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Literature summary for 3.2.1.133 extracted from

  • Manas, N.H.; Bakar, F.D.; Illias, R.M.
    Computational docking, molecular dynamics simulation and subsite structure analysis of a maltogenic amylase from Bacillus lehensis G1 provide insights into substrate and product specificity (2016), J. Mol. Graph. Model., 67, 1-13 .
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Alkalihalobacillus lehensis X5CPN2
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Alkalihalobacillus lehensis G1 X5CPN2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-cyclodextrin + H2O the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin Alkalihalobacillus lehensis maltose + ?
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beta-cyclodextrin + H2O the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin Alkalihalobacillus lehensis G1 maltose + ?
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 ?
additional information the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above Alkalihalobacillus lehensis ?
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additional information the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above Alkalihalobacillus lehensis G1 ?
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 ?

Synonyms

Synonyms Comment Organism
MAG1
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 Alkalihalobacillus lehensis