21708-76-9

Basic information

• Product Name: S-{(9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} hexanethioate (non-preferred
• CAS NO: 21708-76-9
• Molecular Formula: C₂₇H₄₆N₇O₁₇P₃S
• Molecular Weight: 865.6771
• Mol File: 21708-76-9.mol
• Article Data: 13

Chemical Properties

• Density: 1.76g/cm³
• Refractive Index: 1.685
• CAS DataBase Reference: S-{(9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} hexanethioate (non-preferred(CAS DataBase Reference)
• NIST Chemistry Reference: S-{(9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} hexanethioate (non-preferred(21708-76-9)
• EPA Substance Registry System: S-{(9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} hexanethioate (non-preferred(21708-76-9)

Safety Data

• Hazardous Substances Data: 21708-76-9(Hazardous Substances Data)

Upstream product

• 6701-39-9 (2E)-hexenoyl-coenzyme A 
• 13419-69-7 (E)-2-Hexenoic acid 
• 142-62-1 hexanoic acid 
• 132129-32-9 [5']adenylic acid hexanoic acid-anhydride 
• 85-61-0 coenzyme A 
• 288-32-4 1H-imidazole 
• 1191-04-4 2-hexenoic acid 
• 72531-43-2 C₉H₁₆O₄ 
• 60988-34-3 1-(1-imidazolyl)-1-hexanone 

Downstream Products

• 524735-63-5 4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one 
• 81017-02-9 4-hydroxy-6-pentyl-2H-pyrone 
• 327175-05-3 4-hydroxy-6-(2-oxoheptyl)-2-pyrone 
• 142-62-1 hexanoic acid 
• 6701-39-9 (2E)-hexenoyl-coenzyme A 
• 5665-89-4 1-(2,4,6-trihydroxyphenyl)hexan-1-one 
• 1159918-23-6 6-(2-(2,4-dihydroxy-6-methylphenyl)-2-oxoethyl)-4-hydroxy-2-pyrone 
• 1184818-23-2 N-[2-(4-hydroxyphenyl)ethyl]hexanamide 
• 1443502-36-0 urauchimycin B 

Relevant articles and documents

Non-enzymic reactions of acyl adenylate and imidazole.

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In vitro studies of maleidride-forming enzymes

In vitro assays of enzymes involved in the biosynthesis of maleidrides from polyketides in fungi were performed. The results show that the enzymes are closely related to primary metabolism enzymes of the citric acid cycle in terms of stereochemical preferences, but with an expanded substrate selectivity. A key citrate synthase can react both saturated and unsaturated acyl CoA substrates to give solely anti substituted citrates. This undergoes anti-dehydration to afford an unsaturated precursor which is cyclised in vitro by ketosteroid-isomerase-like enzymes to give byssochlamic acid. This journal is

Repurposing the 3-Isocyanobutanoic Acid Adenylation Enzyme SfaB for Versatile Amidation and Thioesterification

Genome mining of microbial natural products enables chemists not only to discover the bioactive molecules with novel skeletons, but also to identify the enzymes that catalyze diverse chemical reactions. Exploring the substrate promiscuity and catalytic mechanism of those biosynthetic enzymes facilitates the development of potential biocatalysts. SfaB is an acyl adenylate-forming enzyme that adenylates a unique building block, 3-isocyanobutanoic acid, in the biosynthetic pathway of the diisonitrile natural product SF2768 produced by Streptomyces thioluteus, and this AMP-ligase was demonstrated to accept a broad range of short-chain fatty acids (SCFAs). Herein, we repurpose SfaB to catalyze amidation or thioesterification between those SCFAs and various amine or thiol nucleophiles, thereby providing an alternative enzymatic approach to prepare the corresponding amides and thioesters in vitro.

Screening and Engineering the Synthetic Potential of Carboxylating Reductases from Central Metabolism and Polyketide Biosynthesis

Carboxylating enoyl-thioester reductases (ECRs) are a recently discovered class of enzymes. They catalyze the highly efficient addition of CO2 to the double bond of α,β-unsaturated CoA-thioesters and serve two biological functions. In primary metabolism of many bacteria they produce ethylmalonyl-CoA during assimilation of the central metabolite acetyl-CoA. In secondary metabolism they provide distinct α-carboxyl-acyl-thioesters to vary the backbone of numerous polyketide natural products. Different ECRs were systematically assessed with a diverse library of potential substrates. We identified three active site residues that distinguish ECRs restricted to C4 and C5-enoyl-CoAs from highly promiscuous ECRs and successfully engineered a selected ECR as proof-of-principle. This study defines the molecular basis of ECR reactivity, allowing for predicting and manipulating a key reaction in natural product diversification.