38689-30-4

Basic information

• Product Name: H-D-LEU-D-LEU-OH
• Synonyms: D-LEU-D-LEU;D-LEUCYL-D-LEUCINE;H-D-LEU-D-LEU-OH;D-leu-d-leucrystalline;(R)-2-[[(R)-2-Amino-4-methylvaleryl]amino]-4-methylvaleric acid;D-Leu-D-Leu-OH;N-D-Leucyl-D-leucine;(R)-2-((R)-2-amino-4-methylpentanamido)-4-methylpentanoic acid
• CAS NO: 38689-30-4
• Molecular Formula: C₁₂H₂₄N₂O₃
• Molecular Weight: 244.33
• Mol File: 38689-30-4.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-D-LEU-D-LEU-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-LEU-D-LEU-OH(38689-30-4)
• EPA Substance Registry System: H-D-LEU-D-LEU-OH(38689-30-4)

Safety Data

• Hazardous Substances Data: 38689-30-4(Hazardous Substances Data)

Usage

General Description

H-D-LEU-D-LEU-OH, also known as N-(tert-butoxycarbonyl)-D-leucyl-D-leucine, is a chemical compound that belongs to the class of dipeptide analogs. H-D-LEU-D-LEU-OH is often used in biochemical research as a tool to study the structure and function of peptides and proteins. The presence of D-amino acids in this compound makes it resistant to enzymatic degradation, making it an attractive candidate for drug development. H-D-LEU-D-LEU-OH has been studied for its potential as an anticancer agent and as a treatment for neurodegenerative diseases. Its unique structure and properties make it a valuable tool for investigating peptide-based therapies and drug design.

Upstream product

• 21156-62-7 (R)-N-acetylphenylalanine methyl ester 
• 46741-65-5 D-leucine benzyl ester 
• 23032-21-5 D-leucine methyl ester 

Downstream Products

• 3303-31-9 L-leucyl-L-leucine 
• 17665-02-0 L-leucyl-D-leucine 
• 952-43-2 (3S,6S)-3,6-diisobutylpiperazine-2,5-dione 

Relevant articles and documents

Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp

From investigation of 2000 soil isolates, we identified two serine-type amidohydrolases that can hydrolyze d-aminoacyl derivatives from the culture supernatant of Streptomyces species 82F2 and 83D12. The enzymes, redesignated as 82F2-DAP and 83D12-DAP, were purified for homogeneity and characterized. Each enzyme had molecular mass of approximately 40 kDa, and each showed moderate stability with respect to temperature and pH. Among hydrolytic activities toward d-aminoacyl-pNAs, the enzymes showed strict specificity toward d-Phe-pNA, but showed broad specificity toward d-aminoacyl esters. The specific activity for d-Phe-pNA hydrolysis of 82F2-DAP was ten-fold higher than that of 83D12-DAP. As a second function, each enzyme showed peptide bond formation activity by its function of aminolysis reaction. Based on results of d-Phe-d-Phe synthesis under various conditions, we propose a reaction mechanism for d-Phe-d-Phe production. Furthermore, the enzymes exhibited peptide elongation activity, producing oligo homopeptide in a one-pot reaction. We cloned the genes encoding each enzyme, which revealed that the primary structure of each enzyme showed 30-60% identity with those of peptidases belonging to the clan SE, S12 peptidase family categorized as serine peptidase with d-stereospecificity.