ExplorEnz: EC 1.14.11.53

Your query returned 1 entry. Printable version

1.14.11.53

Accepted name:

mRNA N⁶-methyladenine demethylase

Reaction:

N⁶-methyladenine in mRNA + 2-oxoglutarate + O₂ = adenine in mRNA + formaldehyde + succinate + CO₂

Other name(s):

ALKBH5; FTO

Systematic name:

mRNA-N⁶-methyladenosine,2-oxoglutarate:oxygen oxidoreductase (formaldehyde-forming)

Comments:

Contains iron(II). Catalyses oxidative demethylation of mRNA N⁶-methyladenine. The FTO enzyme from human can also demethylate N³-methylthymine from single stranded DNA and N³-methyluridine from single stranded RNA [1,2] with low activity [3].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Jia, G., Yang, C.G., Yang, S., Jian, X., Yi, C., Zhou, Z. and He, C. Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO. FEBS Lett. 582 (2008) 3313–3319. [DOI] [PMID: 18775698]
2.	Han, Z., Niu, T., Chang, J., Lei, X., Zhao, M., Wang, Q., Cheng, W., Wang, J., Feng, Y. and Chai, J. Crystal structure of the FTO protein reveals basis for its substrate specificity. Nature 464 (2010) 1205–1209. [DOI] [PMID: 20376003]
3.	Jia, G., Fu, Y., Zhao, X., Dai, Q., Zheng, G., Yang, Y., Yi, C., Lindahl, T., Pan, T., Yang, Y.G. and He, C. N⁶-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO. Nat. Chem. Biol. 7 (2011) 885–887. [DOI] [PMID: 22002720]
4.	Zheng, G., Dahl, J.A., Niu, Y., Fedorcsak, P., Huang, C.M., Li, C.J., Vagbo, C.B., Shi, Y., Wang, W.L., Song, S.H., Lu, Z., Bosmans, R.P., Dai, Q., Hao, Y.J., Yang, X., Zhao, W.M., Tong, W.M., Wang, X.J., Bogdan, F., Furu, K., Fu, Y., Jia, G., Zhao, X., Liu, J., Krokan, H.E., Klungland, A., Yang, Y.G. and He, C. ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility. Mol. Cell 49 (2013) 18–29. [DOI] [PMID: 23177736]
5.	Feng, C., Liu, Y., Wang, G., Deng, Z., Zhang, Q., Wu, W., Tong, Y., Cheng, C. and Chen, Z. Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition. J. Biol. Chem. 289 (2014) 11571–11583. [DOI] [PMID: 24616105]
6.	Xu, C., Liu, K., Tempel, W., Demetriades, M., Aik, W., Schofield, C.J. and Min, J. Structures of human ALKBH5 demethylase reveal a unique binding mode for specific single-stranded N⁶-methyladenosine RNA demethylation. J. Biol. Chem. 289 (2014) 17299–17311. [DOI] [PMID: 24778178]
7.	Aik, W., Scotti, J.S., Choi, H., Gong, L., Demetriades, M., Schofield, C.J. and McDonough, M.A. Structure of human RNA N⁶-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation. Nucleic Acids Res. 42 (2014) 4741–4754. [DOI] [PMID: 24489119]

[EC 1.14.11.53 created 2016]