60115-34-6

Upstream product

• 60115-45-9 S-(o-nitrophenyl)-L-cysteine 
• 49732-37-8 2-Nitrobenzenediazonium Bisulfate 
• 407-41-0 L-phosphoserine 
• 137-07-5 2-amino-benzenethiol 
• 5147-00-2 O-acetyl-L-serine 
• 1493-27-2 ortho-nitrofluorobenzene 

Relevant academic research and scientific papers

Expanding the Structural Diversity of Protein Building Blocks with Noncanonical Amino Acids Biosynthesized from Aromatic Thiols

Incorporation of structurally novel noncanonical amino acids (ncAAs) into proteins is valuable for both scientific and biomedical applications. To expand the structural diversity of available ncAAs and to reduce the burden of chemically synthesizing them, we have developed a general and simple biosynthetic method for genetically encoding novel ncAAs into recombinant proteins by feeding cells with economical commercially available or synthetically accessible aromatic thiols. We demonstrate that nearly 50 ncAAs with a diverse array of structures can be biosynthesized from these simple small-molecule precursors by hijacking the cysteine biosynthetic enzymes, and the resulting ncAAs can subsequently be incorporated into proteins via an expanded genetic code. Moreover, we demonstrate that bioorthogonal reactive groups such as aromatic azides and aromatic ketones can be incorporated into green fluorescent protein or a therapeutic antibody with high yields, allowing for subsequent chemical conjugation.

Facile Synthesis of S-Substituted L-Cysteines with Nano-sized Immobilized O-Acetylserine Sulfhydrylase

Many S-substituted l-cysteines are useful pharmaceutical intermediates but require a simple synthesis method. Here we developed enzymatic synthesis of several S-aryl-l-cysteines and S-benzyl-l-cysteine directly from O-acetylserine (OAS) with immobilized O-acetylserine sulfhydrylase CysM. Novel iron-oxide magnetic nanoparticles (MNPs) with cobalt-nitrilotriacetic acid function were prepared with a diameter of 80 nm in 75 % yield. Direct immobilization of His-tagged CysM in the cell-free extract on the MNPs via affinity attachment afforded stable nanobiocatalyst with 97 % enzyme loading efficiency and 93 % free enzyme activity. The immobilized enzyme catalyzed the biotransformation of benzylthiol and OAS to give S-benzyl-l-cysteine in 88 % yield. The nanobiocatalyst also demonstrated high recyclability, retaining 95 % productivity in the fifth cycle. The immobilized CysM accepts various arylthiols to react with OAS, giving rise to a new synthesis route of several S-substituted l-cysteines in 60–96 % yield.

Unnatural amino acid synthesis by thermostable O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1

O-Acetyl-L-serine sulfhydrylase (OASS) from plants and bacteria synthesizes cysteine and unnatural amino acids that are important building blocks for active pharmaceuticals and agrochemicals. A thermostable O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1 (OPSSAp) exhibits a function similar to OASS. In the present study, we examined the synthesis of various unnatural amino acids using OPSSAp and demonstrated OPSSAp could efficiently synthesize various sulfur-containing amino acids. OPSSAp would be useful for industrial production of biologically important unnatural amino acids.