The Lyme Disease Network
Medical / Scientific Abstract
|Title:||Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi.|
|Authors:||Deng Z, Roberts D, Wang X, Kemp RG|
|Source:||Arch Biochem Biophys 1999 Nov 15;371(2):326-31|
|Organization:||Department of Microbiology and Immunology, Chicago Medical School, North Chicago, Illinois 60064, USA.|
The two genes for the putative pyrophosphate-dependent phosphofructokinases (PPi-PFKs) of Borrelia burgdorferi were cloned by PCR and expressed in Escherichia coli, and their protein products were purified to near homogeneity. The larger of the two gene products, a 62-kDa protein, is an active PPi-PFK and exists in solution as a dimer. It has apparent K(m) values for fructose 6-P and PPi of 109 and 15 microM, respectively, and a pH optimum of 6.4 to 7.2. The 62-kDa protein was crystallized and subjected to preliminary diffraction analysis. The smaller gene product, a 48-kDa protein, exists in solution as a higher polymer and shows no ATP- or PPi-dependent activity, despite having a secondary structure as estimated by circular dichroism that is not significantly different from that of other PFKs. Copyright 1999 Academic Press.
Animal, Borrelia burgdorferi, ENZYMOLOGY, Cloning, Molecular, Crystallography, X-Ray, Diphosphates, METABOLISM, Entamoeba histolytica, ENZYMOLOGY, Genes, Bacterial, Hydrogen-Ion Concentration, Kinetics, Reading Frames, Recombinant Proteins, ISOLATION & PURIF, METABOLISM, Support, U.S. Gov't, P.H.S., 6-Phosphofructokinase, CHEMISTRY, GENETICS, METABOLISM
Unique ID: 20014531
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