17043-71-9

Usage

Uses

Used in Biochemical Research:
H-LYS-ALA-OH HYDROBROMIDE SALT is used as a research tool for studying protein synthesis, amino acid interactions, and metabolic pathways. Its unique properties allow for the investigation of biological processes and the development of new methodologies in the field of biochemistry.
Used in Pharmaceutical Development:
H-LYS-ALA-OH HYDROBROMIDE SALT is utilized as a building block in the synthesis of pharmaceutical compounds. Its versatility and stability make it a valuable component in the development of new drugs and therapeutic agents.
Used in Chemical Reactions:
H-LYS-ALA-OH HYDROBROMIDE SALT is employed as a reactant in various chemical processes. Its ability to participate in different types of reactions, such as condensation or substitution, makes it a useful compound in the synthesis of complex organic molecules and the production of specialty chemicals.

Upstream product

• 122242-30-2 N-(N²,N⁶-bis-benzyloxycarbonyl-L-lysyl)-L-alanine 
• 94149-28-7 Lys-Ala-AMC 
• 405-39-0 N,N'-di-[(phenylmethoxy)carbonyl]-L-lysine 
• 120335-48-0 N-(N²,N⁶-bis-benzyloxycarbonyl-L-lysyl)-L-alanine ethyl ester 
• 20314-31-2 (S)-2,6-Diamino-hexanoic acid [(S)-1-(naphthalen-2-ylcarbamoyl)-ethyl]-amide 

Relevant academic research and scientific papers

Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from porphyromonas gingivalis

Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is a major causative organism of chronic periodontitis. Because the bacterium utilizes amino acids as energy and carbon sources and incorporates them mainly as dipeptides, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. In a dpp4-7-11-disrupted P. gingivalis ATCC 33277, a DPP7-like activity still remained. PGN-0756 possessed an activity indistinguishable from that of the mutant, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with a molecular mass of 77,453, and existed as a dimer while migrating at 66 kDa on SDS-PAGE. It preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 μM and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of DPP- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also widely distributed in bacteria and archaea.