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Literature summary extracted from
- The role of the active site Zn in the catalytic mechanism of the GH38 Golgi alpha -mannosidase II: implications from noeuromycin inhibition (2006), Biocatal. Biotransform., 24, 55-61.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.114 | drug development | development of specific inhibitors of GMII that can lead to novel anti-metastatic or anti-inflammatory compounds | Drosophila melanogaster |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.114 | noeuromycin | - |
Drosophila melanogaster |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.114 | Zn2+ | GMII contains a Zn atom which forms contacts with substrate analogues, stabilizes catalytic intermediates, and other inhibitors observed in the active site | Drosophila melanogaster | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.114 | Drosophila melanogaster | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.114 | GH38 Golgi alpha-mannosidase II | - |
Drosophila melanogaster |
| 3.2.1.114 | GmII | - |
Drosophila melanogaster |
| 3.2.1.114 | Golgi alpha-mannosidase II | - |
Drosophila melanogaster |
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Release 2023.1 (January 2023)
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