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The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2019 Nov 1;294(44):16479. doi: 10.1074/jbc.AAC119.011308

Correction: Phosphoglycolate phosphatase is a metabolic proofreading enzyme essential for cellular function in Plasmodium berghei.

Lakshmeesha Kempaiah Nagappa, Pardhasaradhi Satha, Thimmaiah Govindaraju, Hemalatha Balaram
PMCID: PMC6827321  PMID: 31676556

VOLUME 294 (2019) PAGES 4997–5007

During copy editing, an error was introduced in a column label in Table 1. The label of the last column should be kcat/Km. This error has now been corrected and does not affect the results and conclusions of this work.

Table 1.

Substrate Kinetic parameters
Kmm) Vmax (μmol min−1 mg−1) kcat (s−1) kcat/Km (m−1 s−1)
Kinetic parameters of PbPGP
    β-Glycerophosphate 2110 ± 11 16.2 ± 0.14 10.18 ± 0.08 4827
    2-Phosphoglycolate 2526 ± 494 119.5 ± 12.5 75.15 ± 7.86 29,747
    2-Phospho-l-lactate 4773 ± 574 107 ± 13.2 67.34 ± 8.31 14,108
Kinetic parameters of murine PGPa
    2-Phosphoglycolate 766 ± 68 11.34b 6.56 ± 0.44 8564
    2-Phospho-l-lactate 174 ± 55 3.14b 1.82 ± 0.34 10,480
Kinetic parameters of S. cerevisiae Pho13a
    2-Phosphoglycolate 221 ± 13 32.87b 19.0 ± 0.44 85,700
    2-Phospho-l-lactate 747 ± 135 13.09b 7.57 ± 1.04 10,113

a Values taken from Collard et al., 2016 (20).

b Vmax was calculated using kcat values from Collard et al., 2016 (20). Molecular mass values of 34,540.68 Da and 34,624.58 Da for murine PGP and Pho13, respectively, were used in the calculation.


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