Literature summary extracted from

Swift, R.V.; Ong, C.D.; Amaro, R.E.
Magnesium-induced nucleophile activation in the guanylyltransferase mRNA capping enzyme (2012), Biochemistry, 51, 10236-10243.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.7.7.50	empirical and thermodynamic integration pKa estimates, along with conventional molecular dynamics simulations based on PDB entries 1ckm and 1ckn. Magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation	Paramecium bursaria Chlorella virus 1

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
2.7.7.50	Mg2+	magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation	Paramecium bursaria Chlorella virus 1

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.7.50	Paramecium bursaria Chlorella virus 1	Q84424	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.7.7.50	GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA	magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation	Paramecium bursaria Chlorella virus 1	a

Synonyms

EC Number	Synonyms	Comment	Organism
2.7.7.50	guanylyltransferase mRNA capping	-	Paramecium bursaria Chlorella virus 1

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Release 2023.1 (January 2023)