HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by O'Brien, W. E. Articles by Wood, H. G. Search for Related Content PubMed PubMed Citation Articles by O'Brien, W. E. Articles by Wood, H. G. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 22, 8690-8695, Nov, 1975

Isolation and characterization of a pyrophosphate-dependent phosphofructokinase from Propionibacterium shermanii

W. E. O'Brien, S. Bowien and H. G. Wood

A pyrophosphate-dependent phosphofructokinase (pyrophosphate; D-fructose-6-phosphate-1-phosphotransferase) has been purified and characterized from extracts of Propionibacterium shermanii. The enzyme catalyzes the transfer of phosphate from pyrophosphate to fructose 6-phosphate to yield fructose-1,6-P2 and phosphate. This unique enzymatic activity was observed initially in Entamoeba histolytica (Reeves, R.E., South, D.J., Blytt, H.G., and Warren, L. G. (1974) J. Biol. Chem. 249, 7734-7741). This is the third pyrophosphate-utilizing enzyme that these two diverse organisms have in common. The others are phosphoenolpyruvate carboxytransphosphorylase and pyruvate phosphate dikinase. The PPi-phosphofructokinase from P. shermanii is specific for fructose-6-P and fructose-1,6-P2, no other phosphorylated sugars were utilized. Phosphate could be replaced by arsenate. The Km values are: phosphate, 6.0 X 10(-4) M; fructose-1, 6-P2, 5.1 X 10(-5) M; pyrophosphate, 6.9 X 10(-5) M; and fructose-6-P, 1.0 X 10(-4) M. The S20w is 5.1 S. The molecular weight of the native enzyme is 95,000. Sodium dodecyl sulfate electrophoresis of the enzyme showed a single band migrating with an Rf corresponding to a molecular weight of 48,000. Extracts of P. shermanii have PPi-phosphofructokinase activity approximately 6 times greater than ATP-phosphofructokinase and 15 to 20 times greater than fructose diphosphatase activities. It is proposed that (a) PPi may replace ATP in the formation of fructose-1-6-P2 when the organism is grown on glucose and (b) when the organism is grown on lactate or glycerol the conversion of fructose-1,6-P2 to fructose-6-P during gluconeogenesis may occur by phosphorolysis rather than hydrolysis.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. Costa dos Santos, W. Seixas da-Silva, L. de Meis, and A. Galina Proton Transport in Maize Tonoplasts Supported by Fructose-1,6-Bisphosphate Cleavage. Pyrophosphate-Dependent Phosphofructokinase as a Pyrophosphate-Regenerating System Plant Physiology, October 1, 2003; 133(2): 885 - 892. [Abstract] [Full Text] [PDF]

				Y.-H. R. Ding, R. S. Ronimus, and H. W. Morgan Sequencing, Cloning, and High-Level Expression of the pfp Gene, Encoding a PPi-Dependent Phosphofructokinase from the Extremely Thermophilic Eubacterium Dictyoglomus thermophilum J. Bacteriol., August 15, 2000; 182(16): 4661 - 4666. [Abstract] [Full Text]

				P. H. Janssen Pathway of Glucose Catabolism by Strain VeGlc2, an Anaerobe Belonging to the Verrucomicrobiales Lineage of Bacterial Descent Appl. Envir. Microbiol., December 1, 1998; 64(12): 4830 - 4833. [Abstract] [Full Text]

				C. M. Fraser, S. J. Norris, G. M. Weinstock, O. White, G. G. Sutton, R. Dodson, M. Gwinn, E. K. Hickey, R. Clayton, K. A. Ketchum, et al. Complete Genome Sequence of Treponema pallidum, the Syphilis Spirochete Science, July 17, 1998; 281(5375): 375 - 388. [Abstract] [Full Text]

				B. Siebers, H.-P. Klenk, and R. Hensel PPi-Dependent Phosphofructokinase from Thermoproteus tenax, an Archaeal Descendant of an Ancient Line in Phosphofructokinase Evolution J. Bacteriol., April 15, 1998; 180(8): 2137 - 2143. [Abstract] [Full Text]