61043-86-5

Basic information

• Product Name: H-THR-SER-OH
• Synonyms: THR-SER;H-THR-SER-OH
• CAS NO: 61043-86-5
• Molecular Formula: C7H14N2O5
• Molecular Weight: 206.2
• Mol File: 61043-86-5.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: H-THR-SER-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-THR-SER-OH(61043-86-5)
• EPA Substance Registry System: H-THR-SER-OH(61043-86-5)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 61043-86-5(Hazardous Substances Data)

Usage

General Description

H-THR-SER-OH, also known as threonine-serine-alcohol, is a chemical compound that contains the amino acids threonine and serine, along with a hydroxyl group. Threonine and serine are both essential amino acids that are important for protein synthesis and various physiological processes in the body. Threonine is involved in the formation of collagen, elastin, and other proteins, as well as in the function of the nervous system and immune system. Serine is important for the synthesis of purines, pyrimidines, and other amino acids, and is also a precursor for the production of phospholipids, which are important for cell membrane structure. The presence of the hydroxyl group in H-THR-SER-OH indicates that it is in an alcohol form. Overall, H-THR-SER-OH plays a crucial role in various biological processes and is essential for overall health and wellbeing.

Relevant articles and documents

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.