NudT16: Difference between revisions

No edit summary
No edit summary
Line 2: Line 2:
__TOC__
__TOC__
==Introduction==
==Introduction==
'''NudT16''' is a member of the Nudix superfamily of hydrolases which breaks a phosphorus-oxygen bond between the two phosphates in nucleoside diphosphate-linked to moiety X molecules resulting in a nucleoside monophosphate (NMP) and a phosphate linked to moiety X. While NudT16 was initially described as a nuclear RNA and cytoplasmic mRNA decapping enzyme, further studies have shown that it also effectively hydrolyzes inosine diphosphate (IDP) and its hazardous deoxyribose cognate (dIDP) into inosine monophosphate (IMP) and deoxy inosine monophosphate (dIMP), respectively <ref>PMID: 26121039</ref>. NudT16 has also been shown to regulate levels of 53BP1, an adaptor protein that recruits other proteins to the site of a DNA breakage, through hydrolytic removal of ADP-ribose (ADPr) from Poly-ADP-ribosylated 53BP1 <ref>PMID: 31911551</ref>.   
'''NudT16''' is a member of the Nudix superfamily of hydrolases which breaks a phosphorus-oxygen bond between the two phosphates in nucleoside diphosphate-linked to moiety X molecules resulting in a nucleoside monophosphate (NMP) and a phosphate linked to moiety X. While NudT16 was initially described as a nuclear [[RNA]] and cytoplasmic mRNA decapping enzyme, further studies have shown that it also effectively hydrolyzes inosine diphosphate (IDP) and its hazardous deoxyribose cognate (dIDP) into inosine monophosphate (IMP) and deoxy inosine monophosphate (dIMP), respectively <ref>PMID: 26121039</ref>. NudT16 has also been shown to regulate levels of 53BP1, an adaptor protein that recruits other proteins to the site of a DNA breakage, through hydrolytic removal of ADP-ribose (ADPr) from Poly-ADP-ribosylated 53BP1 <ref>PMID: 31911551</ref>.   


==Structure==  
==Structure==  

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Tihitina Y Aytenfisu, Hannah Campbell, Sandra B. Gabelli, Michal Harel