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Literature summary for 3.2.1.24 extracted from
- Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates (2003), J. Biol. Chem., 278, 48074-48083.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop vapour diffusion method, crystallization of wild-type enzyme in complex with 5-fluoro-beta-L-gulosyl fluoride, mutant enzyme D341N in complex with 2-deoxy-2-fluoro-alpgha-D-mannosyl fluoride and mutant enzyme D341N in complex with 5-fluoro-beta-L-gulosyl fluoride | Drosophila melanogaster |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D341N | the turnover numberis lower by roughly 200fold compared with that of wild-type enzyme | Drosophila melanogaster |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-deoxy-2-fluoro-alpha-D-mannosyl fluoride | for mutant enzyme D341N, no inhibition of wild-type enzyme | Drosophila melanogaster |  |
| 5-fluoro-beta-L-gulosyl fluoride | reversible, acts as a slow substrate for the D341 mutant enzyme, with deglycosylation as the rate-limiting step. Inactivation is only observed when assayed at low temperatures such that deglycosylation is slow relative to the assay time | Drosophila melanogaster | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the KM-value for 2-deoxy-2-fluoro-alpha-D-mannosyl fluoride is above 25 mM, wild-type enzyme | Drosophila melanogaster | |
| 0.2 | - |
5-fluoro-beta-L-gulosyl fluoride | wild-type enzyme | Drosophila melanogaster | |
| 5 | - |
2,4-dinitrophenyl alpha-D-mannoside | wild-type enzyme | Drosophila melanogaster | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| Golgi apparatus | - |
Drosophila melanogaster | 5794 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2,4-dinitrophenyl alpha-D-mannoside + H2O | - |
Drosophila melanogaster | 2,4-dinitrophenol + alpha-D-mannose | - |
? | |
| 2-deoxy-2-fluoro-alpha-D-mannosyl fluoride + H2O | substrate for wild-type enzyme and very slow substrate of mutant enzyme D341N | Drosophila melanogaster | ? | - |
? | |
| 5-fluoro-beta-L-gulosyl fluoride + H2O | acts as a slow substrate for the D341 mutant enzyme, with deglycosylation as the rate-limiting step. Inactivation is only observed when assayed at low temperatures such that deglycosylation is slow relative to the assay time | Drosophila melanogaster | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Golgi alpha-mannosidase II | - |
Drosophila melanogaster |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0051 | - |
5-fluoro-beta-L-gulosyl fluoride | wild-type enzyme | Drosophila melanogaster | |
| 0.048 | - |
2,4-dinitrophenyl alpha-D-mannoside | mutant enzyme D341N | Drosophila melanogaster | |
| 8.6 | - |
2,4-dinitrophenyl alpha-D-mannoside | wild-type enzyme | Drosophila melanogaster | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.6 | - |
5-fluoro-beta-L-gulosyl fluoride | - |
Drosophila melanogaster | |
| 7.5 | - |
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride | - |
Drosophila melanogaster | |
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