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Pyruvate decarboxylase from Kluyveromyces lactis : An enzyme with an extraordinary substrate activation behaviour by Florian Krieger; Michael Spinka; Ralph Golbik; Gerhard Hübner; Stephan König is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Pyruvate decarboxylase from Kluyveromyces lactis : An enzyme with an extraordinary substrate activation behaviour about?

Pyruvate decarboxylase (EC 4.1.1.1) was isolated and purified from the yeast __Kluyveromyces lactis__. The properties of this enzyme relating to the native oligomeric state, the subunit size, the nucleotide sequence of the coding gene(s), the catalytic activity, and protein fluorescence as well as circular dichroism are very similar to those of the well characterized pyruvate decarboxylase species from yeast. Remarkable differences were found in the substrate activation behaviour of the two pyruvate decarboxylases using three independent methods: steady‐state kinetics, stopped‐flow measurements, and kinetic dilution experiments. The dependence of the observed activation rate constant on the substrate concentration of pyruvate decarboxylase from __K. lactis__ showed a minimum at a pyruvate concentration of 1.5 mm. According to the mechanism of substrate activation suggested this local minimum occurs due to the big ratio of the dissociation constants for the binding of the first (regulatory) and the second (catalytic) substrate molecule. The microscopic rate constants of the substrate activation could be determined by a refined fit procedure. The influence of the artificial activator

Who reads Pyruvate decarboxylase from Kluyveromyces lactis : An enzyme with an extraordinary substrate activation behaviour?

Author

Florian Krieger; Michael Spinka; Ralph Golbik; Gerhard Hübner; Stephan König

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)