Glucose-1-phosphate thymidylyltransferase

Function

Glucose-1-phosphate thymidylyltransferase (RmlA) catalyzes the conversion of dTTP and α-D-glucose 1-phosphate (DGP) to diphosphate and dTDP-glucose or dTDP- rhamnose. RmlA participates in nucleotide sugars metabolism, streptomycin biosynthesis and polyketide sugar metabolism^[1].

Relevance

dTDP- rhamnose is a component of bacterial cell wall, hence RmlA inhibition is a potential therapeutic target as drugs against pathogenic bacteria.

Structural highlights

RmlA 3D structure can be divided into three functional domains: a core domain which binds . The is formed by the core and sugar-binding domains and the residues comprising it can be divided to catalytic residues (in cyan) and thymidine-specific residues (in green). ^[2].

3D structures of glucose-1-phosphate thymidylyltransferase

Glucose-1-phosphate thymidylyltransferase 3D structures