PMID: 6402366Feb 1, 1983Paper

6-phospho-D-gluconate dehydrogenase from Pseudomonas fluorescens. Properties and subunit structure

European Journal of Biochemistry
C StournarasG Kurz

Abstract

1. The 6-phospho-D-gluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) from Pseudomonas fluorescens, a B-side stereospecific enzyme, is active with both NAD+ and NADP+, having a specific activity of the homogeneous enzyme of 121 mumols NADH and 23 mumols NADPH, respectively, formed min-1 mg protein-1. The pI of the native enzyme is 4.62, the pH optimum is about 8.2. 2. The molecular weight of the native enzyme has been determined to be 126000 by sedimentation equilibrium studies. The molecular weight of the polypeptide chains composing the enzyme has been found to be 32000 by dodecylsulfate/polyacrylamide gel electrophoresis and 31000 by sedimentation equilibrium studies in presence of 6 M guanidine hydrochloride. The native enzyme is composed of four polypeptide chains. 3. Reacting enzyme centrifugation studies gave at pH 8.2 a sedimentation coefficient s20, w of 8.04 S and a diffusion coefficient D20, w of 6.56 F, resulting in a molecular weight of 115000 for the catalytically active form. Thus, the enzyme is active as the tetramer. So far the enzyme from P. fluorescens is the sole 6-phospho-D-gluconate dehydrogenase (decarboxylating) composed of four polypeptide chains.

References

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Citations

Jan 1, 1986·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M del Mar Medina-Puerta, A Garrido-Pertierra
Oct 20, 2005·Journal of Bioscience and Bioengineering·Hitomi OharaHitoshi Kondo
Mar 1, 1987·Plant Physiology·S O Salminen, J G Streeter
Oct 1, 1991·Protein Expression and Purification·D O SomersM J Adams
Aug 19, 2015·Frontiers in Microbiology·Sebastiaan K SpaansServé W M Kengen
Sep 8, 2007·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Raju Mukherjee, Dipankar Chatterji

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