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

FEBS Letters

Remenyik, Judit¹  Kandra, Lili²  Gyémánt, Gyöngyi²  Hovánszki, György³  Lipták, András² 

[1] Research Group for Carbohydrates of Hungarian Academy of Sciences, P.O. Box 55, H-4010 Debrecen, Hungary;University of Debrecen, Faculty of Sciences, Department of Biochemistry, P.O. Box 55, H-4010 Debrecen, Hungary;University of Debrecen, Faculty of Agriculture, Department of Agricultural Chemistry, P.O. Box 36, H-4015 Debrecen, Hungary

关键词: α-Amylase;    2-Chloro-4-nitrophenyl;    Benzylidene;    Maltooligosaccharide;    Bond-cleavage frequency;    Binding energy;    BAA;    Bacillus amyloliquefaciens α-amylase;    BCF;    bond-cleavage frequency;    BLA;    Bacillus licheniformis α-amylase;    Bnl;    4;    6-O-benzylidene;    CNP;    2-chloro-4-nitrophenyl;    DP;    degree of polymerisation;    NP;    4-nitrophenyl;   

DOI  :  10.1016/S0014-5793(02)02649-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown