Mar 1, 1976

Some properties of the pyruvate carboxylase from Pseudomonas fluorescens

Journal of General Microbiology
S R Milrad de Forchetti, J J Cazzulo

Abstract

The pyruvate carboxylase of Pseudonomas fluorescens was purified 160-fold from cells grown on glucose at 20 degrees C. The activity of this purified enzyme was not affected by acetyl-coenzyme A or L-aspartate, but was strongly inhibited by ADP, which was competitive towards ATP. Pyruvate gave a broken double reciprocal plot, from which two apparent Km values could be determined, namely 0-08 and 0-21 mM, from the lower and the higher concentration ranges, respectively. The apparent Km for HCO3 at pH 6-9, in the presence of the manganese ATP ion (MnATP2-), was 3-1 mM. The enzyme reaction had an optimum pH value of 7-1 or 9-0 depending on the use of MnATP2- or MgATP2-, respectively, as substrate. Free Mg2+ was an activator at pH values below 9-0. The enzyme was strongly activated by monovalent cations; NH4+ and K+ were the better activators, with apparent Ka values of 0-7 and 1-6 mM, respectively. Partially purified enzymes from cells grown on glucose at 1 or 20 degrees C had the same properties, including the thermal stability. In both cases 50% of the enzyme activity was lost after pre-incubation for 10 min at 46 degrees C. The molecular weight was estimated to be about 300000 daltons by gel filtration on Sephadex G-200. The reg...Continue Reading

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Mentioned in this Paper

Manganese
Sephadex G 200
Enzymes, antithrombotic
Aspartic Acid, Magnesium-Potassium (2:1:2) Salt
Coenzyme A
Aspartate
Biodermatin
Pyruvate Measurement
Acetyl Coenzyme A
Glucose, (beta-D)-Isomer

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