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Visualizing the reaction coordinate of an O-GlcNAc hydrolase.

He Y, Macauley MS, Stubbs KA, Vocadlo DJ, Davies GJ
J Am Chem Soc 132 1807-9 (2010)
Related entries: 2wzi, 2x0h

Cited: 44 times
EuropePMC logo PMID: 20067256

Abstract

N-Acetylglucosamine beta-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcNAc) has been linked to neurodegeneration, cellular stress response, and transcriptional regulation. Removal of O-GlcNAc is catalyzed by O-GlcNAcase (OGA) using a substrate-assisted catalytic mechanism. Here we define the reaction coordinate using chemical approaches and directly observe both a Michaelis complex and the oxazoline intermediate.

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  1. O-GlcNAc signalling: implications for cancer cell biology. Slawson C, Hart GW. Nat Rev Cancer 11 678-684 (2011)
  2. The chitinolytic machinery of Serratia marcescens--a model system for enzymatic degradation of recalcitrant polysaccharides. Vaaje-Kolstad G, Horn SJ, Sørlie M, Eijsink VG. FEBS J 280 3028-3049 (2013)
  3. O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation. Vocadlo DJ. Curr Opin Chem Biol 16 488-497 (2012)
  4. Sirtuins: NAD(+)-dependent deacetylase mechanism and regulation. Sauve AA, Youn DY. Curr Opin Chem Biol 16 535-543 (2012)
  5. Glycoside hydrolases: catalytic base/nucleophile diversity. Vuong TV, Wilson DB. Biotechnol Bioeng 107 195-205 (2010)
  6. Chemical approaches to study O-GlcNAcylation. Banerjee PS, Hart GW, Cho JW. Chem Soc Rev 42 4345-4357 (2013)
  7. O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling? Alonso J, Schimpl M, van Aalten DM. J Biol Chem 289 34433-34439 (2014)
  8. Deciphering the Functions of Protein O-GlcNAcylation with Chemistry. Worth M, Li H, Jiang J. ACS Chem Biol 12 326-335 (2017)
  9. Computational enzymatic catalysis--clarifying enzymatic mechanisms with the help of computers. Sousa SF, Fernandes PA, Ramos MJ. Phys Chem Chem Phys 14 12431-12441 (2012)
  10. Chemical tools to explore nutrient-driven O-GlcNAc cycling. Kim EJ, Bond MR, Love DC, Hanover JA. Crit Rev Biochem Mol Biol 49 327-342 (2014)
  11. Development of inhibitors as research tools for carbohydrate-processing enzymes. Gloster TM. Biochem Soc Trans 40 913-928 (2012)
  12. Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases. Coines J, Cuxart I, Teze D, Rovira C. J Phys Chem B 126 802-812 (2022)
  13. In Vitro Biochemical Assays for O-GlcNAc-Processing Enzymes. Kim EJ. Chembiochem 18 1462-1472 (2017)

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  2. Nutrient-driven O-GlcNAc cycling - think globally but act locally. Harwood KR, Hanover JA. J Cell Sci 127 1857-1867 (2014)
  3. Structural and functional insight into human O-GlcNAcase. Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ. Nat Chem Biol 13 610-612 (2017)
  4. Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. Li B, Li H, Lu L, Jiang J. Nat Struct Mol Biol 24 362-369 (2017)
  5. Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase. Li B, Li H, Hu CW, Jiang J. Nat Commun 8 666 (2017)
  6. Structure of a complete four-domain chitinase from Moritella marina, a marine psychrophilic bacterium. Malecki PH, Malecki PH, Raczynska JE, Vorgias CE, Rypniewski W. Acta Crystallogr D Biol Crystallogr 69 821-829 (2013)
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  17. OGA inhibition by GlcNAc-selenazoline. Kim EJ, Love DC, Darout E, Abdo M, Rempel B, Withers SG, Rablen PR, Hanover JA, Knapp S. Bioorg Med Chem 18 7058-7064 (2010)
  18. Oxazoline or Oxazolinium Ion? The Protonation State and Conformation of the Reaction Intermediate of Chitinase Enzymes Revisited. Coines J, Alfonso-Prieto M, Biarnés X, Planas A, Rovira C. Chemistry 24 19258-19265 (2018)
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  30. Human O-GlcNAcase Uses a Preactivated Boat-skew Substrate Conformation for Catalysis. Evidence from X-ray Crystallography and QM/MM Metadynamics. Calvelo M, Males A, Alteen MG, Willems LI, Vocadlo DJ, Davies GJ, Rovira C. ACS Catal 13 13672-13678 (2023)
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