19764-30-8

Basic information

• Product Name: N-Acetyl-D-leucine
• Synonyms: 2-Acetylamino-4-methylvaleric acid;N-Acetyl-2-isobutylglycine;D-2-Acetylamino-4-methylvaleric acid;2,N-Acetyl-D-leucine;(R)-2-acetaMido-4-Methylpentanoic acid;D-Leucine, N-acetyl-;N-Ac-D-Leu-OH;(R)-Ac-2-amino-4-methylpentanoic acid
• CAS NO: 19764-30-8
• Molecular Formula: C₈H₁₅NO₃
• Molecular Weight: 173.21
• EINECS: 1533716-785-6
• Product Categories: Amino Acids;Modified Amino Acids;amino acid;Amino ACIDS SERIES;chiral;Amino Acids;Leucine [Leu, L];Ac-Amino Acids;Amino Acids (N-Protected);Biochemistry;N-Acetyl-Amino acid series;A - H
• Mol File: 19764-30-8.mol
• Article Data: 11

Chemical Properties

• Melting Point: 176-177C
• Boiling Point: 369.7 °C at 760 mmHg
• Flash Point: 177.4 °C
• Appearance: /
• Density: 1.069 g/cm³
• Refractive Index: 23 ° (C=4, EtOH)
• Storage Temp.: −20°C
• Solubility: DMSO (Slightly), Ethanol (Slightly, Sonicated), Methanol (Slightly)
• PKA: 3.67±0.10(Predicted)
• CAS DataBase Reference: N-Acetyl-D-leucine(CAS DataBase Reference)
• NIST Chemistry Reference: N-Acetyl-D-leucine(19764-30-8)
• EPA Substance Registry System: N-Acetyl-D-leucine(19764-30-8)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36
• WGK Germany: 3
• Hazardous Substances Data: 19764-30-8(Hazardous Substances Data)

Usage

Chemical Properties

White to off-white powder

Upstream product

• 57289-25-5 methyl N-acetyl-leucinate 
• 99-15-0 N-acetylleucine 
• 915008-30-9 2-acetylamino-4-methyl-pent-2-enoic acid 
• 64896-30-6 (Z)-2-Acetylamino-4-methyl-pent-2-enoic acid 
• 328-38-1 (R)-leucine 
• 830-03-5 4-nitrophenol acetate 
• 2256-97-5 N-acetyl-DL-isoleucine butyl ester 
• 60-35-5 acetamide 
• 201230-82-2 carbon monoxide 
• 590-86-3 isovaleraldehyde 

Downstream Products

• 328-38-1 (R)-leucine 
• 187345-48-8 (R)-2-Acetylamino-4-methyl-pentanoic acid ((R)-3-benzyl-1-benzyloxy-2,5-dioxo-pyrrolidin-3-yl)-amide 
• 221685-11-6 (R)-2-Acetylamino-4-methyl-pentanoic acid ((S)-3-benzyl-1-benzyloxy-2,5-dioxo-pyrrolidin-3-yl)-amide 
• 909122-82-3 potassium N-acetyl-D-leucine salt 
• 374926-58-6 1-(R)-1-(2,3-dihydrobenzofuran-5-yl)-2-benzyl-2,3,4,9-tetrahydro-1H-β-carboline 
• 608142-28-5 (R)-1-(3-ethoxy-4-methoxyphenyl)-2-(methylsulfonyl)ethylamine N-acetyl-D-leucine salt 
• 876290-45-8 (R)-tetrahydropapaverine-N-acetyl-D-leucine salt 
• 187345-49-9 (+)-(3R)-3-(N-acetyl-D-leucylamino)-3-benzyl-1-hydroxysuccinimide 

Relevant articles and documents

Development of a high throughput screening tool for biotransformations utilising a thermophilic l-aminoacylase enzyme

Micro-reactors containing a monolith-immobilised thermophilic l-aminoacylase, from Thermococcus litoralis, have been developed for use in biotransformation reactions and a study has been carried out to investigate the stereospecificity and stability of the immobilised enzyme. The potential to use the developed micro-reactors as a tool for rapid screening of enzyme specificity was demonstrated, confirming that the l-aminoacylase showed a similar substrate specificity to that previously reported of the free enzyme. From this baseline, the technique was employed as a tool to evaluate potential unreported substrates with N-benzoyl- (l-threonine, l-leucine and l-arginine) and N-acetyl- (d,l-serine, d,l-leucine, l-tyrosine and l-lysine) protecting groups. The order of preferred substrates was found to be Phe > Thr > Leu > Arg for N-benzoyl substrates and Phe ? Ser > Leu > Met > Tyr > Trp for N-acetyl substrates. It was found that by using the micro-reactor a significantly smaller quantity of enzyme and substrates was required. It was shown that the micro-reactors were still operational in the presence of selected organic solvents, such as ethanol, methanol, acetone, dimethylformamide (DMF) and dimethylsulfoxide (DMSO). The results indicated that a combination of a small amount of an appropriate solvent (5% DMSO) and a higher reaction temperature could be employed in biotransformations where substrate solubility was an issue.

Enantioselective hydrolytic reactions of rice bran lipase (RBL): A first report

Enantioselectivity has been observed in the hydrolysis of racemic N-acetyl amino acid esters with rice bran lipase (RBL). The enzyme shows selectivity towards the (S)-enantiomer. Products with high enantiomeric excess (e.e. >99%) are obtained depending upon the hydrophobicity of the amino acid as well as that of the leaving group.

Selectivity in Carbonic Anhydrase Catalyzed Hydrolysis of Standard N-Acetyl-DL-amino Acid Methyl Esters

Carbonic anhydrase-catalyzed hydrolysis of some standard N-acetyl-DL-amino acid methyl esters proceeds with high enantioselectivity.This enzyme hydrolyses selectively D amino acid derivatives in contrast to proteases which have a L stereoselectivity. Key Words: carbonic anhydrase, hydrolysis, N-acetyl-DL-amino acid methyl esters, enantioselectivity.