Nucleotidyltransferase

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]

Nucleotidyltransferases are

nucleoside monophosphates

. The general reaction of transferring a nucleoside monophosphate moiety from A to B, can be written as:

A-P-N + B

\rightleftharpoons

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:

uridylyl
- groups
adenylyl
- groups
guanylyl
- groups
cytidylyl
- groups
thymidylyl
- groups

Role in metabolism

Many metabolic enzymes are modified by nucleotidyltransferases. 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).^[1]

Role in DNA repair mechanisms

Nucleotidyl transferase is a component of the repair pathway for single nucleotide

template strand as the reference.^[2]

References

^ ^a ^b Voet D, Voet JG, Pratt CW (2008). Fundamentals of Biochemistry (3rd ed.). John Wiley & Sons, pp. 767
^ Yuan Liu; Rajendra Prasad; William A. Beard; Padmini S. Kedar; Esther W. Hou; David D. Shock; Samuel H. Wilson (May 4, 2007). "Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β". Journal of Biological Chemistry. 282 (18): 13532–13541.
PMID 17355977
. The enzymes and accessory factors involved in the BER subpathways in mammalian cells have received considerable attention. As summarized above, five distinct enzymatic reaction are involved during SN-BER. These are 1) removal of a modified base by a lesion-specific monofunctional DNA N-glycosylase, 2) 5'-incision of the abasic site by a hydrolytic strand incision enzyme, 3) DNA synthesis by a nucleotidyltransferase, 4) removal of the 5'-dRP group by a'-elimination reaction, and 5) nick sealing by DNA ligase (36, 37)

External links

Nucleotidyltransferases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This

EC 2.7 enzyme-related article is a stub. You can help Wikipedia by expanding it.

[:0-1] Voet D, Voet JG, Pratt CW (2008). Fundamentals of Biochemistry (3rd ed.). John Wiley & Sons, pp. 767

[2] Yuan Liu; Rajendra Prasad; William A. Beard; Padmini S. Kedar; Esther W. Hou; David D. Shock; Samuel H. Wilson (May 4, 2007). "Coordination of Steps in Single-nucleotide Base Excision Repair Mediated by Apurinic/Apyrimidinic Endonuclease 1 and DNA Polymerase β". Journal of Biological Chemistry. 282 (18): 13532–13541.
PMID 17355977
. The enzymes and accessory factors involved in the BER subpathways in mammalian cells have received considerable attention. As summarized above, five distinct enzymatic reaction are involved during SN-BER. These are 1) removal of a modified base by a lesion-specific monofunctional DNA N-glycosylase, 2) 5'-incision of the abasic site by a hydrolytic strand incision enzyme, 3) DNA synthesis by a nucleotidyltransferase, 4) removal of the 5'-dRP group by a'-elimination reaction, and 5) nick sealing by DNA ligase (36, 37)

[1]

[2]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)