Literature summary for 2.7.7.96 extracted from

Wright, R.; Fernandez-Fuentes, N.; Oliva, B.; Beato, M.
Insight into the machinery that oils chromatin dynamics (2016), Nucleus, 7, 532-539 .

Search for more literature for 2.7.7.96

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of a crystal structure of human NUDIX5/NUDT5 homodimer bound with one ADPR on each of the 2 active sites	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
nucleus	-	Homo sapiens	5634	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + D-ribose 5-phosphate	Homo sapiens	-	diphosphate + ADP-D-ribose	-	r
diphosphate + ADP-D-ribose	Homo sapiens	-	ATP + D-ribose 5-phosphate	-	r
additional information	Homo sapiens	enzyme NUDIX5 catalyzes not only the formation of AMP but also the synthesis of ATP within the cell nucleus	?	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9UKK9	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	phosphorylation of T45 is predicted to prevent the flipping of NUDIX5 monomers, hindering the formation of the hexamer. Thus, dephosphorylation of NUDIX5 may trigger the switch to a conformational change that activates the energy generating molecular machine	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
breast cancer cell	-	Homo sapiens	-
T-47D cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + D-ribose 5-phosphate	-	Homo sapiens	diphosphate + ADP-D-ribose	-	r
diphosphate + ADP-D-ribose	-	Homo sapiens	ATP + D-ribose 5-phosphate	-	r
additional information	enzyme NUDIX5 catalyzes not only the formation of AMP but also the synthesis of ATP within the cell nucleus	Homo sapiens	?	-	-

Subunits

Subunits	Comment	Organism
oligomer	phosphorylation of T45 is predicted to prevent the flipping of NUDIX5 monomers, hindering the formation of the hexamer. Thus, dephosphorylation of NUDIX5 may trigger the switch to a conformational change that activates the energy generating molecular machine. NUDIX5 homodimer exists in equilibrium between the dominant ADPR hydrolysing conformation and a minor ATP synthesising conformation, in which the relative orientation of the monomer flips yielding more open active sites that can accommodate the presence of PPi required for ATP synthesis	Homo sapiens

Synonyms

Synonyms	Comment	Organism
NUDIX5	-	Homo sapiens
NUDT5	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	chromatin remodelling measured by histones H1 and H2A displacement at later stages after PAR accumulation and degradation, is dependent on PARP1, PARG, and NUDIX5	Homo sapiens
additional information	NUDIX5 homodimer exists in equilibrium between the dominant ADPR hydrolysing conformation and a minor ATP synthesising conformation, in which the relative orientation of the monomer flips yielding more open active sites that can accommodate the presence of diphosphate required for ATP synthesis	Homo sapiens
physiological function	in response to hormones, i.e. synthetic promegestone (R5020 or 17alpha,21-dimethyl-19-norpregna-4,9-diene-3,20-dione), a nuclear ATP synthesis mechanism is activated that utilizes ADP-ribose and diphosphate as substrates. Enzyme NUDIX5 utilizes an increase in ADP-D-ribose and diphosphate to generate ATP. ATP produced in the nucleus is used for stable displacement of H1 and H2A/H2B opening the chromatin for access of transcriptional regulators leading to gene activation/repression and ultimately to cell proliferation. NUDIX5 interacts with both poly-ADP-ribose glycohydrolase (PARG) and poly-ADP-ribose (PAR) by co-immunoprecipitation following hormone treatment	Homo sapiens

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Release 2023.1 (January 2023)