Literature summary extracted from
Mariappa, D.; Zheng, X.; Schimpl, M.; Raimi, O.; Ferenbach, A.; Müller, H.; Van Aalten, D.
Dual functionality of O-GlcNAc transferase is required for Drosophila development (2015), Open Biology, 5, 15023.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.4.1.255 |
expression in Escherichia coli, N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D1–352) |
Drosophila melanogaster |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.4.1.255 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.4.1.255 |
D955A |
inactive |
Drosophila melanogaster |
2.4.1.255 |
H537A |
5.6% of wild-type activity |
Drosophila melanogaster |
2.4.1.255 |
H596F |
3.0% of wild-type activity |
Drosophila melanogaster |
2.4.1.255 |
K872M |
mutation of a key catalytic lysine, crystallized in complex with the inhibitor/substrate analogue UDP-5S-GlcNAc. Inactive |
Drosophila melanogaster |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.4.1.255 |
UDP-S-GlcNAc |
- |
Drosophila melanogaster |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
2.4.1.255 |
0.0178 |
- |
UDP-GlcNAc |
pH 7.5, temperature not specified in the publication |
Drosophila melanogaster |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.255 |
Drosophila melanogaster |
Q7KJA9 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.255 |
KENSPCVTPVSTA + UDP-GlcNAc |
- |
Drosophila melanogaster |
? + UDP |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.4.1.255 |
super sex combs |
- |
Drosophila melanogaster |
2.4.1.255 |
Sxc |
- |
Drosophila melanogaster |
Ki Value [mM]
EC Number |
Ki Value [mM] |
Ki Value maximum [mM] |
Inhibitor |
Comment |
Organism |
Structure |
---|
2.4.1.255 |
0.0362 |
- |
UDP-S-GlcNAc |
pH 7.5, temperature not specified in the publication |
Drosophila melanogaster |
|
IC50 Value
EC Number |
IC50 Value |
IC50 Value Maximum |
Comment |
Organism |
Inhibitor |
Structure |
---|
2.4.1.255 |
0.0683 |
- |
pH 7.5, temperature not specified in the publication |
Drosophila melanogaster |
UDP-S-GlcNAc |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.4.1.255 |
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 |