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Literature summary for 3.2.1.58 extracted from
- Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe clamp at the active site entrance (2010), FEBS J., 277, 4549-4561.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Pichia pastoris | Candida albicans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| mutants F258I, E292Q, E292S /F229A and F144Y/F258Y, and mutant E292S/F229A complexed with laminaritriose | Candida albicans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E292Q | inactive, crystal structure analysis | Candida albicans |
| E292S/F229A | inactive, crystal structure analysis | Candida albicans |
| F144A | about 1% of wild-type activity | Candida albicans |
| F144A/F258A | inactive | Candida albicans |
| F144Y/F258Y | about 3% of wild-type activity | Candida albicans |
| F229A | 17fold loss of hydrolytic activity | Candida albicans |
| F258A | activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala | Candida albicans |
| F258I | activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala | Candida albicans |
| F258W | activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala | Candida albicans |
| F258Y | activity of the F258 mutants falls off steadily in the order Phe>Trp>Tyr>Ile>Ala | Candida albicans |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
Laminarin | KM value of wild-type is 4.8 mg/ml, pH 5.6, 37°C | Candida albicans |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Candida albicans | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | P29717 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| laminarin + H2O | - |
Candida albicans | D-glucose + ? | - |
? | |
| additional information | requirement for double-sided CH/pi interactions at the +1 subsite, and necessity for phenylalanine rather than tyrosine or tryptophan. Carbohydrate-protein interactions at the +1 subsite of Exg provide the main contribution to the transition state interaction energy | Candida albicans | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Exg | - |
Candida albicans |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.7 | - |
Laminarin | mutant F144A, pH 5.6, 37°C | Candida albicans | |
| 8 | - |
Laminarin | mutant F144A/F258Y, pH 5.6, 37°C | Candida albicans | |
| 9 | - |
Laminarin | mutant F258I, pH 5.6, 37°C | Candida albicans | |
| 25 | - |
Laminarin | mutant F229A, pH 5.6, 37°C | Candida albicans | |
| 88.3 | - |
Laminarin | mutant F258W, pH 5.6, 37°C | Candida albicans | |
| 157 | - |
Laminarin | wild-type, pH 5.6, 37°C | Candida albicans | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
Laminarin | kcat/KM value of wild-type is 32.7 mg per ml and sec, pH 5.6, 37°C | Candida albicans | |
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