Literature summary for 2.1.1.56 extracted from

Bueren-Calabuig, J.A.; G Bage, M.; Cowling, V.H.; Pisliakov, A.V.
Mechanism of allosteric activation of human mRNA cap methyltransferase (RNMT) by RAM insights from accelerated molecular dynamics simulations (2019), Nucleic Acids Res., 47, 8675-8692 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
RNMT-activating miniprotein	RNMT-activating miniprotein stabilizes the enzyme and enhances the active site conformations promoting the substrates binding	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]	Homo sapiens	-	S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O43148	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]	-	Homo sapiens	S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]	-	?

Synonyms

Synonyms	Comment	Organism
mRNA cap methyltransferase	-	Homo sapiens
RNA guanine-N7 methyltransferase	-	Homo sapiens
RNMT	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme in complex with RNMT-activating miniprotein catalyzes the formation of a N7-methylated guanosine cap structure on the 5' end of nascent RNA polymerase II transcripts. The mRNA cap protects the primary transcript from exonucleases and recruits cap binding complexes that mediate RNA processing, export and translation	Homo sapiens

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Release 2023.1 (January 2023)