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

BRENDA support

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.
    View publication on PubMedView publication on EuropePMC

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