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The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2015 Jul 31;290(31):19008. doi: 10.1074/jbc.A110.192831

Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates.

Samuel H Light, George Minasov, Ludmilla Shuvalova, Mark-Eugene Duban, Michael Caffrey, Wayne F Anderson, Arnon Lavie
PMCID: PMC4521023  PMID: 26232400

VOLUME 286 (2011) PAGES 3531–3539

PAGE 3537:

The Km value of 36 ± 9 μm reported for the reaction of wild type dehydroquinate dehydratase from Gram-positive Clostridium difficile (wild type cd-DHQD) in Table 2 was not correct. The correct Km value is 171 ± 36 μm. This correction does not affect the interpretation of the results or the conclusions of this work.

TABLE 2.

Kinetic characterization of seDHQD and cdDHQD

Errors were calculated by fitting of the kinetic data to the Michaelis-Menten equation and expressed as ± S.D.

kcat Km kcat/Km
s1 μm s1 μm1
seDHQD wild type 210 ± 5 21 ± 3 10 ± 1
seDHQD K170M 0.015 ± 0.007 33 ± 4 4.5 × 10−4 ± 2.3 × 10−4
cdDHQD wild type 125 ± 4 171 ± 36 0.7 ± 0.15

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