93413-07-1

Basic information

• Product Name: asperlicin D
• Synonyms: asperlicin D
• CAS NO: 93413-07-1
• Molecular Formula: C25H18N4O2
• Molecular Weight: 406.443
• Mol File: 93413-07-1.mol

Chemical Properties

• Boiling Point: 704.1°Cat760mmHg
• Flash Point: 379.6°C
• Appearance: /
• Density: 1.43g/cm³
• Vapor Pressure: 1.14E-19mmHg at 25°C
• Refractive Index: 1.766
• CAS DataBase Reference: asperlicin D(CAS DataBase Reference)
• NIST Chemistry Reference: asperlicin D(93413-07-1)
• EPA Substance Registry System: asperlicin D(93413-07-1)

Safety Data

• Hazardous Substances Data: 93413-07-1(Hazardous Substances Data)

Usage

InChI:InChI=1/C25H18N4O2/c30-24-22(13-15-14-26-19-10-4-1-7-16(15)19)29-23(17-8-2-5-11-20(17)28-24)27-21-12-6-3-9-18(21)25(29)31/h1-12,14,22,26-27H,13H2/t22-/m0/s1

Upstream product

• 118-48-9 isatoic anhydride 
• 34897-85-3 o-azidobenzoyl chloride 
• 610-14-0 2-nitrobenzyl chloride 
• 4299-70-1 L-tryptophan methyl ester 
• 106466-76-6 asperlicin D 
• 13139-14-5 Boc-Trp-OH 
• 118-92-3 anthranilic acid 
• 73-22-3 L-Tryptophan 

Downstream Products

• 101389-64-4 C₂₅H₁₈N₄O₂ 

Relevant articles and documents

Total synthesis of asperlicin D

Cyclodehydration of a linear tripeptide furnished the first total synthesis of asperlicin D in moderate yield. The cyclodehydration process was triggered by an intramolecular nucleophilic acyl substitution and an intramolecular aza-Wittig reaction.

An iterative, bimodular nonribosomal peptide synthetase that converts anthranilate and tryptophan into tetracyclic asperlicins

The bimodular 276 kDa nonribosomal peptide synthetase AspA from Aspergillus alliaceus, heterologously expressed in Saccharomyces cerevisiae, converts tryptophan and two molecules of the aromatic β-amino acid anthranilate (Ant) into a pair of tetracyclic peptidyl alkaloids asperlicin C and D in a ratio of 10:1. The first module of AspA activates and processes two molecules of Ant iteratively to generate a tethered Ant-Ant-Trp-S-enzyme intermediate on module two. Release is postulated to involve tandem cyclizations, in which the first step is the macrocyclization of the linear tripeptidyl-S-enzyme, by the terminal condensation (CT) domain to generate the regioisomeric tetracyclic asperlicin scaffolds. Computational analysis of the transannular cyclization of the 11-membered macrocyclic intermediate shows that asperlicin C is the kinetically favored product due to the high stability of a conformation resembling the transition state for cyclization, while asperlicin D is thermodynamically more stable.

Assembly of asperlicin peptidyl alkaloids from anthranilate and tryptophan: A two-enzyme pathway generates heptacyclic scaffold complexity in asperlicin E

Members of the asperlicin family of fungal metabolites produced by Aspergillus alliaceus are known potent CCKA antagonists. Herein, we report the identification of the gene cluster responsible for directing their biosynthesis. We validate and probe the pathway by genetic manipulation, and provide the first biochemical characterization of the oxidative cyclization en route to the heptacyclic asperlicin E by reconstituting the activity of the FAD depend monooxygenase AspB. This report provides the first genetic characterization of a NRPS assembly line that efficiently activates two anthranilate building blocks and illustrates the remarkably efficient biosynthesis of the complex heptacyclic asperlicin E.