The inhibition of citrate synthase by adenosine triphosphate

Jangaard, N. O.; Unkeless, Jay C.; Atkinson, Daniel E.

doi:10.1016/0005-2744(68)90177-0

Cited by 83 publications

(22 citation statements)

References 38 publications

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“…0.8 mM) observed in the present study for yeast citrate synthase in situ might suggest that the availability of acetyl-CoA is a regulatory factor or that some unknown control mechanism operating in vivo can lower this parameter. Although, as mentioned above in the Introduction, Our results emphasize the complexities of enzyme citrate synthase isolated from various sources has been regulation and underline the fact that despite the reported to be inhibited by ATP, low concentrations numerous regulatory phenomena which have been of Mg*+ have been found to reduce this inhibition [5,6,14,151. This finding has itself detracted from the appeal of ATP inhibition as a physiological control.…”

Section: Resultssupporting

confidence: 54%

In situ regulation of yeast citrate synthase. Absence of ATP inhibition observed in vitro

Weitzman

Hewson

1973

FEBS Letters

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Section: Resultssupporting

confidence: 54%

In situ regulation of yeast citrate synthase. Absence of ATP inhibition observed in vitro

Weitzman

Hewson

1973

FEBS Letters

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“…Inhibition of bacterial citrate synthase activity by ATP, and in most cases also by ADP, has been reported in Escherichia coli (Weitzman, 1966;Jangaard et al, 1968), Rhodopseudomonas spheroides (Borriss & Ohman, 1972) and two thiobacilli (Taylor, 1970). However, the high concentrations of ATP required, and the fact that ADP also inhibits, makes it unlikely that this inhibition is physiologically important in bacteria (cf.…”

Section: Resultsmentioning

confidence: 99%

“…Borriss & Ohman, 1972). Inhibition of citrate synthase activity by lower concentrations of ATP has been observed in yeast (Hathaway & Atkinson, 1965), animals (Hathaway & Atkinson, 1965;Jangaard et al, 1968;Shepherd & Garland, 1966;Kosicki & Lee, 1966) and plants (Bogin & Wallace, 1966). This could represent a feedback control mechanism, as ATP can be considered another end product of the catabolic function of the tricarboxylic acid cycle.…”

Section: Resultsmentioning

confidence: 99%

Regulation of citrate synthase activity in methylotrophs by reduced nicotinamide-adenine dinucleotide, adenine nucleotides and 2-oxoglutarate

Colby¹,

Zatman²

1975

Biochemical Journal

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“…Isocitrate dehydrogenase is directly inhibited by NADH [38,39], but the activity of citrate synthase is influenced by the concentration of oxaloacetate , because the normal level in the mitochondrial compartment is calculated to be well below the K , value [40,41]. The level of oxaloacetate has been suggested to decrease because of the ethanol-induced shift in the malate/ oxaloacetate redox pair [4,9,10].…”

Section: Discussionmentioning

confidence: 99%

Role of the Redox State in Ethanol‐Induced Suppression of Citrate‐Cycle Flux in the Perfused Liver of Normal, Hyper‐ and Hypothyroid Rats

Lindros¹

1972

European Journal of Biochemistry

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1. The mechanism of the ethanol-induced suppression of the citric acid cycle has been studied by single-passage perfusion of livers from normal, triiodothyronine-treated and propylthiouraciltreated rats.2. Ethanol oxidation increased the lactate/pyruvate ratio in the perfusion medium to about 50 and depressed the 14C0, formation from [ l-14C]acetate and [l-14C]hexanoate (taken to reflect citrate cycle flux) by 6701, and 600/,, respectively, in normal livers. I n the livers of the hyperthyroid animals ethanol suppressed [1-l4C]acetate oxidation by 22O/, and [1-l4C]hexanoate oxidation by 34O/,, and the lactatelpyruvate ratio was only increased to about 20. I n the hypothyroid group ethanol enhanced the lactate/pyruvate ratio slightly more than in the controls and suppressed t,he oxidation of acetate and hexanoate by 79 and 620/,, respectively.3. Hepatic ethanol elimination was slightly slower in the hyper-and hypothyroid groups than in the controls. Hexanoate (1 mM) stimulated oxygen uptake in all groups but inhibited ethanol oxidation by 45O/, in the hyperthyroid group and only by 1 8 O / , in the hypothyroid group. Pyruvate, on the other hand, stimulated ethanol elimination only slightly in the hyperthyroid group, by about 50°/, in the controls and by about 70°/, in the hypothyroid group.4. Oxidation of acetate and hexanoate was also depressed by acetaldehyde. This effect was potentiated by pyrazole, which blocked the reduction of acetaldehyde and caused an increased shift in the lactatelpyruvate ratio, thus indicating that acetaldehyde also affects the citric acid cycle by causing a shift in the redox state. 5. A highly significant correlation was observed between the effect of ethanol on the output of 14C0, from the labelled substrates and the shift in the lactate/pyruvate ratio. Experiments with different input levels of lactate and pyruvate demonstrated that the citric acid cycle is susceptible to the fall in pyruvate resulting from the shift in the redox state during ethanol oxidation.

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The inhibition of citrate synthase by adenosine triphosphate

Cited by 83 publications

References 38 publications

In situ regulation of yeast citrate synthase. Absence of ATP inhibition observed in vitro

In situ regulation of yeast citrate synthase. Absence of ATP inhibition observed in vitro

Regulation of citrate synthase activity in methylotrophs by reduced nicotinamide-adenine dinucleotide, adenine nucleotides and 2-oxoglutarate

Role of the Redox State in Ethanol‐Induced Suppression of Citrate‐Cycle Flux in the Perfused Liver of Normal, Hyper‐ and Hypothyroid Rats

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