Application | Comment | Organism |
---|---|---|
analysis | the small enzyme is an ideal computational model for its family of enzymes, GH5, and can be used to create several enzyme-substrate models starting from a crystallographic glucanase inhibitor structure | Candida albicans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-1,3-glucan + H2O | Candida albicans | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candida albicans | P29717 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-1,3-glucan + H2O | - |
Candida albicans | ? | - |
? | |
laminarihexaose + H2O | - |
Candida albicans | ? | - |
? | |
laminaripentaose + H2O | - |
Candida albicans | ? | - |
? | |
laminaritetraose + H2O | - |
Candida albicans | ? | - |
? | |
additional information | two surface loops, amino acids 36-47 and 101-106, might play a functional role after substrate binding. The loops could bind the enzyme to a glucan chain in the cell wall. Molecular dynamics and modelling of enzyme-substrate complexes, overview | Candida albicans | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | generation of a series of enzyme-substrate complexes using molecular docking, ranging from Exg-glucose to Exg-laminarihexaose, structure optimizations followed by molecular dynamics, conducted for each complex to assess the flexibility of the substrate, of the enzyme as a whole, and of enzyme-substrate interactions, overview | Candida albicans |
Synonyms | Comment | Organism |
---|---|---|
beta-1,3-exoglucanase | - |
Candida albicans |
Exg | - |
Candida albicans |
More | the enzyme belongs to the glycosyl hydrolase family 5, GH5 | Candida albicans |