18867-82-8

Basic information

• Product Name: L-Leucine, L-leucyl-L-leucyl-L-leucyl-
• CAS NO: 18867-82-8
• Molecular Formula: C24H46N4O5
• Molecular Weight: 470.653
• Mol File: 18867-82-8.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: L-Leucine, L-leucyl-L-leucyl-L-leucyl-(CAS DataBase Reference)
• NIST Chemistry Reference: L-Leucine, L-leucyl-L-leucyl-L-leucyl-(18867-82-8)
• EPA Substance Registry System: L-Leucine, L-leucyl-L-leucyl-L-leucyl-(18867-82-8)

Safety Data

• Hazardous Substances Data: 18867-82-8(Hazardous Substances Data)

Usage

General Description

L-Leucine is an essential amino acid that the body cannot produce on its own, so it must be obtained through dietary sources. It is an important building block for protein synthesis and muscle growth. L-leucyl-L-leucyl-L-leucyl- is a peptide derived from L-leucine and is often used in research as a tool to study protein structure and function, particularly in relation to enzyme regulation and inhibition. In combination with L-leucine, it may have potential applications in the field of pharmaceuticals and biomedical research.

Upstream product

• 61-90-5 L-leucine 

Relevant articles and documents

A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis

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.