Correction: dehydratase mediated 1-propanol production in metabolically engineered Escherichia coli

  • Rachit Jain1 and

    Affiliated with

    • Yajun Yan1Email author

      Affiliated with

      Microbial Cell Factories201211:38

      DOI: 10.1186/1475-2859-11-38

      Received: 16 March 2012

      Accepted: 30 March 2012

      Published: 30 March 2012

      Correction

      After publication of this work [1], we have noticed accidental errors that were introduced during our revision process. In our revision process, to address review comments we reduced the number of significant digits for the results of our enzyme assay experiments. As we reduced the number of significant digits to two in Tables 1 and 2, we overlooked the corresponding values mentioned in the text of "Results and Discussion" section discussing the "Methylglyoxal Synthase Assay" and "Secondary Alcohol Dehydrogenase Assay" [1]. In order to maintain consistency between the text and the tables, we would like to correct Tables 1 and 2 by increasing the number of significant digits up to four, which were used for our original submission. These changes will in no manner affect the outcome/interpretation of the experiments as described in the original publication and will not affect the merit of this work. In addition, we would like to modify the "Competing Interests" as below. The authors apologize for any inconvenience caused thereof.
      Table 1

      Methylglyoxal synthase assay results

      mgsA source

      Specific Activity (U/mg)

      K m (mM)

      Specific Activity/K m (U/mg/mM)

      C. acetobutylicum

      0.0541 ± 0.0042

      0.776 ± 0.005

      0.0697

      B. subtilis

      0.0561 ± 0.0031

      0.473 ± 0.070

      0.1186

      C. difficile

      0.0597 ± 0.0039

      1.439 ± 0.060

      0.0415

      E. coli

      0.1242 ± 0.0069

      1.418 ± 0.120

      0.0876

      T. thermophilus

      0.0161 ± 0.0004

      2.118 ± 0.070

      0.0076

      K. pneumoniae

      0.0165 ± 0.0009

      2.820 ± 0.300

      0.0058

      P. fluorescens

      0.0133 ± 0.0082

      1.560 ± 0.020

      0.0085

      R. eutropha

      0.0052 ± 0.0004

      0.700 ± 0.030

      0.0074

      Substrate dihydroxyacetone phosphate concentration was varied from 0.15 mM to 1.5 mM for all reactions. 1 unit (U) was defined as the amount (μmoles) of methylglyoxal formed per unit time (min).

      Table 2

      Specific activity and K m determination of the secondary alcohol dehydrogenases

      Gene

      Methylglyoxal

      Hydroxyacetone

       

      Specific Activity

      (U/mg)

      K m

      (mM)

      Specific Activity

      (U/mg)

      K m

      (mM)

      gldA

      2.456 ± 0.001

      68.24 ± 0.05

      0.912 ± 0.008

      10.47 ± 0.55

      budC

      3.718 ± 0.066

      0.78 ± 0.03

      4.970 ± 0.007

      1.83 ± 0.63

      The decrease in absorbance of NADH at 340 nm was recorded and used for calculations using the substrates methylglyoxal and hydroxyacetone. Substrate concentration was varied from 20 mM - 120 mM. 1 unit (U) was defined as the amount (μmoles) of product formed per unit time (min).

      Declarations

      Authors’ Affiliations

      (1)
      Biochemical Engineering Program, Faculty of Engineering, 601B Driftmier Engineering Center, University of Georgia

      References

      1. Jain R, Yan Y: Dehydratase mediated 1-propanol production in metabolically engineered Escherichia coli. Microbial Cell Factories 2011, 10:97.View Article

      Copyright

      © Jain and Yan; licensee BioMed Central Ltd. 2012

      Advertisement