ExplorEnz: EC 3.1.1.106

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3.1.1.106

Accepted name:

O-acetyl-ADP-ribose deacetylase

Reaction:

(1) 3′′-O-acetyl-ADP-D-ribose + H₂O = ADP-D-ribose + acetate
(2) 2′′-O-acetyl-ADP-D-ribose + H₂O = ADP-D-ribose + acetate

Other name(s):

ymdB (gene name); MACROD1 (gene name)

Systematic name:

O-acetyl-ADP-D-ribose carboxylesterase

Comments:

The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2′′ or 3′′ position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286, protein acetyllysine N-acetyltransferase. The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Chen, D., Vollmar, M., Rossi, M.N., Phillips, C., Kraehenbuehl, R., Slade, D., Mehrotra, P.V., von Delft, F., Crosthwaite, S.K., Gileadi, O., Denu, J.M. and Ahel, I. Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J. Biol. Chem. 286 (2011) 13261–13271. [PMID: 21257746]
2.	Zhang, W., Wang, C., Song, Y., Shao, C., Zhang, X. and Zang, J. Structural insights into the mechanism of Escherichia coli YmdB: A 2′-O-acetyl-ADP-ribose deacetylase. J. Struct. Biol. 192 (2015) 478–486. [PMID: 26481419]
3.	Agnew, T., Munnur, D., Crawford, K., Palazzo, L., Mikoc, A. and Ahel, I. MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria. Front. Microbiol. 9:20 (2018). [PMID: 29410655]

[EC 3.1.1.106 created 2019]