OENC42112
Catalytic biopart
Map View
experimental evidence
Name
Chassis
-
Escherichia coli
Catalytic functions
External Links
EC number
-
3.2.1.169 Protein O-GlcNAcase.
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
External Links
EC number
-
3.2.1.169 Protein O-GlcNAcase.
Bioparts catalyze this reaction
| Biopart ID | Organisms | pH | temperature(ºC) | km |
|---|
Qualitative and quantitative parameters:
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Temperature
Temperature optimum(ºC)
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37.0
pH
pH optimum
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6.0
Organism
Taxonomy
Taxonomy ID
Lineage
cellular organisms; Bacteria; FCB group; Bacteroidetes/Chlorobi group; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides thetaiotaomicron;
Sequence and structure
Protein sequence
Protein ID
Xref
Sequence
TESTMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSARQLLARLDARPLAARAAVDVAALVRRAGATLRLRRKEAVSVLDSADIEVTDSRLPHATIVDHRPQHRWLETCNAPPQLIQGKAHSAPKPSQASGKAHSAPKPSQASGAMEPRTGGAANPKGSRGSRGPSPLAGPSAR静态页面数据
Protein family
Protein structure
References
- 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.
- Jian Xu; Magnus K Bjursell; Jason Himrod; Su Deng; Lynn K Carmichael; Herbert C Chiang; Lora V Hooper; Jeffrey I Gordon; . 2003: A genomic view of the human-Bacteroides thetaiotaomicron symbiosis. Science (New York, N.Y.), 299 2074-6.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- Yuan He; Matthew S Macauley; Keith A Stubbs; David J Vocadlo; Gideon J Davies; . 2010: Visualizing the reaction coordinate of an O-GlcNAc hydrolase. Journal of the American Chemical Society, 132 1807-9.
- 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, .
Cross links
Brenda
Uniprot
Enzyme