COAA E.Coli
Description
COAA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Recombinant expression of pantothenate kinase in Escherichia coli (E. coli) has been extensively studied due to its importance in metabolic engineering and synthetic biology. E. coli is a widely used host for the production of recombinant proteins because of its well-characterized genetics, rapid growth, and ability to express foreign genes efficiently .
The recombinant pantothenate kinase from E. coli is typically produced as a single, non-glycosylated polypeptide chain. It consists of 340 amino acids and has a molecular mass of approximately 38.9 kDa. The enzyme is often fused to a His-tag at the N-terminus to facilitate purification through affinity chromatography .
Pantothenate kinase plays a pivotal role in maintaining the intracellular levels of CoA. The enzyme’s activity is regulated by feedback inhibition, where high levels of CoA and its derivatives inhibit its function. This regulation ensures a balanced supply of CoA within the cell, which is essential for various metabolic processes .
The recombinant expression of pantothenate kinase in E. coli has several biotechnological applications:
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Enhanced Production of CoA Derivatives: By overexpressing pantothenate kinase, researchers can increase the intracellular levels of CoA, which in turn enhances the production of CoA derivatives such as 3-hydroxybutyrate (3HB). This is particularly useful in the production of bioplastics and other valuable compounds .
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Metabolic Engineering: Pantothenate kinase is used in metabolic engineering to optimize the production of various metabolites. For example, co-expressing pantothenate kinase with other enzymes involved in fatty acid biosynthesis can significantly increase the yield of fatty acids in E. coli .
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Synthetic Biology: In synthetic biology, pantothenate kinase is employed to construct synthetic pathways for the production of novel compounds. By manipulating the CoA biosynthetic pathway, researchers can create engineered strains of E. coli capable of producing a wide range of biochemicals .
Recent studies have focused on the expression of pantothenate kinase from different taxonomic origins in E. coli to identify variants with improved properties. For instance, expressing pantothenate kinase from Aspergillus nidulans and Mus musculus in E. coli has shown promising results in enhancing the production of 3HB . These studies highlight the potential of using heterologous expression systems to improve the efficiency of CoA biosynthesis and its derivatives.
