Literature DB >> 949715

Subsite mapping of enzymes: collecting and processing experimental data--a case study of an amylase-malto-oligosaccharide system.

J A Thoma, J D Allen.   

Abstract

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.

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Year:  1976        PMID: 949715     DOI: 10.1016/s0008-6215(00)83518-1

Source DB:  PubMed          Journal:  Carbohydr Res        ISSN: 0008-6215            Impact factor:   2.104


  3 in total

1.  Subsite mapping of enzymes. Application of the depolymerase computer model to two alpha-amylases.

Authors:  J D Allen; J A Thoma
Journal:  Biochem J       Date:  1976-10-01       Impact factor: 3.857

2.  Subsite mapping of enzymes. Depolymerase computer modelling.

Authors:  J D Allen; J A Thoma
Journal:  Biochem J       Date:  1976-10-01       Impact factor: 3.857

3.  Subsite structure of the endo-type chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS.

Authors:  Omid Hekmat; Ken Tokuyasu; Stephen G Withers
Journal:  Biochem J       Date:  2003-09-01       Impact factor: 3.857

  3 in total

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