Literature summary extracted from

Barabas, O.; Nemeth, V.; Bodor, A.; Perczel, A.; Rosta, E.; Kele, Z.; Zagyva, I.; Szabadka, Z.; Grolmusz, V.I.; Wilmanns, M.; Vertessy, B.G.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling (2013), Nucleic Acids Res., 41, 10542-10555.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
3.6.1.23	-	Mason-Pfizer monkey virus

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.6.1.23	in complex with nucleotides. Reaction starts with dUTPase capturing and properly positioning two substrates: dUTP and the catalytic water molecule. the catalytic water molecule is placed near the alpha-phosphate group opposite from the leaving group. Hydrolysis is then initiated by nucleophilic attack of Wthe water on the alpha-phosphate along the line of the scissile bond (in-line attack). A symmetric phosphorane-like transition state structure is formed with significant bond order in both forming and breaking bonds. Bond breaking is concomitant with inversion of the alpha-phosphate configuration and diphosphate-Mg2+ escape. The dUMP product then relaxes by rotation of the alpha-phosphate group and establishes a configuration similar to the one observed for this moiety in the E-S complex	Mason-Pfizer monkey virus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.6.1.23	Mason-Pfizer monkey virus	O92810	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.6.1.23	alpha,beta-imido-dUTP + H2O	-	Mason-Pfizer monkey virus	dUMP + amino-diphosphate	-	?
3.6.1.23	dUTP + H2O	-	Mason-Pfizer monkey virus	dUMP + diphosphate	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.6.1.23	Pr95	-	Mason-Pfizer monkey virus

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Release 2023.1 (January 2023)