14486-15-8 Usage
Uses
Used in Pharmaceutical Industry:
H-MET-MET-MET-OH is used as a potential therapeutic agent for its antioxidant properties, which can help neutralize free radicals and protect cells from oxidative damage. This makes it a candidate for the development of treatments targeting conditions associated with oxidative stress.
Used in Biochemical Research:
H-MET-MET-MET-OH is used as a research tool in biochemical studies to explore the effects of methionine-rich peptides on various biological processes, including protein synthesis and antioxidant mechanisms.
Used in Nutraceutical Industry:
H-MET-MET-MET-OH is used as a dietary supplement to support overall health and well-being by providing antioxidant benefits and potentially enhancing the body's natural defense mechanisms against oxidative stress.
Used in Cosmetics Industry:
H-MET-MET-MET-OH is used as an ingredient in cosmetic products for its potential antioxidant properties, which may help protect the skin from environmental damage and promote a healthier, more youthful appearance.
Used in Agricultural Industry:
H-MET-MET-MET-OH is used as a natural antioxidant in animal feed to improve the health and well-being of livestock by providing protection against oxidative stress and supporting overall health.
Check Digit Verification of cas no
The CAS Registry Mumber 14486-15-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,4,8 and 6 respectively; the second part has 2 digits, 1 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 14486-15:
(7*1)+(6*4)+(5*4)+(4*8)+(3*6)+(2*1)+(1*5)=108
108 % 10 = 8
So 14486-15-8 is a valid CAS Registry Number.
InChI:InChI=1/C15H29N3O4S3/c1-23-7-4-10(16)13(19)17-11(5-8-24-2)14(20)18-12(15(21)22)6-9-25-3/h10-12H,4-9,16H2,1-3H3,(H,17,19)(H,18,20)(H,21,22)/t10-,11-,12-/m0/s1
14486-15-8Relevant academic research and scientific papers
A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis
Kino, Kuniki,Arai, Toshinobu,Tateiwa, Daisuke
experimental part, p. 129 - 134 (2010/04/24)
L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligo-mers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.
