Nucleotidyltransferase

Nucleotidyltransferases are transferase enzymes of phosphorus-containing groups, e.g., substituents of nucleotidylic acids or simply nucleoside monophosphates.

The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as: For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide.

The attachment of an AMP (adenylylation) or UMP (uridylylation) can activate or inactivate an enzyme or change its specificity (see figure).

These modifications can lead to intricate regulatory networks that can finely tune enzymatic activities so that only the needed compounds are made (here: glutamine).

This repair mechanism begins when a single nucleotide is recognized by DNA glycosylase as incorrectly matched or has been mutated in some way (UV light, chemical mutagen, etc.

Regulation of bacterial glutamine synthase (GlnA) by adenylylation and (indirectly) by uridylylation . Uridylyltransferase (GlnD) uridylylates the regulatory PII protein (GlnB) which determines whether adenylyltransferase (GlnE) adenylylates or de-adenylylates glutamine synthase. GlnD is a bifunctional enzyme that both attaches and removes UMP from GlnB. GlnD is activated by α-ketoglutarate and ATP (green) but inhibited by glutamine and inorganic phosphate (P i , in red). The protein names are those in E. coli . Homologs in other bacteria may have different names. [ 1 ]