Enzymes associated with carbohydrate metabolism of scyphistomae of Aurelia aurita and Chrysaora quinquecirrha (Scyphozoa: semaeostomae)

Alan L. Lin, Paul L. Zubkoff

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

1. 1. A functional tricarboxylic acid cycle in the scyphistomae of Aurelia aurita and Chrysaora quinquecirrha is indicated by the presence of NADP+-linked isocitrate dehydrogenase (IDH, E.C. 1.1.1.42), succinate dehydrogenase (SDH, E.C. 1.3.99.1), and malate dehydrogenase (MDH,E.C. 1.1.1.37). 2. 2. These scyphistomae are potentially capable of survival under low oxygen conditions by utilizing phosphoenol pyruvate carboxykinase (PEPCK, E.C. 4.1.1.32), MDH, and SDH in the absence of lactate dehydrogenase. 3. 3. The Michaelis constants (Km), energies of activation (Ea), and temperature dependence are reported for several enzymes. 4. 4. The scyphistomae cultured at lower temperature always have a higher substrate enzyme affinity (lower Km) and lower Ea than organisms maintained at room temperature. The reduction in velocity of enzymatic reaction with decreased temperature may be partially, or, sometimes fully, offset by a decrease of Km and Ea. 5. 5. The pH dependence of pyruvate kinase (PK, E.C. 2.7.1.40), PEPCK, and MDH is discussed in relation to possible pH control at the branch point of phosphoenol pyruvate.

Original languageEnglish (US)
Pages (from-to)303-308
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume57
Issue number4
DOIs
StatePublished - 1977

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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