ATP-Binding Domain-Containing Protein 4 (ATPBD4) Antibody

Background

DPH6 is an ATP-dependent enzyme responsible for converting the diphthine intermediate to diphthamide through the addition of an amidino group. It acts in the final step of diphthamide biosynthesis, ensuring that the modified histidine residue on eEF2 achieves its fully functional state. DPH6 relies on the coordinated action of other diphthamide biosynthesis proteins to access substrates and carry out its catalytic activity. Genetic studies indicate that mutations or disruptions in DPH6 can result in resistance to bacterial toxins such as diphtheria toxin and impaired ribosomal translocation, highlighting its critical cellular role. DPH6 contains conserved ATP-binding motifs essential for its enzymatic function, and its expression is tightly regulated in metabolically active tissues. The absence of functional DPH6 disrupts protein synthesis, leading to cellular and organismal defects, particularly in systems dependent on high translational efficiency. DPH6 also interacts with DPH7, facilitating the amidination reaction and ensuring proper coordination of the biosynthesis pathway.