Proteinska O-GlcNAkaza
Proteinska O-GlcNAkaza (EC 3.2.1.169, OGA, glikozidna hidrolaza O-GlcNAkaza, O-GlcNAkaza, BtGH84, O-GlcNAc hidrolaza) je enzim sa sistematskim imenom (protein)-3-O-(N-acetil-D-glukozaminil)-L-serin/treonin N-acetilglukozaminil hidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Proteinska O-GlcNAkaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.169 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (1) [protein]-3-O-(N-acetil-beta-D-glukozaminil)-L-serin + H2O [protein]-L-serin + N-acetil-D-glukozamin
- (2) [protein]-3-O-(N-acetil-beta-D-glukozaminil)-L-treonin + H2O [protein]-L-treonin + N-acetil-D-glukozamin
Kod viših eukariota posttranslaciona modifikacija proteinskih serina/treonina sa N-acetilglukozaminom (O-GlcNAc) je dinamička, induktivna i izobilna. Njome se regulišu mnogi ćelijski procesi putem ometanja proteinske fosforilacije.
Reference uredi
- ↑ Gao, Y., Wells, L., Comer, F.I., Parker, G.J. and Hart, G.W. (2001). „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. PMID 11148210.
- ↑ Wells, L., Gao, Y., Mahoney, J.A., Vosseller, K., Chen, C., Rosen, A. and Hart, G.W. (2002). „Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase”. J. Biol. Chem. 277: 1755-1761. PMID 11788610.
- ↑ Cetinbas, N., Macauley, M.S., Stubbs, K.A., Drapala, R. and Vocadlo, D.J. (2006). „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. PMID 16533067.
- ↑ Dennis, R.J., Taylor, E.J., Macauley, M.S., Stubbs, K.A., Turkenburg, J.P., Hart, S.J., Black, G.N., Vocadlo, D.J. and Davies, G.J. (2006). „Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity”. Nat. Struct. Mol. Biol. 13: 365-371. PMID 16565725.
- ↑ Kim, E.J., Kang, D.O., Love, D.C. and Hanover, J.A. (2006). „Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate”. Carbohydr. Res. 341: 971-982. PMID 16584714.
- ↑ Dong, D.L. and Hart, G.W. (1994). „Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol”. J. Biol. Chem. 269: 19321-19330. PMID 8034696.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.