152899-13-3

Basic information

• Product Name: 2-Oxazolidinone, 3-(1-oxooctyl)-4-(phenylmethyl)-, (4S)-
• CAS NO: 152899-13-3
• Molecular Formula: C18H25NO3
• Molecular Weight: 303.401
• Mol File: 152899-13-3.mol
• Article Data: 11

Chemical Properties

• CAS DataBase Reference: 2-Oxazolidinone, 3-(1-oxooctyl)-4-(phenylmethyl)-, (4S)-(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Oxazolidinone, 3-(1-oxooctyl)-4-(phenylmethyl)-, (4S)-(152899-13-3)
• EPA Substance Registry System: 2-Oxazolidinone, 3-(1-oxooctyl)-4-(phenylmethyl)-, (4S)-(152899-13-3)

Safety Data

• Hazardous Substances Data: 152899-13-3(Hazardous Substances Data)

Upstream product

• 131685-53-5 (S)-4-benzyl-3-propionyl-2-oxazolidinone 
• 111-64-8 n-octanoic acid chloride 
• 152899-15-5 <3(2'R),4S>-3-(2-Methyl-1-oxooctyl)-4-(phenylmethyl)-2-oxazolidinone 
• 87877-11-0 Phe-Chlor 
• 3081-24-1 H-Phe-OEt 
• 3182-95-4 L-Phenylalaninol 
• 63-91-2 L-phenylalanine 
• 124-07-2 Octanoic acid 
• 90719-32-7 (S)-4-Benzyl-2-oxazolidinone 
• 101711-90-4 (S)-4-benzyl-2-oxazolidinone lithium salt 

Downstream Products

• 90719-32-7 (S)-4-Benzyl-2-oxazolidinone 
• 548783-48-8 (S)-3-((R)-2-allyloctanoyl)-4-benzyloxazolidin-2-one 
• 1336884-44-6 methyl 6-((1S,2R)-2-((S)-4-benzyl-2-oxooxazolidine-3-carbonyl)-1-hydroxyoctyl)phenazine-1-carboxylate 

Relevant articles and documents

Understanding Programming of Fungal Iterative Polyketide Synthases: The Biochemical Basis for Regioselectivity by the Methyltransferase Domain in the Lovastatin Megasynthase

Highly reducing polyketide synthases (HR-PKSs) from fungi synthesize complex natural products using a single set of domains in a highly programmed, iterative fashion. The most enigmatic feature of HR-PKSs is how tailoring domains function selectively during different iterations of chain elongation to afford structural diversity. Using the lovastatin nonaketide synthase LovB as a model system and a variety of acyl substrates, we characterized the substrate specificity of the LovB methyltransferase (MT) domain. We showed that, while the MT domain displays methylation activity toward different β-ketoacyl groups, it is exceptionally selective toward its naturally programmed β-keto-dienyltetraketide substrate with respect to both chain length and functionalization. Accompanying characterization of the ketoreductase (KR) domain displays broader substrate specificity toward different β-ketoacyl groups. Our studies indicate that selective modifications by tailoring domains, such as the MTs, are achieved by higher kinetic efficiency on a particular substrate relative to the rate of transformation by other competing domains.

Structural Requirements of HDAC Inhibitors: SAHA Analogues Modified at the C2 Position Display HDAC6/8 Selectivity

Histone deacetylase (HDAC) proteins are epigenetic regulators that deacetylate protein substrates, leading to subsequent changes in cell function. HDAC proteins are implicated in cancers, and several HDAC inhibitors have been approved by the FDA as antica

Total synthesis of emericellamides A and B

The total synthesis of emericellamides A and B is reported. A convergent, flexible strategy employing peptide chemistry, asymmetric alkylations, and culminating in macrolactamization is described. The previously reported structure of both compounds is confirmed.