Literature summary for 2.7.7.50 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.

Search for more literature for 2.7.7.50

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Paramecium bursaria Chlorella virus 1	Q84424	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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

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

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Release 2023.1 (January 2023)