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Publication : Location and characterization of the O-GlcNAcase active site.

First Author  Toleman C Year  2006
Journal  Biochim Biophys Acta Volume  1760
Issue  5 Pages  829-39
PubMed ID  16517082 Mgi Jnum  J:112861
Mgi Id  MGI:3663844 Doi  10.1016/j.bbagen.2006.01.017
Citation  Toleman C, et al. (2006) Location and characterization of the O-GlcNAcase active site. Biochim Biophys Acta 1760(5):829-39
abstractText  NCOAT is a bifunctional nucleo-cytoplasmic protein with both O-GlcNAcase and histone acetyltransferase domains. The O-GlcNAcase domain catalyzes the removal of O-linked GlcNAc modifications from proteins and we have found that it resides in the N-terminal third of NCOAT. The recognition of the substrate GlcNAc suggests that the O-GlcNAcase is related in structure and catalytic mechanism to chitinases, hexosaminidases and hyaluronidases. These families of glycosidases all possess a catalytic doublet of carboxylate-containing residues, with one providing an acid-base function, and the second acting to orient and use the N-acetyl group of GlcNAc during catalysis. Indeed, we show that the O-GlcNAcase also possesses the catalytic doublet motif shared among these enzymes and that these two essential residues are aspartic acids at positions 175 and 177, respectively, in mouse NCOAT. In addition, a conserved cysteine at 166 and a conserved aspartic acid at 174 were also found to be necessary for fully efficient enzymatic activity. Given this information, we propose that the O-GlcNAcase active site resembles those of the above glycosidases which carry out the hydrolysis of GlcNAc linkages in a substrate-assisted acid-base manner.
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