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Proteinska O-GlcNAkaza

Izvor: Wikipedija
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

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

(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

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  1. 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. 
  2. 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. 
  3. 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. 
  4. 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. 
  5. 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. 
  6. 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

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Spoljašnje veze

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