1548502-95-9

Upstream product

• 1548502-83-5 (2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-(4-azidobutoxy)-2-(hydroxymethyl)tetrahydrofuranol 
• 1548502-93-7 ((2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-(4-azidobutoxy)-3-((tert-butyldimethylsilyl)oxy)tetrahydrofuran-2-yl)methyl sulfamate 
• 3674-06-4 Boc-Phe-ONSu 
• 1548502-85-7 ((2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-(4-azidobutoxy)-3-((tert-butyldimethylsilyl)oxy)tetrahydrofuran-2-yl)methanol 
• 1548502-84-6 9-((2R,3R,4R,5R)-3-(4-azidobutoxy)-4-((tert-butyldimethylsilyl)oxy)-5-(((tert-butyldimethylsilyl)oxy)methyl)tetrahydrofuran-2-yl)-9H-purin-6-amine 

Downstream Products

• 1548502-99-3 ((2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-(4-aminobutoxy)-3-((tert-butyldimethylsilyl)oxy)tetrahydrofuran-2-yl)methyl ((S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanoyl)sulfamate 

Relevant academic research and scientific papers

Active site-directed proteomic probes for adenylation domains in nonribosomal peptide synthetases

We describe a general strategy for selective chemical labeling of individual adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) using active site-directed proteomic probes coupled to the 5′-O-N-(aminoacyl)sulfamoyladenosine (AMS) scaffold

Specific enrichment of nonribosomal peptide synthetase module by an affinity probe for adenylation domains

We targeted the development of an affinity probe for adenylation (A) domains that can facilitate enrichment, identification, and quantification of A domain-containing modules in nonribosomal peptide synthetase (NRPS)-polyketide synthase (PKS) hybrids and NRPSs. A 5′-O-sulfamoyladenosine (AMS) non-hydrolyzable analogue of adenosine monophosphate (AMP) has been reported as a scaffold for the design of inhibitors exhibiting tight binding of adenylation enzymes. Here we describe the application of an affinity probe for A domains. Our synthetic probe, a biotinylated l-Phe-AMS (l-Phe-AMS-biotin) specifically targets the A domains in NRPS modules that activates l-Phe to an aminoacyladenylate intermediate in both recombinant NRPS enzyme systems and whole proteomes.