OENC42113 Catalytic biopart Map View
experimental evidence
Chassis
Catalytic functions

1) 3-O-(N-acetyl-β-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine

3-O-(N-acetyl-β-D-glucosaminyl)-L-seryl-[protein]
GENERIC: 12251
+
H2O
CHEBI: 15377
Formula: H2O
=
L-seryl-[protein]
GENERIC : 9863
+
N-acetyl-D-glucosamine
CHEBI : 506227
Formula: C8H15NO6
External Links
EC number

Bioparts catalyze this reaction

Biopart ID Organisms pH temperature(ºC) km

2) 3-O-(N-acetyl-β-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine

3-O-(N-acetyl-β-D-glucosaminyl)-L-threonyl-[protein]
GENERIC: 12252
+
H2O
CHEBI: 15377
Formula: H2O
=
L-threonyl-[protein]
GENERIC : 11060
+
N-acetyl-D-glucosamine
CHEBI : 506227
Formula: C8H15NO6
External Links
EC number

Bioparts catalyze this reaction

Biopart ID Organisms pH temperature(ºC) km
Qualitative and quantitative parameters:
Organism

Taxonomy

Lineage
cellular organisms; Bacteria; Terrabacteria group; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium perfringens;
Sequence and structure

Protein sequence

Xref

Sequence

TESTMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSAR静态页面数据

Protein family

Protein structure

Nucleotide sequences (Optimized nucleotide sequences according to different chassises)

NT seq ID
Gene name

Sequence

ASGSDGLJSLKJGOJSIDJIOJG静态数据
References
  1. D L Dong; G W Hart; . 1994: Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. The Journal of Biological Chemistry, 269 19321-30.
  2. Matthew S Macauley; Garrett E Whitworth; Aleksandra W Debowski; Danielle Chin; David J Vocadlo; . 2005: O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. The Journal of Biological Chemistry, 280 25313-22.
  3. Keith A Stubbs; Nelson Zhang; David J Vocadlo; . 2006: A divergent synthesis of 2-acyl derivatives of PUGNAc yields selective inhibitors of O-GlcNAcase. Organic & biomolecular chemistry, 4 839-45.
  4. Francesco V Rao; Helge C Dorfmueller; Fabrizio Villa; Matthew Allwood; Ian M Eggleston; Daan M F van Aalten; . 2006: Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. The EMBO journal, 25 1569-78.
  5. Rebecca J Dennis; Edward J Taylor; Matthew S Macauley; Keith A Stubbs; Johan P Turkenburg; Samuel J Hart; Gary N Black; David J Vocadlo; Gideon J Davies; . 2006: Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity. Nature structural & molecular biology, 13 365-71.
  6. Eun Ju Kim; Dae Ook Kang; Dona C Love; John A Hanover; . 2006: Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate. Carbohydrate research, 341 971-82.
  7. Garry S A Myers; David A Rasko; Jackie K Cheung; Jacques Ravel; Rekha Seshadri; Robert T DeBoy; Qinghu Ren; John Varga; Milena M Awad; Lauren M Brinkac; Sean C Daugherty; Daniel H Haft; Robert J Dodson; Ramana Madupu; William C Nelson; M J Rosovitz; Steven A Sullivan; Hoda Khouri; George I Dimitrov; Kisha L Watkins; Stephanie Mulligan; Jonathan Benton; Diana Radune; Derek J Fisher; Helen S Atkins; Tom Hiscox; B Helen Jost; Stephen J Billington; J Glenn Songer; Bruce A McClane; Richard W Titball; Julian I Rood; Stephen B Melville; Ian T Paulsen; . 2006: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome research, 16 1031-40.
  8. Thomas N Lee; William E Alborn; Michael D Knierman; Robert J Konrad; . 2006: The diabetogenic antibiotic streptozotocin modifies the tryptic digest pattern for peptides of the enzyme O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase that contain amino acid residues essential for enzymatic activity. Biochemical Pharmacology, 72 710-8.
  9. Elizabeth Ficko-Blean; Alisdair B Boraston; . 2006: The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor. The Journal of Biological Chemistry, 281 37748-57.
  10. Shalini Pathak; Helge C Dorfmueller; Vladimir S Borodkin; Daan M F van Aalten; . 2008: Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death. Chemistry & Biology, 15 799-807.
  11. Gladys A Ngoh; Heberty T Facundo; Tariq Hamid; Wolfgang Dillmann; Natasha E Zachara; Steven P Jones; . 2009: Unique hexosaminidase reduces metabolic survival signal and sensitizes cardiac myocytes to hypoxia/reoxygenation injury. Circulation research, 104 41-9.
  12. Elizabeth Ficko-Blean; Katie J Gregg; Jarrett J Adams; Jan-Hendrik Hehemann; Mirjam Czjzek; Steven P Smith; Alisdair B Boraston; . 2009: Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens. The Journal of Biological Chemistry, 284 9876-84.
  13. Yuan He; Carlos Martinez-Fleites; Abigail Bubb; Tracey M Gloster; Gideon J Davies; . 2009: Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase. Carbohydrate research, 344 627-31.
  14. Helge C Dorfmueller; Vladimir S Borodkin; Marianne Schimpl; Daan M F van Aalten; . 2009: GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation. Biochemical Journal, 420 221-7.
  15. Matthew S Macauley; David J Vocadlo; . 2010: Increasing O-GlcNAc levels: An overview of small-molecule inhibitors of O-GlcNAcase. Biochimica et biophysica acta, 1800 107-21.
  16. Marianne Schimpl; Vladimir S Borodkin; Lindsey J Gray; Daan M F van Aalten; . 2012: Synergy of peptide and sugar in O-GlcNAcase substrate recognition. Chemistry & Biology, 19 173-8.
  17. Daniel Mariappa; Nithya Selvan; Vladimir S Borodkin; Jana Alonso; Andrew T Ferenbach; Claire Shepherd; Iva Hopkins Navratilova; Daan M F van Aalten; . 2015: A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development. Biochemical Journal, 470 255-62.
  18. Nathaniel L Elsen; Sangita B Patel; Rachael E Ford; Dawn L Hall; Fred Hess; Hari Kandula; Maria Kornienko; John Reid; Harold Selnick; Jennifer M Shipman; Sujata Sharma; Kevin J Lumb; Stephen M Soisson; Daniel J Klein; . 2017: Insights into activity and inhibition from the crystal structure of human O-GlcNAcase. Nature chemical biology, .
  19. Nithya Selvan; Ritchie Williamson; Daniel Mariappa; David G Campbell; Robert Gourlay; Andrew T Ferenbach; Tonia Aristotelous; Iva Hopkins-Navratilova; Matthias Trost; Daan M F van Aalten; . 2017: A mutant O-GlcNAcase enriches Drosophila developmental regulators. Nature chemical biology, .
Brenda
Uniprot
Rhea
Enzyme