Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.50 extracted from

  • Bharati, A.P.; Singh, N.; Kumar, V.; Kashif, M.; Singh, A.K.; Singh, P.; Singh, S.K.; Siddiqi, M.I.; Tripathi, T.; Akhtar, M.S.
    The mRNA capping enzyme of Saccharomyces cerevisiae has dual specificity to interact with CTD of RNA Polymerase II (2016), Sci. Rep., 6, 31294.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.50

Protein Variants

Protein Variants Comment Organism
K175A no loss of interaction with polymerase II C-terminal domain Saccharomyces cerevisiae
K198A no loss of interaction with polymerase II C-terminal domain Saccharomyces cerevisiae
R159A loss of interaction with polymerase II C-terminal domain. Residue Arg159 of Ceg1 interacts strongly with polymerase II C-terminal domain Saccharomyces cerevisiae
R185A loss of interaction with polymerase II C-terminal domain. Residue Arg185 of Ceg1 interacts strongly with polymerase II C-terminal domain Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q01159
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNA guanylyltransferase Ceg1 has dual specificity and interacts not only with Ser5P but also with Ser7P of the C-terminal domain of RNA polymerase II. Ser7 of the C-terminal domain is essential for the unconditional growth and efficient priming of the mRNA capping complex. Residues Arg159 and Arg185 of Ceg1 are the key residues that interact with the Ser5P, while Lys175 interacts with Ser7P of the C-terminal domain. These interactions appear to be in a specific pattern of Ser5PSer7PSer5P in a tri-heptad C-terminal domain (YSPTS(P)-PSYSPTSPS(P)YSPTS(P)PS) Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Ceg1
-
 Saccharomyces cerevisiae