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Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Additionally we are shipping RNA Guanylyltransferase and 5'-Phosphatase Proteins (5) and and many more products for this protein.
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These results identify a new domain of CE that is specific to its function in cytoplasmic capping, and a new role for Nck1 (show NCK1 Antibodies) in regulating gene expression through its role as the scaffold for assembly of the cytoplasmic capping complex.
Our biochemical studies provide the first insight that MZP can inhibit the formation of the RNA cap structure catalyzed by HCE.
Data show that human capping enzyme residues 229-567 comprise the minimum enzymatically active human GTase (hGTase) domain and determine the structure by X-ray crystallography.
Overall, both in vivo and in vitro studies indicate that the functional domain of Mce1 is between a.a. 211 and 567, and the heptapeptide sequence between 561 and 567 may play an important role in the enzyme activity.
Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.
mRNA capping enzyme
, RNA guanylyltransferase and 5'-phosphatase
, mRNA-capping enzyme
, mRNA-capping enzyme-like
, capping enzyme
, RNA guanylyltransferase and 5-phosphatase