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Literature summary for 2.7.8.15 extracted from
- GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation (2018), Nat. Struct. Mol. Biol., 25, 217-224 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures of human GPT in complex with tunicamycin for both the canonical Pro129 variant and a His129 variant, to 3.10 A and 2.95 A resolution, respectively. GPT crystallizes as a homodimer with one tunicamycin molecule bound to the active site of each protomer near the cytosolic side of the ER membrane. Comparison of the GPT-tunicamycin complex to the MraY-tunicamycin complex. GPT and MraY (EC 2.7.8.13) have drastically different dimer organization and differ in the the role of Mg2+ in tunicamycin inhibition, in active site shape and solvent accessibility and in the lipid substrate specificity | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
| membrane | - |
Homo sapiens | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9H3H5 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DPAGT1 | - |
Homo sapiens |
| GPT | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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