Existing parts

BioBricks Name Type Function
BBa_K4209001 SULT1A1 Existing Parts rSULT1A1 is a cytosolic sulfotransferase that uses 3′-phosphoadenosine-5′-phosphosulfate (PAPS) as the sulfate donor to catalyze sulfation of diverse phenolic substrates. In this project it is used to sulfate p-coumaric acid to generate zosteric acid (p-coumaric acid 4-sulfate), functioning as the key terminal catalyst of the pathway.
BBa_K4209000 TAL Existing Parts FjTAL is a cofactor-independent enzyme that deaminates L-tyrosine to form p-coumaric acid, providing the essential aromatic precursor for downstream transformations. Within this pathway, FjTAL supplies the substrate required for zosteric acid formation.
BBa_K4209002 cysDNCQ Existing Parts The cysDN and cysCQ modules enhance sulfate activation and recycling of PAPS, thus sustaining the sulfur donor supply needed for the sulfotransferase reaction.

New basic parts

BioBricks Name Type Function
BBa_25AQDPGM SULT1A1-M1 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M1 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25B27O03 SULT1A1-M2 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M2 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25DITMET SULT1A1-M3 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M3 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_253NAKKG SULT1A1-M4 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M4 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25E1JJX1 SULT1A1-M5 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M5 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_252K220E SULT1A1-M6 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M6 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_2507CD4D SULT1A1-M7 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M7 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_258BPWPI SULT1A1-M8 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M8 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25OZ1TUD SULT1A1-M9 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M9 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25HLROGB SULT1A1-M10 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M10 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_255EHRZ2 SULT1A1-M11 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M11 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_25IGZ0OP SULT1A1-M12 New Basic Part This part encodes an improved version of the sulfotransferase SULT1A1(Part:BBa_K4209001), which catalyzes the sulfation of p-hydroxycinnamic acid (pHCA) to produce zosteric acid (ZA). The M12 variant was designed based on computational analysis (ProtSSN residue scoring and Rosetta ΔΔG predictions) to enhance folding stability and catalytic performance. It is expected to express more efficiently in E. coli and to convert pHCA to ZA with higher efficiency compared with wild-type SULT1A1.
BBa_259597SP KlATPSL New Basic Part This part encodes for the ATP sulfurylase from the yeast Kluyveromyces lactis. ATP sulfurylase is a key enzyme in the inorganic sulfur assimilation pathway, responsible for the ATP-dependent activation of inorganic sulfate to adenosine 5'-phosphosulfate (APS). In the context of Zosteric acid (ZA) biosynthesis, KIATPSL plays a crucial role in Module 2 of the pathway by ensuring a stable supply of PAPS (3'-phosphoadenosine 5'-phosphosulfate), which serves as an essential cofactor for SULT1A1-mediated conversion of p-hydroxycinnamic acid (pHCA) to ZA. The enzyme has a molecular weight of approximately 56.7 kDa and is essential for organisms that utilize sulfate as their primary sulfur source.
BBa_254YRO9Z PcAPSK New Basic Part This part encodes for the adenosine 5'-phosphosulfate (APS) kinase from the filamentous fungus Penicillium chrysogenum. APS kinase is the second enzyme in the inorganic sulfur assimilation pathway, responsible for the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine 5'-phosphosulfate (PAPS). In the context of Zosteric acid (ZA) biosynthesis, PcAPSK plays a crucial role in Module 2 of the pathway by converting APS to PAPS, which serves as an essential cofactor for SULT1A1-mediated conversion of p-hydroxycinnamic acid (pHCA) to ZA. The enzyme has a molecular weight of approximately 23.8 kDa and is essential for organisms that utilize sulfate as their primary sulfur source.
BBa_25SPDVOA SULT1A1-2GS-TAL New Basic Part SULT-2GS-TAL is designed to improve the catalytic efficiency of the SULT enzyme by fusing it with TAL via a flexible 2GS linker. This fusion protein aims to facilitate substrate channeling and enhance the overall metabolic throughput of the Zosteric acid (ZA) biosynthesis pathway. The SULT domain catalyzes the transfer of sulfonate groups from PAPS to p-hydroxycinnamic acid (pHCA), while the TAL domain converts L-tyrosine to p-coumaric acid. The 2GS linker provides structural flexibility while maintaining the independent folding and function of both domains, enabling efficient conversion of substrates in the ZA production pathway.
BBa_2532GRGV SULT1A1-2EA-TAL New Basic Part SULT1A1-2EA-TAL is designed to improve the catalytic efficiency of the SULT enzyme by fusing it with TAL via a rigid linker (EAAAK)2. This fusion protein aims to facilitate substrate channeling and enhance the overall metabolic throughput of the Zosteric acid (ZA) biosynthesis pathway. The SULT domain catalyzes the transfer of sulfonate groups from PAPS to p-hydroxycinnamic acid (pHCA), while the TAL domain converts L-tyrosine to p-coumaric acid. The linker can maintain the independent folding and function of both domains, enabling efficient conversion of substrates in the ZA production pathway.
BBa_25K1DD3C TAL-2GS-SULT1A1 New Basic Part TAL-2GS-SULT1A1 is designed to improve the catalytic efficiency of the TAL enzyme by fusing it with SULT via a flexible 2GS linker. This fusion protein aims to facilitate substrate channeling and enhance the overall metabolic throughput of the Zosteric acid (ZA) biosynthesis pathway. The SULT domain catalyzes the transfer of sulfonate groups from PAPS to p-hydroxycinnamic acid (pHCA), while the TAL domain converts L-tyrosine to p-coumaric acid. The 2GS linker provides structural flexibility while maintaining the independent folding and function of both domains, enabling efficient conversion of substrates in the ZA production pathway.
BBa_25VFSS2P TAL-2EA-SULT1A1 New Basic Part TAL-2EA-SULT1A1 is designed to improve the catalytic efficiency of the TAL enzyme by fusing it with SULT via a flexible 2EA linker. This fusion protein aims to facilitate substrate channeling and enhance the overall metabolic throughput of the Zosteric acid (ZA) biosynthesis pathway. The SULT domain catalyzes the transfer of sulfonate groups from PAPS to p-hydroxycinnamic acid (pHCA), while the TAL domain converts L-tyrosine to p-coumaric acid. The 2EA linker can maintain the independent folding and function of both domains, enabling efficient conversion of substrates in the ZA production pathway.
BBa_25HTW1DS gRNA-cysH New Basic Part Acts as the recognition module in CRISPR-Cas systems, forming a ribonucleoprotein complex with Cas enzymes and directing them to cysH sequences through Watson-Crick base pairing, thereby enabling programmable genome manipulation.
BBa_257LRWZA SULT1A1gscatcher New Basic Part The SULT1A1-GS-Catcher fusion protein combines a sulfotransferase enzyme with the GS-Catcher tag, enabling covalent conjugation to corresponding GS-Tag-modified partner proteins (such as TAL) for the assembly of multi-enzyme complexes aimed at enhancing metabolic flux in zosteric acid biosynthesis.
BBa_25DOJ6JL TALgstag New Basic Part The TALgsSpyTag fusion protein integrates tyrosine ammonia-lyase (TAL) with the SpyTag peptide via a flexible glycine-serine (GS) linker. This construct serves dual functions: the TAL domain catalyzes the conversion of L-tyrosine to p-coumaric acid, a key precursor in zosteric acid biosynthesis, while the C-terminal SpyTag enables spontaneous, covalent conjugation to SpyCatcher-fused partner proteins (e.g., SULT1A1). This modular design facilitates the assembly of multi-enzyme complexes, allowing for optimized substrate channeling and enhanced metabolic flux in engineered microbial strains.

New composite parts

BioBricks Name Type Function
BBa_25FRDAI1 KlATPSL+PcAPSK New Composite Part The KlATPSL and PcAPSK enzymes function as a coordinated two-step PAPS biosynthesis system. KlATPSL (ATP sulfurylase) catalyzes the primary activation step, converting ATP and inorganic sulfate to adenosine 5'-phosphosulfate (APS). PcAPSK (APS kinase) then phosphorylates APS using a second ATP molecule to generate 3'-phosphoadenosine-5'-phosphosulfate (PAPS)—the universal sulfonate donor for enzymatic sulfation reactions. This coupled reaction system enhances the intracellular PAPS pool, which is crucial for supporting the sulfotransferase-mediated biosynthesis of sulfated compounds like zosteric acid in engineered microbial hosts.
BBa_25LD9YEH SULT1A1-M12+TAL New Composite Part The part achieved efficient catalytic conversion from L tyrosine to Zosteric Acid (ZA) by co-expressing the optimized enzymes SULT1A1-M12 and TAL. TAL is responsible for converting L tyrosine to p coumaric acid (pHCA), while SULT1A1-M12 uses PAPS as a sulfuric acid donor to sulfate pHCA to create ZA
BBa_251QOJZW TAL-SpyTag/SpyCatcher-SULT1A1 New Composite Part The TAL-SpyTag/SpyCatcher-SULT1A1 composite part is a genetically encoded multi-enzyme complex designed for enhanced zosteric acid (ZA) biosynthesis. Through specific covalent binding between SpyTag and SpyCatcher modules, this system spatially co-localizes TAL (which produces p-coumaric acid from L-tyrosine) with SULT1A1 (which sulfonates p-coumaric acid to form ZA), potentially enabling substrate channeling and increased metabolic flux toward ZA production.