Recombinant Escherichia coli Transaldolase B (talB)

Amino acids 2-317 form the expressed segment for recombinant Escherichia coli (strain K12) talB. The theoretical molecular weight of the talB protein is 42.5 kDa. This talB recombinant protein is manufactured in e.coli. The N-terminal 10xHis tag and C-terminal Myc tag was smoothly integrated into the coding gene of talB, which enables a simple process of detecting and purifying the talB recombinant protein in the following steps.

Transaldolase B (TalB) in Escherichia coli is an enzyme involved in the non-oxidative phase of the pentose phosphate pathway (PPP), a metabolic pathway crucial for the production of ribose-5-phosphate and NADPH. TalB specifically catalyzes the reversible transfer of a three-carbon dihydroxyacetone moiety from the ketose donor fructose-6-phosphate to the aldose acceptor erythrose-4-phosphate. This reaction results in the formation of sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The pentose phosphate pathway plays a vital role in balancing the cell's need for ribose-5-phosphate, a precursor for nucleotide biosynthesis, and generating reducing equivalents in the form of NADPH. TalB's involvement in this pathway positions it at the intersection of central carbon metabolism and nucleotide biosynthesis, making it crucial for cellular growth and homeostasis. Understanding the functions of TalB contributes to the broader knowledge of bacterial metabolism and has potential applications in metabolic engineering for the production of biofuels or other valuable compounds.