Literature summary for 2.4.1.255 extracted from

Mariappa, D.; Zheng, X.; Schimpl, M.; Raimi, O.; Ferenbach, A.; M�ller, H.; Van Aalten, D.
Dual functionality of O-GlcNAc transferase is required for Drosophila development (2015), Open Biology, 5, 15023.

Search for more literature for 2.4.1.255

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli, N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D1352)	Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment)	Organism
N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D135), 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 (535566) 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

Crystallization (Comment)

Organism

N-terminally truncated construct starting at amino acid 353 in tetratricopeptide repeat TPR 10 (D135), 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 (535566) 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

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

Inhibitors	Comment	Organism	Structure
UDP-S-GlcNAc	-	Drosophila melanogaster

KM Value [mM]

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

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	Q7KJA9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
KENSPCVTPVSTA + UDP-GlcNAc	-	Drosophila melanogaster	? + UDP	-	?

Synonyms

Synonyms	Comment	Organism
super sex combs	-	Drosophila melanogaster
Sxc	-	Drosophila melanogaster

Ki Value [mM]

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	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

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