| EC |
3.6.1.74 |
| Accepted name: |
mRNA 5′-phosphatase |
| Reaction: |
a 5′-triphospho-[mRNA] + H2O = a 5′-diphospho-[mRNA] + phosphate |
| Other name(s): |
5′-polynucleotidase; polynucleotide 5′-phosphohydrolase; RNGTT (gene name); CET1 (gene name); mRNA 5′-triphosphate monophosphatase |
| Systematic name: |
5′-triphospho-mRNA 5′-phosphohydrolase |
| Comments: |
The enzyme, found in eukaryotes and some plus strand RNA viruses (e.g. alphavirus), is involved in mRNA capping. Unlike the eukaryotic enzyme, the viral enzyme requires a purine in the first position of the mRNA. The human enzyme is a multi domain protein that also has the activity of EC 2.7.7.50, mRNA guanylyltransferase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Itoh, N., Mizumoto, K. and Kaziro, Y. Messenger RNA guanlyltransferase from Saccharomyces cerevisiae. II. Catalytic properties. J. Biol. Chem. 259 (1984) 13930–13936. [PMID: 6094533] |
| 2. |
Tsukamoto, T., Shibagaki, Y., Murakoshi, T., Suzuki, M., Nakamura, A., Gotoh, H. and Mizumoto, K. Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme. Biochem. Biophys. Res. Commun. 243 (1998) 101–108. [DOI] [PMID: 9473487] |
| 3. |
Vasiljeva, L., Merits, A., Auvinen, P. and Kaariainen, L. Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2. J. Biol. Chem. 275 (2000) 17281–17287. [DOI] [PMID: 10748213] |
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| [EC 3.6.1.74 created 2021] |
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