21469-33-0

Basic information

• Product Name: Octanamide, N-[2-(4-hydroxyphenyl)ethyl]-
• CAS NO: 21469-33-0
• Molecular Formula: C16H25NO2
• Molecular Weight: 263.38
• Mol File: 21469-33-0.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: Octanamide, N-[2-(4-hydroxyphenyl)ethyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: Octanamide, N-[2-(4-hydroxyphenyl)ethyl]-(21469-33-0)
• EPA Substance Registry System: Octanamide, N-[2-(4-hydroxyphenyl)ethyl]-(21469-33-0)

Safety Data

• Hazardous Substances Data: 21469-33-0(Hazardous Substances Data)

Upstream product

• 51-67-2 tyrosamine 
• 111-64-8 n-octanoic acid chloride 
• 60-19-5 tyramine hydrochloride 
• 71478-41-6 (ethoxycarbonyl)octanoate 
• 124-07-2 Octanoic acid 
• 1264-52-4 octanoyl coenzyme A 

Relevant articles and documents

YUA001, a novel aldose reductase inhibitor isolated from alkalophilic Corynebacterium sp. YUA25 II. Chemical modification and biological activity

A series of novel N-substituted tyramine (2-p-hydroxyphenylethylamine) derivatives (1-11) were synthesized and evaluated for their inhibitory activity against pig kidney aldose reductase (EC 1, 1, 1, 21). Of these compounds, N-2-p-hydroxyphenylethyl maleamic acid (10) exhibits the strongest aldose reductase inhibitory activity, which is 22 times more potent than that of YUA0011).

Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases

(Chemical Equation Presented). Arylalkylamine N-acetyltransferase (AANAT) catalyzes the penultimate step in the biosynthesis of melatonin and other N-acetylarylalkylamides from the corresponding arylalkylamine and acetyl-CoA. The N-acetylation of arylalkylamines is a critical step in Drosophila melanogaster for the inactivation of the bioactive amines and the sclerotization of the cuticle. Two AANAT variants (AANATA and AANATB) have been identified in D. melanogaster , in which AANATA differs from AANATB by the truncation of 35 amino acids from the N-terminus. We have expressed and purified both D. melanogaster AANAT variants (AANATA and AANATB) in Escherichia coli and used the purified enzymes to demonstrate that this N-terminal truncation does not affect the activity of the enzyme. Subsequent characterization of the kinetic and chemical mechanism of AANATA identified an ordered sequential mechanism, with acetyl-CoA binding first, followed by tyramine. We used a combination of pH-activity profiling and site-directed mutagenesis to study prospective residues believed to function in AANATA catalysis. These data led to an assignment of Glu-47 as the general base in catalysis with an apparent pKa of 7.0. Using the data generated for the kinetic mechanism, structure-function relationships, pH-rate profiles, and site-directed mutagenesis, we propose a chemical mechanism for AANATA.