187537-23-1

Basic information

• Product Name: N-[(2S)-2-hydroxy-3-(naphthalen-1-yloxy)propyl]acetamide
• CAS NO: 187537-23-1
• Molecular Formula: C₁₅H₁₇NO₃
• Molecular Weight: 259.3004
• Mol File: 187537-23-1.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 544.4°C at 760 mmHg
• Flash Point: 283°C
• Density: 1.192g/cm³
• Vapor Pressure: 1.1E-12mmHg at 25°C
• Refractive Index: 1.6
• CAS DataBase Reference: N-[(2S)-2-hydroxy-3-(naphthalen-1-yloxy)propyl]acetamide(CAS DataBase Reference)
• NIST Chemistry Reference: N-[(2S)-2-hydroxy-3-(naphthalen-1-yloxy)propyl]acetamide(187537-23-1)
• EPA Substance Registry System: N-[(2S)-2-hydroxy-3-(naphthalen-1-yloxy)propyl]acetamide(187537-23-1)

Safety Data

• Hazardous Substances Data: 187537-23-1(Hazardous Substances Data)

Upstream product

• 88547-38-0 (-)-Desisopropylpropranolol 
• 72-89-9 acetylcoenzyme A 
• 88547-39-1 (+)-Desisopropylpropranolol 

Relevant articles and documents

Enantioselective N-acetylation of N-desisopropylpropranolol by rat liver acetyltransferase

The enantioselective N-acetylation of N-desisopropylpropranolol (NDP), one of the main metabolites of propranolol (PL), by rat liver acetyltransferase (AT), was investigated. R(+)-NDP or S(-)-NDP was used as a substrate at concentrations ranging from 10 to 200 μM. The cytosol fraction of a rat liver containing 3.93 mg protein/ml served as the source of AT. For 1-amino-3-(1-naphthyloxy)-2-propanol (AcNDP) formation from R(+)-NDP or s(- )-NDP in the presence of infinite AcCoA (250 μM), the K(m) value was calculated to be 67.5 or 62.4 μM, and the V(max) value was 0.462 or 0.205 nmol/min/mg protein. Based on these findings, the enantioselective N- acetylation of NDP was proved, i.e., AcNDP formation from R(+)-NDP was found to take place more easily than that from S(-)-NDP. Furthermore, AcNDP formation from NDP was competitively inhibited by the exogenous arylamine, p- aminobenzoic acid (PABA), which is well-known to be a typical substrate of AT. The presence of enantioselective inhibition for AcNDP formation was thus confirmed based on the K(i) values, 440 μM in the case of R(+)-NDP and 250 μM in the case of S(-)-NDP, respectively, i.e. two-fold enantioselective inhibition was demonstrated based on the Ki values in S(-)-enantiomer in comparison with R(+)-enantiomer.