Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates

Lili Kandra, Gyöngyi Gyémánt, Judit Remenyik, György Hovánszki, András Lipták

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44 Citations (Scopus)


This study represents the first characterisation of the substrate-binding site of Bacillus licheniformis α-amylase (BLA). It describes the first subsite map, namely, number of subsites, apparent subsite energies and the dual product specificity of BLA. The product pattern and cleavage frequencies were determined by high-performance liquid chromatography, utilising a homologous series of chromophore-substituted maltooligosaccharides of degree of polymerisation 4-10 as model substrates. The binding region of BLA is composed of five glycone, three aglycone-binding sites and a 'barrier' subsite. Comparison of the binding energies of subsites, which were calculated with a computer program, shows that BLA has similarity to the closely related Bacillus amyloliquefaciens α-amylase.

Original languageEnglish
Pages (from-to)79-82
Number of pages4
JournalFEBS letters
Issue number1-3
Publication statusPublished - May 8 2002



  • 2-Chloro-4-nitrophenyl
  • Benzylidene
  • Binding energy
  • Bond-cleavage frequency
  • Maltooligosaccharide
  • α-Amylase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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