transferaseplus

TransferasePlus is a designed bifunctional enzyme that expands the transferase family by combining two catalytic modules into one polypeptide. It is capable of mediating sequential group transfers on small molecules and peptides, enabling modifications that would otherwise require two separate enzymes. The term is used mainly in synthetic biology and biocatalysis contexts.

Structure and domains: The protein consists of two modular domains connected by a flexible linker. The N-terminal domain mimics a glycosyltransferase scaffold, while the C-terminal domain provides a distinct donor site. The arrangement supports substrate channeling and cooperative catalysis, though exact geometry depends on design and expression system.

Catalysis and substrates: TransferasePlus transfers functional groups such as sugars, acetyl, phosphate, or methyl groups from a donor to an acceptor. Reactions are typically consecutive, with each domain contributing its own active-site residues. Substrate scope is engineered, often focusing on UDP-sugars and nucleophilic acceptors like hydroxyls or amines.

Development and status: The concept arose in protein-engineering studies of modular enzyme fusion. Research aims to improve stability, solubility, and catalytic efficiency, with linker optimization and directed evolution helping to tailor activity to chosen donors and acceptors.

Applications and outlook: Potential uses include streamlined synthesis of glycosylated natural products, modified drugs, and novel materials. In biotechnology, transferasePlus can simplify pathway design by enabling one-pot multi-step transformations. Ongoing work seeks to expand donor/acceptor compatibility and establish robust, scalable performance.