alanine 

Downstream Products

• 5625-46-7 cyclo(-DL-Ala-DL-Ala-) 
• 2392-63-4 N-pyruvoyl-alanine 
• 22221-70-1 Cbz-HN-Ala-Ala 
• 106659-81-8 2-[2-(2-Cyano-ethylamino)-propionylamino]-propionic acid 
• 338-69-2 D-Alanine 
• 56672-76-5 1-hippuroyl-L-proline 
• 56-41-7 L-alanin 

Relevant academic research and scientific papers

The peptide formation mediated by cyanate revisited. N-carboxyanhydrides as accessible intermediates in the decomposition of N-carbamoylamino acids

Similar to many ureas, N-carbamoylamino acids were shown to be hydrolyzed in aqueous solution through elimination mechanisms at close to neutral pH, the nucleophilic attack of water being a minor process. Two competing elimination mechanisms can take place involving either cyanate or isocyanate transient intermediates. Peptide formation was observed and attributed to the latter pathway through the intermediacy of amino acid N-carboxyanhydride (NCA). Eventually, cyanate and its precursors (including urea) unexpectedly behave as amino acid activating agents because of their ability in amino acid carbamoylation. Owing to its ability to generate a background prebiotic production of NCAs on the primitive Earth, this reaction is suggested to have contributed to the origin of life process. Copyright

Small peptides as modular catalysts for the direct asymmetric aldol reaction: Ancient peptides with aldolase enzyme activity

Simple peptides and their analogues having a primary amino group as the catalytic residue mediate the direct asymmetric intermolecular aldol reaction with high stereoselectivity and furnish the corresponding aldol products with up to 99% ee; this intrinsic ability of highly modular peptides may explain the initial molecular evolution of aldolase enzymes. The Royal Society of Chemistry 2005.