Nudix hydrolase
{{Short description|Superfamily of hydrolytic enzymes}}
{{Infobox protein family
| Symbol = NUDIX
| Name = NUDIX
| image = PDB 1mp2 EBI.jpg
| width =
| caption = Structure of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis
| Pfam = PF00293
| Pfam_clan = CL0261
| ECOD = 221.4.1
| InterPro = IPR000086
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = NUDIX-like
| Name = NUDIX-like
| image = PDB 1vk6 EBI.jpg
| width =
| caption = Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 a resolution
| Pfam = PF09296
| Pfam_clan = CL0261
| InterPro = IPR015375
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1vk6
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
NUDIX hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x (any moiety), hence their name.{{cite journal |vauthors=Bessman MJ, Frick DN, O'Handley SF |title=The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes |journal=J. Biol. Chem. |volume=271 |issue=41 |pages=25059–62 |date=October 1996 |pmid=8810257 |doi= 10.1074/jbc.271.41.25059|doi-access= free}}{{cite journal |vauthors=Mildvan AS, Xia Z, Azurmendi HF, etal |title=Structures and mechanisms of Nudix hydrolases |journal=Arch. Biochem. Biophys. |volume=433 |issue=1 |pages=129–43 |date=January 2005 |pmid=15581572 |doi=10.1016/j.abb.2004.08.017 }}{{cite journal |author=McLennan AG |title=The Nudix hydrolase superfamily |journal=Cell. Mol. Life Sci. |volume=63 |issue=2 |pages=123–43 |date=January 2006 |pmid=16378245 |doi=10.1007/s00018-005-5386-7 |s2cid=30202446 |doi-access=free |pmc=11136074 }}{{Cite journal|last1=Carreras-Puigvert|first1=Jordi|last2=Zitnik|first2=Marinka|last3=Jemth|first3=Ann-Sofie|last4=Carter|first4=Megan|last5=Unterlass|first5=Judith E.|last6=Hallström|first6=Björn|last7=Loseva|first7=Olga|last8=Karem|first8=Zhir|last9=Calderón-Montaño|first9=José Manuel|last10=Lindskog|first10=Cecilia|last11=Edqvist|first11=Per-Henrik|date=2017-11-16|title=A comprehensive structural, biochemical and biological profiling of the human NUDIX hydrolase family|journal=Nature Communications|volume=8|issue=1|pages=1541|doi=10.1038/s41467-017-01642-w|issn=2041-1723|pmc=5688067|pmid=29142246|bibcode=2017NatCo...8.1541C }} The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the NUDIX superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.
There are two components to the NUDIX family: the so-called NUDIX fold of a beta sheet with alpha helices on each side and the NUDIX motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is isoleucine, leucine or valine, and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids. NUDIX hydrolases include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A hydrolases, RppH, and many others.{{Cite journal | last1 = Mildvan | first1 = A.S. | last2 = Xia | first2 = Z. | last3 = Azurmendi | first3 = H.F. | last4 = Saraswat | first4 = V. | last5 = Legler | first5 = P.M. | last6 = Massiah | first6 = M.A. | last7 = Gabelli | first7 = S.B. | last8 = Bianchet | first8 = M.A. | last9 = Kang | first9 = L.W. | last10 = Amzel | first10 = L.M. | year = 2005 | title = Structures and mechanisms of Nudix hydrolases | journal = Archives of Biochemistry and Biophysics | pmid = 15581572 | volume = 433 | issue = 1 | pages = 129–143 | doi = 10.1016/j.abb.2004.08.017 | display-authors = 8 }}