Phosphofructokinase of <i>Leishmania donovani</i> and <i>Leishmania braziliensis</i> and its Role in Glycolysis*

Berens, Randolph L.; Marr, J. Joseph

doi:10.1111/j.1550-7408.1977.tb00991.x

Cited by 20 publications

(15 citation statements)

References 19 publications

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“…3) [31] similar to the observation previously reported for the T. brucei enzyme [5]. The PFK activity in Leishmania species [32–34] and in T. borreli (J. Van Roy, F. Opperdoes, N. Chevalier & P. A. M. Michels, unpublished results) is also known to be ATP‐dependent.…”

Section: Analysis Of Kinetoplastid Pfk Genessupporting

confidence: 82%

“…No activity (less than 1%) was observed when PP i (at concentrations up to 5 m m ) was used as alternative phospho donor. As reported previously for PFK of T. brucei [7] and other Leishmania species [32], the activity of the enzyme depends hyperbolically on the concentration of ATP. The kinetic behaviour of the expressed PFK was determined as a function of fructose 6‐phosphate at fixed, saturated ATP concentration (1.0 m m ), and in the presence or absence of AMP and GDP (Fig.…”

Section: Kinetics Of Leishmania Pfksupporting

confidence: 61%

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Leishmania donovani phosphofructokinase

López

Chevalier

Hannaert

et al. 2002

European Journal of Biochemistry

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The characterization of the gene encoding Leishmania donovani phosphofructokinase (PFK) and the biochemical properties of the expressed enzyme are reported. L. donovani has a single PFK gene copy per haploid genome that encodes a polypeptide with a deduced molecular mass of 53 988 and a pI of 9.26. The predicted amino acid sequence contains a C-terminal tripeptide that conforms to an established signal for glycosome targeting. L. donovani PFK showed most sequence similarity to inorganic pyrophosphate (PP i )-dependent PFKs, despite being ATP-dependent. It thereby resembles PFKs from other Kinetoplastida such as Trypanosoma brucei, Trypanoplasma borreli (characterized in this study), and a PFK found in Entamoeba histolytica. It exhibited hyperbolic kinetics with respect to ATP whereas the binding of the other substrate, fructose 6-phosphate, showed slight positive cooperativity. PP i , even at high concentrations, did not have any effect. AMP acted as an activator of PFK, shifting its kinetics for fructose 6-phosphate from slightly sigmoid to hyperbolic, and increasing considerably the affinity for this substrate, whereas GDP did not have any effect. Modelling studies and site-directed mutagenesis were employed to shed light on the structural basis for the AMP effector specificity and on ATP/PP i specificity among PFKs.

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Section: Analysis Of Kinetoplastid Pfk Genessupporting

confidence: 82%

Section: Kinetics Of Leishmania Pfksupporting

confidence: 61%

Leishmania donovani phosphofructokinase

López

Chevalier

Hannaert

et al. 2002

European Journal of Biochemistry

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“…According to Berens and Marr (1977), PFK, which is the key regulatory enzyme in the glycolysis of many organisms, does not play an important role in Leishmania. PFK in Leishmania, and in all trypanosomatids studied, is very little aected by the typical eectors of this enzyme in most glycolytic systems (Cazzulo 1992).…”

Section: Discussionmentioning

confidence: 99%

Activity of key enzymes in glucose catabolism during the growth and metacyclogenesis of Leishmania infantum

Louassini¹,

Foulquié²,

Benı́tez³

et al. 1999

Parasitology Research

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This paper follows the development in the activity of the key enzymes of glycolysis and dehydrogenases of the pentose phosphate shunt throughout the in vitro growth and metacyclogenesis of two human strains of Leishmania infantum - one visceral (VL) and the other cutaneous (CL) - together with changes in the glucose, ammonium, and proton concentrations in the culture medium. In the first stage, ammonium was generated and no glucose was consumed. Later on, all the glucose was consumed and, finally, ammonium was generated again. The ammonium concentration increased 16- and 21-fold in cultures of VL and CL strains, respectively. The activities of the glycosomal enzymes hexokinase and phosphofructokinase differed in each strain, always being higher in CL than in VL and increasing throughout the culture period in CL while decreasing in VL. This probably indicates a different capability to adapt to the culture medium conditions. The activities of the pentose phosphate shunt enzymes examined indicate that 6-phosphogluconate dehydrogenase is possibly a rate-limiting enzyme for this pathway. Pyruvate kinase is a cytosolic control enzyme of glycolysis in trypanosomatids, and its activity decreased throughout the growth and differentiation of both strains of L. infantum, as occurs in other trypanosomatids. It was also observed that glucose catabolism was more active in the cutaneous strain than in the visceral one.

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“…This is consistent with a decrease in the rate of oxidation of ribose seen in most of the data in Table 111. The factors responsible for control of the carbon flow through the PPP and EMP remain to be determined, but control does not appear to reside at hexokinase, glucose-6-phosphate dehydrogenase (l), or phosphofructokinase (2).…”

Section: Discussionmentioning

confidence: 99%

“…Hart et al (1 1) found that not only glucose but also fatty acids stimulated the respiration of promastigotes but that amino acids did not appear to be used as energy substrates. Both Steiger & Meshnick (23) and Hart & Coombs (10) report, however, that glutamate is consumed at a rapid rate during growth while alanine is excreted, and there is evidence that in enriched growth media, amino acids are major substrates during the early and mid-log phases of growth (2,22). Hart et al (1 1) showed that the rate of oxygen uptake by L. mexicana promastigotes was about the same on a per mg protein basis as the amastigotes from which they were derived.…”

mentioning

confidence: 99%

Oxidation of Glucose, Ribose, Alanine, and Glutamate by Leishmania braziliensis panamensis1

Keegan

Sansone

Blum

1987

The Journal of Protozoology

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The metabolism of [1-14C]- and [6-14C]glucose, [1-14C]ribose, [1-14C]- and [U-14C]alanine, and [1-14C]- and [5-14C]glutamate by the promastigotes of Leishmania braziliensis panamensis was investigated in cells resuspended in Hanks' balanced salt solution supplemented with ribose, alanine, or glutamate. The ratio of 14CO2 produced from [1-14C]glucose to that from [6-14C]glucose ranged from about two to six, indicating appreciable carbon flow through the pentose phosphate pathway. A functional pentose phosphate pathway was further demonstrated by the production of 14CO2 from [1-14C]ribose although the rate of ribose oxidation was much lower than the rate of glucose oxidation. The rate of 14CO2 production from [1-14C]glucose was almost linear with time of incubation, whereas that of [6-14C]glucose accelerated, consistent with an increasing rate of flux through the Embden-Meyerhof pathway during incubation. Increasing the assay temperature from 26 degrees C to 34 degrees C had no appreciable effect on the rates or time courses of oxidation of either [1-14C]- or [6-14C]glucose or of [1-14C]ribose. Both alanine and glutamate were oxidized by L. b. panamensis, and at rates comparable to or appreciably greater than the rate of oxidation of glucose. The ratios of 14CO2 produced from [1-14C]- to [U-14C]alanine and from [1-14C]- to [5-14C]glutamate indicated that these compounds were metabolized via a functioning tricarboxylic acid cycle and that most of the label that entered the tricarboxylic acid cycle was oxidized to carbon dioxide.(ABSTRACT TRUNCATED AT 250 WORDS)

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Phosphofructokinase of Leishmania donovani and Leishmania braziliensis and its Role in Glycolysis*

Cited by 20 publications

References 19 publications

Leishmania donovani phosphofructokinase

Leishmania donovani phosphofructokinase

Activity of key enzymes in glucose catabolism during the growth and metacyclogenesis of Leishmania infantum

Oxidation of Glucose, Ribose, Alanine, and Glutamate by Leishmania braziliensis panamensis1

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