Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.255 extracted from

  • Borodkin, V.S.; Schimpl, M.; Gundogdu, M.; Rafie, K.; Dorfmueller, H.C.; Robinson, D.A.; van Aalten, D.M.
    Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors (2014), Biochem. J., 457, 497-502.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitor goblin1, to 3.15 A resolution. UDP adopts the same conformation as observed in the OGT Michaelis complex and the peptide occupies the -4 to +2 subsites with a similar backbone conformation. The three-carbon linker connects the two components without introducing any strain, allowing both the UDP moiety and the peptide part of the inhibitor to adopt the optimal position in the binding site, mimicking the natural substrates Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
goblin1 bisubstrate-linked inhibitor in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C3 linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15294 UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase 110 kDa subunit
-

Synonyms

Synonyms Comment Organism
OGT
-
Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.008
-
pH 7.5, 22°C Homo sapiens goblin1