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Literature summary for 3.2.1.10 extracted from

  • Yamamoto, K.; Miyake, H.; Kusunoki, M.; Osaki, S.
    Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose (2010), FEBS J., 277, 4205-4214.
    View publication on PubMed

Crystallization (Commentary)

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

Inhibitors Comment Organism Structure
maltose competitive inhibitor Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53051
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Substrates and Products (Substrate)

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 310–315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview Saccharomyces cerevisiae ?
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Subunits

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

Synonyms Comment Organism
isomaltase
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Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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assay at Saccharomyces cerevisiae

General Information

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