Threonylcarbamoyl-AMP synthase (YRDC)

Threonylcarbamoyl-AMP synthase (YRDC) is a highly conserved enzyme present in organisms from bacteria to humans. YRDC is essential in some species and functions as part of a universal protein family (YrdC/Sua5), critical for the post-transcriptional modification of tRNA at position 37 (t^6^A^37^, threonylcarbamoyladenosine). This modification is required for accurate and efficient protein translation by stabilizing codon-anticodon interactions and maintaining the translational reading frame[1][4]. YRDC preferentially binds unmodified tRNA and the substrates ATP and threonine, implicating it in the early steps of t^6^A synthesis, likely as an ATP/AMP synthase in an enzymatic complex[1]. In humans, YRDC is involved in genome maintenance and protein synthesis, and its upregulation has been associated with cancer cell proliferation, migration, and drug resistance, possibly by modulating efflux transporter processing[3]. YRDC's structure features a basic, concave surface suitable for double-stranded RNA binding[2]. Current evidence does not indicate the presence of clinically approved drugs targeting YRDC directly, but its expression may influence resistance or sensitivity to cancer therapies[3].

Other names

yrdC N6-threonylcarbamoyltransferase domain containingDopamine receptor-interacting protein 3DRIP3IRIPhIRIPFLJ23476SUA5Ischemia/reperfusion-inducible protein homologGAMOS10yrdC domain-containing protein, mitochondrial

Not a direct drug target; acts as a modulator of cellular processes affecting drug transporter expression and drug sensitivity[3]