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Literature summary for 2.4.1.255 extracted from

  • Lazarus, M.; Nam, Y.; Jiang, J.; Sliz, P.; Walker, S.
    Structure of human O-GlcNAc transferase and its complex with a peptide substrate (2011), Nature, 469, 564-569.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
a binary complex with UDP and a ternary complex with UDP and peptide substrate YPGGSTPVSSANMM, hanging drop vapor diffusion method Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15294
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-GlcNAc + YPGGSTPVSSANMM
-
Homo sapiens UDP + YPGGSTPVS-3-O-(N-acetyl-D-glucosaminyl)-SANMM
-
?

Synonyms

Synonyms Comment Organism
O-GlcNAc transferase
-
Homo sapiens
OGT
-
Homo sapiens

General Information

General Information Comment Organism
physiological function aberrant OGlcNAcylation by the enzyme is linked to insulin resistance, diabetic complications, cancer and neurodegenerative diseases including Alzheimer's disease Homo sapiens