Literature DB >> 11816058

Individual molecules of thermostable alkaline phosphatase support different catalytic rates at room temperature.

Ashley C Dyck1, Douglas B Craig.   

Abstract

Thermus thermophilus cells were grown at 70 degrees C, lysed and the lysate subjected to single molecule alkaline phosphatase assays, using a capillary electrophoresis laser-induced fluorescence detection-based method. The enzyme was found to be heterogeneous with respect to catalytic rate when assayed at room temperature. Turnover numbers ranged 12-fold, with an average of 400 +/- 200 reactions/min for the 80 molecules assayed. Copyright 2002 John Wiley & Sons, Ltd.

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Year:  2002        PMID: 11816058     DOI: 10.1002/bio.672

Source DB:  PubMed          Journal:  Luminescence        ISSN: 1522-7235            Impact factor:   2.464


  4 in total

1.  Single-molecule enzymology of chymotrypsin using water-in-oil emulsion.

Authors:  Alan I Lee; James P Brody
Journal:  Biophys J       Date:  2005-03-11       Impact factor: 4.033

2.  Single molecule assays of beta-galactosidase from two wild-type strains of E. coli: effects of protease inhibitors on microheterogeneity and different relative activities with differing substrates.

Authors:  Ellert R Nichols; Jennilee M A Gavina; Robert G McLeod; Douglas B Craig
Journal:  Protein J       Date:  2007-02       Impact factor: 2.371

3.  Heterogeneous properties of individual molecules of beta-galactosidase from the thermophilic bacteria Geobacillus stearothermophilus.

Authors:  Douglas B Craig
Journal:  Protein J       Date:  2010-01       Impact factor: 2.371

4.  Observing single enzyme molecules interconvert between activity states upon heating.

Authors:  Marcin J Rojek; David R Walt
Journal:  PLoS One       Date:  2014-01-21       Impact factor: 3.240

  4 in total

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