Microenvironment of the enzyme-bound NADH is different in lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenase microcrystals

B. Vértessy, M. Vas, T. Keleti

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Two possible consequences of crystal lattice formation were studied with glyceraldehyde-3-phosphate dehydrogenases isolated from lobster (Palinurus vulgaris) and pig muscle: (i) changes in the microenvironment of the NADH-binding site as detected by fluorescence polarization, and (ii) differences in the maximal activities of the microcrystalline enzymes as compared to those in solution, (i) In solution practically no difference was found between the polarization values of the enzyme-NADH and the catalytic intermediate 3-phosphoglyceroyl-enzyme-NADH complexes whether with lobster or with pig enzyme. In microcrystalline state a similar effect was found with the lobster enzyme. However, fluorescence polarization of NADH bound to the pig enzyme was significantly different in the presence and in the absence of the 3-phosphoglyceroyl group. This indicates some change in the microenvironment of the pig enzyme-bound NADH which occurs upon decomposition of the catalytic intermediate. (ii) The difference between the microcrystalline lobster and pig muscle glyceraldehyde-3-phosphate dehydrogenases pertains also to their functional properties. Packing of soluble pig muscle enzyme into a crystal lattice stabilizes a unique protein conformation of extremely low activity (about 3% of that measured in solution). The maximal molar activity of the lobster enzyme is identical in crystalline state and in solution, which is an exceptional phenomenon.

Original languageEnglish
Pages (from-to)299-305
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume251
Issue number1
DOIs
Publication statusPublished - Nov 15 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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