Subsite mapping of enzymes: collecting and processing experimental data--a case study of an amylase-malto-oligosaccharide system.
Two research groups have independently developed the theory and experimental methodology for quantitatively assessing substrate monomer-subsite binding-energies for depolymerases. When the two approaches are applied to the same enzyme-substrate system they yield surprisingly divergent results. This paper outlines the application of the two approaches to an amylase-maltooligosaccharide system and points out the more important areas of disagreement. We show that by proper data-management, the conflicts between the tow laboratories are basically resolved. The complexities of the subsite model demand extensive data-gathering and exacting data-processing and verification that the computed model-parameters can faithfully reproduce the experimental data.
D000681:Amylases / Q000378:metabolism; D001407:Bacillus / Q000201:enzymology; D001665:Binding Sites; D003201:Computers; D007700:Kinetics; D008320:Maltose; D008433:Mathematics; D008956:Models, Chemical; D009844:Oligosaccharides; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D009844:Oligosaccharides; D008320:Maltose; D000681:Amylases