Back Nukleotidiltransferaza BS Nukleotidyltransferase German Nucléotidyltransférase French Nucleotidiltransferase Galician Nucleotidiltransferase Portuguese Nukleotidiltransferaza Serbo-Croatian 核苷酸基转移酶 Chinese

Nucleotidyltransferase

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 (Pi, in red). The protein names are those in E. coli. Homologs in other bacteria may have different names.[1]

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:

A-P-N + B A + B-P-N

For example, in the case of polymerases, A is pyrophosphate and B is the nascent polynucleotide. They are classified under EC number 2.7.7 and they can be categorised into:

  1. Uridylyltransferases, which transfer uridylyl- groups
  2. Adenylyltransferases, which transfer adenylyl- groups
  3. Guanylyltransferases, which transfer guanylyl- groups
  4. Cytitidylyltransferases, which transfer cytidylyl- groups
  5. Thymidylyltransferases, which transfer thymidylyl- groups
  1. ^ Voet D, Voet JG, Pratt CW (2008). Fundamentals of Biochemistry (3rd ed.). John Wiley & Sons, pp. 767
From Wikipedia, the free encyclopedia · View on Wikipedia

Developed by Tubidy