Unusual steady-state kinetic properties of a chilopod enzyme: l(+)lactate dehydrogenase purified from Scolopendra cingulata

Massimo Dell'Agata, Gianna Pannunzio, Margherita Annicchiarico, Annamaria Coscarella, Alessandro Ferracin

Research output: Contribution to journalArticle

Abstract

1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.

Original languageEnglish
Pages (from-to)439-444
Number of pages6
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume96
Issue number3
DOIs
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

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