Biochemical and Biophysical Research Communications
Volume 84, Issue 2, 29 September 1978, Pages 322-327
Purification and characterization of hepatic porcine gluconolactonase
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Cited by (21)
Specificity and Enzyme Kinetics of the Quorum-quenching N-Acyl Homoserine Lactone Lactonase (AHL-lactonase)
2004, Journal of Biological ChemistryCitation Excerpt :Several groups of lactonases have been reported (37–39). Among those characterized lactonases, the gluconolactonase of porcine liver and the lactonohydrolase from Fusarium oxysporum require divalent metal ions for activity and are inhibited by metal-chelating reagents (40, 41), whereas others, such as 4- and 5-pyridocolactonase and hydroxyglutaric acid lactonase, are independent of such ions for activity (37, 38). AHL-lactonase appears to belong to the latter.
<sup>13</sup>C NMR relaxation studies of gluconate and magnesium-gluconate interactions
1993, Journal of Inorganic BiochemistryIsolation and characterization of the gene encoding gluconolactonase from Zymomonas mobilis
1992, BBA - Gene Structure and ExpressionThe hydrolysis of 1,5-gluconolactone: semi-empirical methods and <sup>13</sup>C NMR confirmation
1992, Journal of Molecular Structure: THEOCHEMNMR studies of paramagnetic metal ion interactions with gluconate and 1,5-gluconolactone
1990, Inorganica Chimica Acta
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