Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli, N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D1–352) | Drosophila melanogaster |
Crystallization (Comment) | Organism |
---|---|
N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D1–35), crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc, to 2.7 A resolution. The enzyme adopts the canonical OGT fold with the bilobal arrangement of two Rossmann-like domains, as well as the additional TPR-like helices (535–566) in the N-terminal of the catalytic domain. As a result, the TPRs are in close association with the glycosyltransferase domain and the catalytic site is aligned with the channel along the main axis of the TPR superhelix | Drosophila melanogaster |
Protein Variants | Comment | Organism |
---|---|---|
D955A | inactive | Drosophila melanogaster |
H537A | 5.6% of wild-type activity | Drosophila melanogaster |
H596F | 3.0% of wild-type activity | Drosophila melanogaster |
K872M | mutation of a key catalytic lysine, crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc. Inactive | Drosophila melanogaster |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
UDP-S-GlcNAc | - |
Drosophila melanogaster |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0178 | - |
UDP-GlcNAc | pH 7.5, temperature not specified in the publication | Drosophila melanogaster |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Drosophila melanogaster | Q7KJA9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
KENSPCVTPVSTA + UDP-GlcNAc | - |
Drosophila melanogaster | ? + UDP | - |
? |
Synonyms | Comment | Organism |
---|---|---|
super sex combs | - |
Drosophila melanogaster |
Sxc | - |
Drosophila melanogaster |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0362 | - |
UDP-S-GlcNAc | pH 7.5, temperature not specified in the publication | Drosophila melanogaster |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0683 | - |
pH 7.5, temperature not specified in the publication | Drosophila melanogaster | UDP-S-GlcNAc |
General Information | Comment | Organism |
---|---|---|
physiological function | mutants of OGT are pupal lethal. Postpupal Drosophila development can proceed with negligible OGT catalysis, while early embryonic development is OGT activity-dependent. A severely hypomorphic OGT mutant complements sxc pupal lethality. The hypomorphic OGT mutant-rescued progeny do not produce F2 adults, because a set of Hox genes is de-repressed in F2 embryos, resulting in homeotic phenotypes | Drosophila melanogaster |