O-GlcNAc - definição. O que é O-GlcNAc. Significado, conceito
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  3. O-GlcNAc

O que (quem) é O-GlcNAc - definição


O-GlcNAc         
  • Chemoenzymatic labeling for the detection of ''O''-GlcNAc. GalT Y289L transfers GalNAz to ''O''-GlcNAc, providing a handle for click chemistry. Various probes can be conjugated via azide-alkyne cycloaddition. Attachment of a PEG5K mass tag allows for visualization of ''O''-GlcNAc stoichiometry.
  • FRET biosensor for ''O''-GlcNAc. Under high ''O''-GlcNAc conditions, GafD will bind the ''O''-GlcNAc group on the CKII peptide substrate, bringing CFP and YFP into proximity for FRET. Various localization sequences can be fused to localize the sensor to various cellular compartments, e.g., nucleus, cytoplasm, and plasma membrane.
  • Structure of IsoTaG probe. Probe consists of a biotin affinity tag (red), a linker (black), an acid-cleavable silane (blue), an isotope recoding motif (green), and an alkyne (purple).
  • Site-directed mutagenesis for manipulating ''O''-GlcNAc. S/T-to-A mutagenesis prevents ''O''-GlcNAc modification at that residue. S/T-to-C mutagenesis allows for generation of the ''S''-GlcNAc modification, a structural analogue of ''O''-GlcNAc that is not readily hydrolyzed by OGA.
  • ''O''-GlcNAcylation of serine and threonine residues is dynamically controlled by OGT and OGA.
  • GalT radiolabeling of cellular proteins with UDP-[<sup>3</sup>H]galactose followed by β-elimination yielded Galβ1-4GlcNAcitol, suggesting that the substrate for GalT was ''O''-GlcNAc. Radiolabeled [<sup>3</sup>H]galactose shown in red.
  • ''Left'': Model of full-length ncOGT in complex with CKII peptide substrate and UDP.<ref name=":5" /> Colors indicate TPR domain (gray), N-terminal region of catalytic domain (light pink), intervening domain (light green), C-terminal region of catalytic domain (light blue), CKII peptide substrate (green), and UDP (cyan). ''Right'': Structure of human OGA D175N dimer in complex with ''O''-GlcNAcylated TAB1 peptide substrate. Monomers shown in blue-white/light yellow with respective peptide substrates in blue/yellow. (PDB: 5VVU)
  • PDB]]: 4GYW)
  • doi-access=free}}</ref>
THE GLYCOSYLATION OF A PROTEIN BY ADDITION OF N-ACETYLGLUCOSAMINE VIA THE O3 ATOM OF PEPTIDYL-THREONINE, FORMING O3-N-ACETYLGLUCOSAMINE-L-THREONINE.
O-linked β-N-acetylglucosamine (O-GlcNAc); O-glcnac; O-linked beta-N-acetylglucosamine; O-Linked β-N-acetylglucosamine; O-GlcNAcylation; O GlcNAc; Oglcnac; O-linked glcnac
O-GlcNAc (short for O-linked GlcNAc or O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc).
https://en.wikipedia.org/wiki/O-GlcNAc
Protein O-GlcNAc transferase         
  • Figure 3: Dynamic Competition between glycosylation and phosphorylation of proteins. A: Competition between OGT and kinase for the serine or threonine functional group of a protein. B: Adjacent-site occupancy where ''O''-GlcNAc and ''O''-phosphatase occur next to each other and can influence the turnover or function of proteins reciprocally. The G circle represents an ''N''-acetylglucosamine group, and the P circle represents a phosphate group. Figure adapted from Hart.<ref name=pmid17460662 />
  • <small style="font-size:85%;">[http://micro.med.harvard.edu/faculty/walker.html Suzanne Walker] describes [https://www.youtube.com/watch?v=Y-m6QlIhZ5kt=1m53s The split personality of human ''O''-GlcNAc transferase] during a seminar at the US NIH, April 18, 2017</small>
  • Figure 2: The proposed catalytic mechanism of ''O''-GlcNAc transferase. It is an ordered sequential bi-bi mechanism with only one step, not including a proton transfer. The peptide is represented by a serine residue with a reactive hydroxyl group.<ref name=Lazarus />
PROTEIN-CODING GENE IN THE SPECIES HOMO SAPIENS
OGT (gene); EC 2.4.1.255; O-GlcNAc transferase; OGTase; O-linked N-acetylglucosaminyltransferase; Protein O-linked beta-N-acetylglucosamine transferase; UDP-N-acetyl-D-glucosamine:protein-O-beta-N-acetyl-D-glucosaminyl transferase
Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme () that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.
https://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase
Ó         
LETTER OF THE LATIN ALPHABET
O acute; O accent; Oacute; O with acute; O-acute; Ṓ; Ṍ; U+00D3
Ó, ó (o-acute) is a letter in the Czech, Emilian-Romagnol, Faroese, Hungarian, Icelandic, Kashubian, Kazakh, Polish, Slovak, and Sorbian languages. This letter also appears in the Afrikaans, Catalan, Dutch, Irish, Nynorsk, Bokmål, Occitan, Portuguese, Spanish, Italian and Galician languages as a variant of letter "o".
https://en.wikipedia.org/wiki/Ó
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