nyltransferases

Nyltransferases are a class of enzymes that catalyze the transfer of a nucleotidyl moiety to an acceptor molecule. These enzymes are crucial in various biological processes, including nucleic acid synthesis, protein modification, and signal transduction. They typically function by cleaving a nucleoside triphosphate (NTP) and forming a new phosphodiester bond, attaching the nucleotidyl group to a substrate.

The most well-known examples of nyltransferases are DNA polymerases and RNA polymerases, which are responsible for the synthesis of DNA and RNA, respectively. These enzymes use nucleoside triphosphates as substrates to build nucleic acid chains. Other nyltransferases play roles in post-translational modification of proteins. For instance, poly(ADP-ribose) polymerases (PARPs) add poly(ADP-ribose) chains to target proteins, influencing DNA repair and other cellular events. Glycosyltransferases, which attach sugar moieties to proteins and lipids, also fall under the broader nyltransferase category, as they transfer a nucleoside diphosphate sugar.

The specificity of nyltransferases is determined by their active site, which binds both the nucleoside triphosphate and the acceptor molecule. This precise recognition ensures that the correct nucleotidyl group is transferred to the appropriate position, maintaining cellular fidelity and function. Dysregulation of nyltransferase activity can lead to various diseases, highlighting their importance in maintaining health.