Disclosed is recombinant Escherichia coli for producing L-tyrosine and application thereof, and belongs to the technical fields of genetic engineering and bioengineering. According to the present disclosure, genes aroP and tyrP are knocked out, expresses the endogenous gene yddG of E. coli, then heterologously expresses fpk from Bifidobacterium adolescentis, expresses the endogenous genes ppsA and tktA of E. coli, and then expresses aroG.sup.fbr and tyrA.sup.fbr. Knocking out tyrR, trpE and pheA, so that the synthesis flux of L-tyrosine is increased. Finally, an endogenous gene poxB is knocked out to realize stable fermentation performance at high glucose concentration.

The present invention provides an isolated or engineered polypeptide, a microorganism comprising a nucleic acid sequence encoded by the polypeptide, and a method for synthesizing a polyphenolic phytochemicals phosphate derivative using the polypeptide or the microorganism. The polypeptide having a homologous protein sequence that is more than 70% identical to the polyphenol phosphorylation synthetase (SEQ ID NO: 13) comprises a conserved domain which sequentially comprises: an ATP-binding domain, which includes active catalytic sites of Lys27, Arg102, and Glu282; a substrate-binding domain, which includes a conserved motif of DDHHFYIDAMLDAKAR (SEQ ID NO: 14), and includes active catalytic sites of Asp627, His629, and His630; and a phosphorylated histidine catalytic domain, which includes His795 based on SEQ ID NO: 13.

Genetically engineered immune cells, which express at least two metabolism modulating polypeptides and optionally a chimeric receptor polypeptide (e.g., an antibody-coupled T cell receptor (ACTR) polypeptide or a chimeric antigen receptor (CAR) polypeptide) capable of binding to a target antigen of interest. Also disclosed herein are uses of the engineered immune cells for inhibiting cells expressing a target antigen in a subject in need thereof.

Bio-production processes that rely on biological activity can be very slow and inefficient, yet, the output of these processes may have significant value. Using biological enzymes outside their natural cellular environments offers a significant and largely untapped opportunity to enhance bio-production processes. By decoupling enzymes from their native contexts, one can modify both their sequences and structures in ways that are favorable for industrial applications. This system and method mixes substrate molecules, PPi, and enzymes that utilize PPi (PPi-dependent enzymes) in a reaction chamber and ends with stable-form products, including phosphorylated molecules.