Crystallization (Comment) | Organism |
---|---|
isomaltase free and in complex with inhibitor maltose, hanging drop vapor diffusion method, 0.003 ml of protein solution containing 4.5 mg/ml protein is mixed with an equal volume of reservoir solution containing 50 mM HEPES, pH 7.3, 0.2 M lithium acetate, and 19% w?v PEG3350, 2 weeks, X-ray diffraction structure determination and analysis at 1.3 A and 1.6 A resolution, respectively | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
maltose | competitive inhibitor | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P53051 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the best substrate for oligo-1,6-glucosidase is isomaltotriose, other, longer-chain oligosaccharides are also good substrates. Isomaltase shows the highest activity towards isomaltose and very little activity towards longer oligosaccharides, because the entrance to the active site pocket of isomaltose is severely narrowed by Tyr158, His280, and loop 310315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | isomaltase contains three domains, namely, A, B, and C. Domain A consists of the (b eta?alpha)8-barrel common to glycoside hydrolase family 13. However, the folding of domain C is rarely seen in other glycoside hydrolase family 13 enzymes | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
isomaltase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
additional information | catalytic residues are Glu277 and Asp352, isomaltase active site structure, role of the water chains in the active site pocket, the hydrogen bond network in the active site of isomaltase, overview | Saccharomyces cerevisiae |