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Enzymatic Synthesis of Oligopeptide
Non-Ribosomal Peptide Synthetases (NRPSs)
Non-ribosomal peptide synthesis is a universal and critical biochemical process catalyzed by NRPSs in bacteria and fungi, through which a wide array of therapeutically important peptides with highly diverse structures and bioactivities, including penicillin, bleomycin, and cyclosporine, are produced. Biocatalysts capable of NRP synthesis could be divided into two groups (ATP-independent and ATP-dependent enzymes) based on the difference in substrate activation. In the ATP-dependent process, enzymes such as tRNA-dependent ligase can activate the substrate through aminoacyl-adenosine monophosphate. In the ATP-independent process, enzymes such as transacylase use aminoacyl phosphate.
Peptide Synthesis at Creative Peptides
| Services | Description |
| Peptide Synthesis Services | We provide high-quality customized peptide synthesis services, from bulk API peptides, high-throughput library peptides, cosmetic peptides, to array peptides, antigen peptides, and other complex or abnormal peptide sequences. |
| Peptide Modification Services | Creative Peptides offers hundreds of peptide modifications to meet any research need. These modifications can improve the overall stability of peptide, change the structure to better understand biological functions, or enhance the immunogenicity of antibody development and production. |
| Custom Conjugation Service | Creative Peptides provides convenient multiple types of peptide conjugation services to meet the needs of different projects, including activating immune responses, obtaining higher stability and cell penetration. |
ATP-Grasp Enzymes
The ATP-grasp enzymes, also known as ATP-dependent carboxylate-amine ligases, activate acids like acylphosphate intermediates and are found in various biological systems such as de novo purine biosynthesis. Notable members of this family include biotin carboxylase, Ddl, and glutathione synthetase. ATP-grasp enzymes usually have a unique structure with three conserved domains, with a nonclassical ATP binding fold enclosing an ATP molecule. Most of these enzymes require an Mg2+ ion coordinated by ATP in the active site.
