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

Rachit Jain 0 Yajun Yan 0 0 Biochemical Engineering Program, Faculty of Engineering, 601B Driftmier Engineering Center, University of Georgia , Athens, GA 30602 , USA - 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 Table 1 Methylglyoxal synthase assay results Specific Activity (U/mg) 0.0541 0.0042 0.0561 0.0031 0.0597 0.0039 0.1242 0.0069 0.0161 0.0004 0.0165 0.0009 0.0133 0.0082 0.0052 0.0004 Table 2 Specific activity and Km determination of the secondary alcohol dehydrogenases 2.456 0.001 3.718 0.066 68.24 0.05 0.78 0.03 0.912 0.008 4.970 0.007 10.47 0.55 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 (moles) of product formed per unit time (min). modify the Competing Interests as below. The authors apologize for any inconvenience caused thereof. Authors contributions YY and RJ conceived the study. RJ performed the experiments under the guidance of YY. An equal contribution by YY and RJ was made for literature review and drafting of the manuscript. Both authors read and approved the final manuscript. 0.473 0.070 1.439 0.060 1.418 0.120 2.118 0.070 2.820 0.300 1.560 0.020 0.700 0.030 Specific Activity/Km (U/mg/mM) 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 (moles) of methylglyoxal formed per unit time (min). (...truncated)