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Literature summary for 2.4.1.255 extracted from

  • Iyer, S.P.; Hart, G.W.
    Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity (2003), J. Biol. Chem., 278, 24608-24616.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
baculovirus expression Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
DELTA2.5OGT Baculovirus-produced recombinant, is partially active toward the OID protein substrate, but is fully active toward the CKII peptide substrate Rattus norvegicus
DELTA5.5OGT Baculovirus-produced recombinant Rattus norvegicus
full-length OGT Baculovirus-produced recombinant Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
additional information the isolated tetratricopeptide repeat domain of OGT competitively inhibits glycosylation of the OID protein, but does not inhibit glycosylation of small peptides, providing kinetic evidence for the role of the tetratricopeptide repeat domain as a protein substrate docking site Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00335
-
OIP106 protein apparent Km of OGT for the OID of OIP106 protein Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein kinase II peptide + UDP-GlcNAc
-
Rattus norvegicus ? + UDP
-
?
additional information enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) Rattus norvegicus ?
-
?
additional information DELTA859 is not able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 Rattus norvegicus ?
-
?
additional information OGT-interacting proteins interact strongly with the tetratricopeptide repeat (TPR) domain of OGT, they are modified by O-GlcNAc and are excellent substrates of OGT Rattus norvegicus ?
-
?
nucleoporin p62 + UDP-GlcNAc high affinity substrate Rattus norvegicus ? + UDP
-
?
OIP106 protein + UDP-GlcNAc N-terminal deletions of OIP106 are generated as S-tagged constructs: DELTAnCC, DELTA491, DELTA639, DELTA859 Rattus norvegicus O-GlcNAc-OIP106 protein + UDP
-
?
UDP-GlcNAc + DELTA639 protein N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 Rattus norvegicus UDP + N-acetyl-D-glucosaminyl-[DELTA639 protein]
-
?
UDP-GlcNAc + DELTAnCC protein N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 Rattus norvegicus UDP + N-acetyl-D-glucosaminyl-[DELTAnCC protein]
-
?
UDP-GlcNAc DELTA491 protein N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106 Rattus norvegicus UDP + N-acetyl-D-glucosaminyl-[DELTA491 protein]
-
?

Synonyms

Synonyms Comment Organism
O-GlcNAc transferase
-
Rattus norvegicus
OGT
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Rattus norvegicus