CATH Classification

Domain Context

CATH Clusters

Superfamily Hyaluronidase post-catalytic domain-like
Functional Family

Enzyme Information

3.2.1.169
Protein O-GlcNAcase.
based on mapping to UniProt Q89ZI2
(1) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine. (2) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-glucosamine.
-!- 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. -!- EC 2.4.1.155 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.

UniProtKB Entries (1)

Q89ZI2
OGA_BACTN
Bacteroides thetaiotaomicron VPI-5482
O-GlcNAcase BT_4395

PDB Structure

PDB 2J4G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Analysis of Pugnac and Nag-Thiazoline as Transition State Analogues for Human O-Glcnacase: Mechanistic and Structural Insights Into Inhibitor Selectivity and Transition State Poise.
Whitworth, G.E., Macauley, M.S., Stubbs, K.A., Dennis, R.J., Taylor, E.J., Davies, G.J., Greig, I.R., Vocadlo, D.J.
J.Am.Chem.Soc.