Skip to Content
MilliporeSigma
  • Catalytically active filaments - pyruvate decarboxylase from Neurospora crassa. pH-controlled oligomer structure and catalytic function.

Catalytically active filaments - pyruvate decarboxylase from Neurospora crassa. pH-controlled oligomer structure and catalytic function.

The FEBS journal (2011-11-15)
Stefanie Hüttl, Juliane Fiebig, Steffen Kutter, Gerd Hause, Hauke Lilie, Michael Spinka, Stephan König
ABSTRACT

Pyruvate decarboxylase is a key enzyme in organisms whose energy metabolism is based on alcoholic fermentation. The enzyme catalyses the nonoxidative decarboxylation of 2-oxo acids in the presence of the cofactors thiamine diphosphate and magnesium ions. Pyruvate decarboxylase species from yeasts and plant seeds studied to date are allosterically activated by their substrate pyruvate. However, detailed kinetic studies on the enzyme from Neurospora crassa demonstrate for the first time the lack of substrate activation for a yeast pyruvate decarboxylase species. The quaternary structure of this enzyme species is also peculiar because it forms filamentous structures. The complex enzyme structure was analysed using a number of methods, including small-angle X-ray solution scattering, transmission electron microscopy, analytical ultracentrifugation and size-exclusion chromatography. These measurements were complemented by detailed kinetic studies in dependence on the pH.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Pyruvate Decarboxylase from baker′s yeast (S. cerevisiae), ammonium sulfate suspension, 5.0-20.0 units/mg protein (biuret)
SKU
Pack Size
Availability
Price
Quantity