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Molecular structure of malate synthase and structural changes upon ligand binding to the enzyme

Authors
  • Schmid, G.
  • Durchschlag, H.
  • Biedermann, G.
  • Eggerer, H.
  • Jaenicke, R.
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Publication Date
Jan 01, 1974
Volume
58
Issue
2
Pages
419–426
Identifiers
DOI: 10.1016/0006-291X(74)90381-7
Source
Elsevier
Keywords
License
Unknown

Abstract

Malate synthase has a molecular weight of about 170 000 as shown by ultracentrifugation, sucrose gradient centrifugation, and thin layer gel-chromatography. High dilution, extremes of pH, succinylation, and treatment with sodium dodecylsulfate suggest the enzyme to be a tetramer. The CD spectrum is typical for a globular protein with moderate helical content (∼30 %), and shows anomalous Cotton effects at 250–290 nm. Binding of substrates (acetyl-CoA, glyoxylate) or the substrate analog pyruvate causes slight conformational changes which are reflected in alterations of the CD bands in the range of aromatic absorption; binding of Mg 2+ causes no structural effects, suggesting the metal ion to be involved in enzymatic catalysis rather than structural alterations.

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