Molecular structure of malate synthase and structural changes upon ligand binding to the enzyme |
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Authors: | G Schmid H Durchschlag G Biedermann H Eggerer R Jaenicke |
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Institution: | Biochemie I/II, Fachbereich Biologie, Universität Regensburg, Germany |
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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 Mg2+ causes no structural effects, suggesting the metal ion to be involved in enzymatic catalysis rather than structural alterations. |
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Keywords: | MS malate synthase (EC 4 1 3 2) CD circular dichroism |
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