Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni

2020 ◽  
Vol 98 (4) ◽  
pp. 518-524
Author(s):  
Adnan Ayna ◽  
Peter C.E. Moody
Keyword(s):  
Campylobacter Jejuni ◽  
Cooperative Control ◽  
Enteric Pathogen ◽  
Glycolytic Pathway ◽  
Type I ◽  
Fructose 1,6 Bisphosphatase ◽  
Futile Cycling ◽  
Amp Inhibition ◽  
Pathway Flux ◽  
Limited Sensitivity

The glycolytic pathway of the enteric pathogen Campylobacter jejuni is incomplete; the absence of phosphofructokinase means that the suppression of futile cycling at this point in the glycolytic–gluconeogenic pathway might not be required, and therefore the mechanism for controlling pathway flux is likely to be quite different or absent. In this study, the characteristics of fructose-1,6-bisphosphatase (FBPase) of C. jejuni are described and the regulation of this enzyme is compared with the equivalent enzymes from organisms capable of glycolysis. The enzyme is insensitive to AMP inhibition, unlike other type I FBPases. Campylobacter jejuni FBPase also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme’s activity found in type I FBPases appears to have been lost.

Campylobacter Infection

PEDIATRICS ◽  
1983 ◽  
Vol 72 (3) ◽  
pp. 437-437
Author(s):  
STANFORD T. SHULMAN ◽  
DONALD MOEL
Keyword(s):  
Hemolytic Uremic Syndrome ◽  
Campylobacter Jejuni ◽  
Enteric Pathogen ◽  
Bloody Diarrhea ◽  
Early Symptom ◽  
White Girl ◽  
Mother And Daughter ◽  
Uremic Syndrome ◽  
Campylobacter Infection

To the Editor.— Chamovitz et al1 recently reported the occurrence of hemolytic-uremia syndrome with evidence of Campylobacter jejuni infection in both a mother and daughter. Although they indicated that there were no previous reports of the association of this enteric pathogen with hemolytic-uremic syndrome, we must point out the report of Denneberg et al,2 who noted this association in 1982. In addition, we have recently treated a 22-month-old white girl with classic hemolytic-uremic syndrome who had bloody diarrhea as an early symptom.

Different Sensitivities of Mutants and Chimeric Forms of Human Muscle and Liver Fructose- 1,6-Bisphosphatases towards AMP

2003 ◽  
Vol 384 (1) ◽  
pp. 51-58 ◽  
Author(s):  
D. Rakus ◽  
H. Tillmann ◽  
R. Wysocki ◽  
S. Ulaszewski ◽  
K. Eschrich ◽  
...  
Keyword(s):  
Liver Enzyme ◽  
Human Liver ◽  
Human Muscle ◽  
Wild Type ◽  
Muscle Enzyme ◽  
Double Mutation ◽  
Binding Domains ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition ◽  
Acid Exchange

Abstract AMP is an allosteric inhibitor of human muscle and liver fructose-1,6-bisphosphatase (FBPase). Despite strong similarity of the nucleotide binding domains, the muscle enzyme is inhibited by AMP approximately 35 times stronger than liver FBPase: I0.5 for muscle and for liver FBPase are 0.14 uM and 4.8 uM, respectively. Chimeric human muscle (L50M288) and chimeric human liver enzymes (M50L288), in which the N-terminal residues (1-50) were derived from the human liver and human muscle FBPases, respectively, were inhibited by AMP 2-3 times stronger than the wild-type liver enzyme. An amino acid exchange within the Nterminal region of the muscle enzyme towards liver FBPase (Lys20→Glu) resulted in 13-fold increased I0.5 values compared to the wild-type muscle enzyme. However, the opposite exchanges in the liver enzyme (Glu20→Lys and double mutation Glu19→Asp/Glu20→Lys) did not change the sensitivity for AMP inhibition of the liver mutant (I0.5 value of 4.9 uM). The decrease of sensitivity for AMP of the muscle mutant Lys20→Glu, as well as the lack of changes in the inhibition by AMP of liver mutants Glu20→Lys and Glu19→Asp/Glu20→Lys, suggest a different mechanism of AMP binding to the muscle and liver enzyme.

Regulation of phosphoenolpyruvate carboxykinase and pyruvate kinase in Saccharomyces cerevisiae grown in the presence of glycolytic and gluconeogenic carbon sources and the role of mitochondrial function on gluconeogenesis

1986 ◽  
Vol 32 (12) ◽  
pp. 969-972 ◽  
Author(s):  
Albert J. Wilson ◽  
J. K. Bhattacharjee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Pyruvate Kinase ◽  
Growth Medium ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Carbon Sources ◽  
Absolute Requirement ◽  
Fructose 1,6 Bisphosphatase ◽  
Futile Cycling ◽  
Respiratory Deficient

Phosphoenolpyruvate carboxykinase (PEPCKase) and pyruvate kinase (PKase) were measured in Saccharomyces cerevisiae grown in the presence of glycolytic and gluconeogenic carbon sources. The PEPCKase activity was highest in ethanol-grown cells. However, high PEPCKase activity was also observed in cells grown in 1% glucose, especially as compared with the activity of sucrose-, maltose-, or galactose-grown cells. Activity was first detected after 12 h when glucose was exhausted from the growth medium. The PKase activity was very high in glucose-grown cells; considerable activity was also present in ethanol- and pyruvate-grown cells. The absolute requirement of respiration for gluconeogenesis was demonstrated by the absence or significantly low levels of PEPCKase and fructose-1,6-bisphosphatase activities observed in respiratory deficient mutants, as well as in wild-type S. cerevisiae cells grown in the presence of glucose and antimycin A or chloramphenicol. Obligate glycolytic and gluconeogenic enzymes were present sumultaneously only in stationary phase cells, but not in exponential phase cells; hence futile cycling could not occur in log phase cells regardless of the presence of carbon source in the growth medium.

scholarly journals The C1-C2 interface residue lysine 50 of pig kidney fructose-1,6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition

2000 ◽  
Vol 267 (8) ◽  
pp. 2242-2251 ◽  
Author(s):  
Juan G. Cárcamo ◽  
Alejandro J. Yañez ◽  
Heide C. Ludwig ◽  
Oscar León ◽  
Rodrigo O. Pinto ◽  
...  
Keyword(s):  
Crucial Role ◽  
Signal Transmission ◽  
Interface Residue ◽  
Pig Kidney ◽  
Fructose 1,6 Bisphosphatase ◽  
Amp Inhibition

scholarly journals Campylobacter jejuni FlpA Binds Fibronectin and Is Required for Maximal Host Cell Adherence

2009 ◽  
Vol 192 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Michael E. Konkel ◽  
Charles L. Larson ◽  
Rebecca C. Flanagan
Keyword(s):  
Amino Acids ◽  
Epithelial Cells ◽  
Campylobacter Jejuni ◽  
Type Strain ◽  
Wild Type Strain ◽  
Major Constituent ◽  
Enzyme Linked Immunosorbent Assay ◽  
Type I ◽  
Wild Type ◽  
Type Iii

ABSTRACT Campylobacter jejuni is one of the most frequent bacterial causes of food-borne gastrointestinal disease in developed countries. Previous work indicates that the binding of C. jejuni to human intestinal cells is crucial for host colonization and disease. Fibronectin (Fn), a major constituent of the extracellular matrix, is a ∼250-kDa glycoprotein present at regions of cell-to-cell contact in the intestinal epithelium. Fn is composed of three types of repeating units: type I (∼45 amino acids), type II (∼60 amino acids), and type III (∼90 amino acids). The deduced amino acid sequence of C. jejuni flpA (Cj1279c) contains at least three Fn type III domains. Based on the presence of the Fn type III domains, we hypothesized that FlpA contributes to the binding of C. jejuni to human INT 407 epithelial cells and Fn. We assessed the contribution of FlpA in C. jejuni binding to host cells by in vitro adherence assays with a C. jejuni wild-type strain and a C. jejuni flpA mutant and binding of purified FlpA protein to Fn by enzyme-linked immunosorbent assay (ELISA). Adherence assays revealed the binding of the C. jejuni flpA mutant to INT 407 epithelial cells was significantly reduced compared with that for a wild-type strain. In addition, rabbit polyclonal serum generated against FlpA blocked C. jejuni adherence to INT 407 cells in a concentration-dependent manner. Binding of FlpA to Fn was found to be dose dependent and saturable by ELISA, demonstrating the specificity of the interaction. Based on these data, we conclude that FlpA mediates C. jejuni attachment to host epithelial cells via Fn binding.

scholarly journals The Unique Phospholipidome of the Enteric Pathogen Campylobacter jejuni: Lysophosholipids Are Required for Motility at Low Oxygen Availability

2020 ◽  
Vol 432 (19) ◽  
pp. 5244-5258 ◽  
Author(s):  
Xuefeng Cao ◽  
Jos F.H.M. Brouwers ◽  
Linda van Dijk ◽  
Chris H.A. van de Lest ◽  
Craig T. Parker ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Oxygen Availability ◽  
Enteric Pathogen ◽  
Low Oxygen

Metabolism of the acutely ischemic dog heart. II. Interpretation of a model

1979 ◽  
Vol 236 (1) ◽  
pp. R31-R39
Author(s):  
D. Garfinkel ◽  
M. J. Achs
Keyword(s):  
Computer Model ◽  
Glycolytic Enzymes ◽  
Glycolytic Pathway ◽  
Muscle Proteins ◽  
Dog Heart ◽  
Phosphohexose Isomerase ◽  
Glycolytic Oscillations ◽  
Pathway Flux ◽  
Reducing Equivalents

The glycolytic oscillations occurring in an acutely ischemic dog heart are analyzed with a computer model. The major regulations of the glycolytic pathway flux occur at phosphohexose isomerase, which is inhibited by accumulated pentose shunt intermediates; at phosphorylase, which shapes the first cycle of the oscillation; and at aldolase, which shapes the last two cycles. Aldolase is not under normal substrate control. Its activity, and that of some subsequent glycolytic enzymes, appears to be regulated by known interactions with the muscle proteins. The mitochondria become reduced as a result of anoxia, and their metabolism reorganizes to export rather than import reducing equivalents. It is in general feasible to account for the behavior of this preparation in terms of the known metabolism of less severely perturbed hearts, especially (but not completely) in terms of effects of anoxia. The reasons for the inapplicability of the crossover theorem previously used to analyze this preparation are described.

scholarly journals Sialoadhesin Promotes Rapid Proinflammatory and Type I IFN Responses to a Sialylated Pathogen, Campylobacter jejuni

2012 ◽  
Vol 189 (5) ◽  
pp. 2414-2422 ◽  
Author(s):  
Mariliis Klaas ◽  
Cornelia Oetke ◽  
Leanne E. Lewis ◽  
Lars P. Erwig ◽  
Astrid P. Heikema ◽  
...  
Keyword(s):  
Campylobacter Jejuni ◽  
Type I ◽  
Type I Ifn

scholarly journals Inactivation precedes changes in allosteric properties and conformation of d-glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-bisphosphatase during denaturation by guanidinium chloride

1994 ◽  
Vol 303 (1) ◽  
pp. 241-245 ◽  
Author(s):  
R F Jiang ◽  
C L Tsou
Keyword(s):  
Conformational Changes ◽  
Enzyme Molecule ◽  
Guanidinium Chloride ◽  
Fructose 1,6 Bisphosphatase ◽  
Enzyme Molecules ◽  
Amp Inhibition ◽  
Allosteric Properties

It has been shown that inactivation of several enzymes precedes overall conformational changes of the enzyme molecules as a whole during denaturation [Tsou (1993) Science, 262, 380-381]. However, the relation between inactivation, loss of allosteric properties of oligomeric enzymes and unfolding of the enzyme molecule during denaturation remain little explored. These have now been compared for D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose-1,6-bisphosphatase (FruP2ase) during denaturation by guanidinium chloride (GdmCl). GAPDH is completely inactivated at 0.3 M GdmCl but at this GdmCl concentration it still binds NAD+ with negative co-operativity. At 0.4 M GdmCl, inactivation of FruP2ase reaches completion whereas its allosteric properties, including the heterotropic effect of AMP inhibition and K+ activation with positive co-operativity, are only partially affected. Much higher GdmCl concentrations are required to bring about unfolding of the overall structures of both enzymes.

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