EC 3.2.1.169 - Protein O-GlcNAcase

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IntEnz Enzyme Nomenclature
EC 3.2.1.169

Names

Accepted name:
protein O-GlcNAcase
Other names:
OGA
glycoside hydrolase O-GlcNAcase
O-GlcNAcase
BtGH84
O-GlcNAc hydrolase
Systematic name:
[protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase

Reactions

Comments:

Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. O-GlcNAc transferase (EC 2.4.1.155) transfers GlcNAc onto substrate proteins and O-GlcNAcase (EC 3.2.1.169) cleaves GlcNAc from the modified proteins.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102167 , GO:0102571 , GO:0102166
UniProtKB/Swiss-Prot:

References

  1. Gao, Y., Wells, L., Comer, F. I., Parker, G. J., Hart, G. W.
    Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain.
    J. Biol. Chem. 276: 9838-9845 (2001). [PMID: 11148210]
  2. Wells, L., Gao, Y., Mahoney, J. A., Vosseller, K., Chen, C., Rosen, A., Hart, G. W.
    Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase.
    J. Biol. Chem. 277: 1755-1761 (2002). [PMID: 11788610]
  3. Cetinbas, N., Macauley, M. S., Stubbs, K. A., Drapala, R., Vocadlo, D. J.
    Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants.
    Biochemistry 45: 3835-3844 (2006). [PMID: 16533067]
  4. Dennis, R. J., Taylor, E. J., Macauley, M. S., Stubbs, K. A., Turkenburg, J. P., Hart, S. J., Black, G. N., Vocadlo, D. J., Davies, G. J.
    Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity.
    Nat. Struct. Mol. Biol. 13: 365-371 (2006). [PMID: 16565725]
  5. Kim, E. J., Kang, D. O., Love, D. C., Hanover, J. A.
    Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate.
    Carbohydr. Res. 341: 971-982 (2006). [PMID: 16584714]
  6. Dong, D. L., Hart, G. W.
    Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol.
    J. Biol. Chem. 269: 19321-19330 (1994). [PMID: 8034696]

[EC 3.2.1.169 created 2011]