Partial purification and characterization of pyruvate, orthophosphate dikinase from Rhodospirillum rubrum

Ernst, Steffen; Budde, Raymond J.A.; Chollet, Raymond

doi:10.1128/jb.165.2.483-488.1986

Cited by 14 publications

(4 citation statements)

References 27 publications

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“…This enzyme has been found in plants, protozoa and several bacteria (Benziman & Palgi, 1970 ;Buchanan, 1974;Ernst et al, 1986;Evans & Wood, 1968, 1971Hatch & Slack, 1968;Matsuoka, 1995;Petzel et al, The GenBanWEMBLaccession numbersforpod-5, pod-6and the 6amHl pod gene fragment reported in this paper are U61377, U61376 and U61378, respectively.…”

Section: Introductionsupporting

confidence: 51%

“…Pyruvate orthophosphate dikinase (PPDK, EC 2.7.9.1) catalyses the reversible reaction : pyruvate + ATP + P i ⇋ phosphoenolpyruvate (PEP) +AMP + PP i (Evans & Wood, 1968; Hatch & Slack, 1968; Reeves et al, 1968). This enzyme has been found in plants, protozoa and several bacteria (Benziman & Palgi, 1970 ; Buchanan, 1974; Ernst et al, 1986; Evans & Wood, 1968, 1971; Hatch & Slack, 1968; Matsuoka, 1995; Petzel et al, 1989; Reeves, 1968, 1971; Reeves et al, 1968; Schwitzguebel & Ettlinger, 1979).…”

Section: Introductionmentioning

confidence: 99%

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Increased pyruvate orthophosphate dikinase activity results in an alternative gluconeogenic pathway in Rhizobium (Sinorhizobium) meliloti

1997

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The formation of phosphoenolpyruvate (PEP) is a major step in the gluconeogenic pathway in which tricarboxylic acid (TCA) cycle intermediates are converted to hexose sugars. In Rhizobium (now Sinorhizobium) meliloti this step is catalysed by the enzyme PEP carboxykinase (PCK) which converts oxaloacetate to PEP. R. meliloti Pck-mutants grow very poorly with TCA cycle intermediates as the sole source of carbon. Here, the isolation and mapping of suppressor mutations which allow Pck-mutants to grow on succinate and other TCA cycle intermediates is reported. Tn5 insertions which abolished the suppressor phenotype and mapped to the suppressor locus were located within the pod gene encoding pyruvate orthophosphate dikinase (PPDK). Strains carrying suppressor mutations had increased PPDK activity compared to the wild-type. The suppressor phenotype was dependent on the combined activities of malic enzyme and PPDK, which thus represent an alternative route for the formation of PEP in R. meliloti. PPDK activity was not required for symbiotic N2 fixation.

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Section: Introductionsupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

Increased pyruvate orthophosphate dikinase activity results in an alternative gluconeogenic pathway in Rhizobium (Sinorhizobium) meliloti

1997

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“…In bacteria (Ernst, Budde and Chollet 1986 ; Ciupka and Gohlke 2017 ) and archaea (Tjaden et al . 2006 ), PPdK appears to be active in homodimeric form, whereas for C4 plants it typically functions optimally as a homotetramer (Shirahashi, Hayakawa and Sugiyama 1978 ; Ohta, Ishida and Usami 2004 ).…”

Section: The Different Enzymes Of the Ppo-nodementioning

confidence: 99%

The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism

Koendjbiharie

Kranenburg

Kengen

2020

FEMS Microbiology Reviews

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At the junction between the glycolysis and the tricarboxylic acid cycle—as well as various other metabolic pathways—lies the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (PPO-node). These three metabolites form the core of a network involving at least eleven different types of enzymes, each with numerous subtypes. Obviously, no single organism maintains each of these eleven enzymes; instead, different organisms possess different subsets in their PPO-node, which results in a remarkable degree of variation, despite connecting such deeply conserved metabolic pathways as the glycolysis and the tricarboxylic acid cycle. The PPO-node enzymes play a crucial role in cellular energetics, with most of them involved in (de)phosphorylation of nucleotide phosphates, while those responsible for malate conversion are important redox enzymes. Variations in PPO-node therefore reflect the different energetic niches that organisms can occupy. In this review, we give an overview of the biochemistry of these eleven PPO-node enzymes. We attempt to highlight the variation that exists, both in PPO-node compositions, as well as in the roles that the enzymes can have within those different settings, through various recent discoveries in both bacteria and archaea that reveal deviations from canonical functions.

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“…Pyruvate kinase (EC 2.7.1.40) was assayed by the procedure of Bucher & Pfleiderer (1955). (viii) Pyruvate orthophosphate dikinase (EC 2.7.9.1) was assayed by the procedure of Ernst et al (1986). (ix) Lactate dehydrogenase (EC 1 .…”

Section: E T H O D Smentioning

confidence: 99%

Presence of Anaplerotic Reactions and Transamination, and the Absence of the Tricarboxylic Acid Cycle in Mollicutes

Manolukas

Barile²,

Chandler³

et al. 1988

Microbiology

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Cell extracts of the fermentative Mollicutes Acholeplasma laidlawii B-PG9, Acholeplasma morum S2, Mycoplasma capricolum 14, Mycoplasma gallisepticum S6, Mycoplasma pneumoniae FH, Mycoplasma hyopneumoniae J and M. genitalium G-37, and the non-fermentative Mycoplasma hominis PG-21, Mycoplasma hominis 1620 and Mycoplasma bovigenitalium PG-11 were examined for 39 cytoplasmic enzyme activities associated with the tricarboxylic acid (TCA) cycle, transamination, anaplerotic reactions and other enzyme activities at the pyruvate locus. Malate dehydrogenase (EC 4.2.1.2) was the only TCA-cycle-associated enzyme activity detected and it was found only in the eight Mycoplasma species. Aspartate aminotransferase (EC 2.6.1.1) activity was detected in all Mollicutes tested except M. gallisepticum S6. Malate synthetase (EC 4.1.3.2) activity, in the direction of malate formation, was found in the eight Mycoplasma species, but not in any of the Acholeplasma species. Phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31) was detected in the direction of oxaloacetate (OAA) formation in both Acholeplasma species, but not in any of the Mycoplasma species. Pyruvate carboxylase (EC 6.4.1.1), pyruvate kinase (EC 2.7.1.40), pyruvate dehydrogenase (EC 1.2.4.1) and lactate dehydrogenase (EC 1.1.1.27) activities were found in all ten Mollicutes tested. No activities were detected in any of the ten Mollicutes for aspartase (EC 4.3.1.1), malic enzyme (EC 1.1.1.40), PEP carboxytransphosphorylase (EC 4.1.1.38), PEP carboxykinase (EC 4.1.1.32) or pyruvate orthophosphate dikinase (EC 2.7.9.1). In these TCA-cycle-deficient Mollicutes the pyruvate-OAA locus may be a point of linkage for the carbons of glycolysis, lipid synthesis, nucleic acid synthesis and certain amino acids. CO2 fixation appears obligatory in the Acholeplasma species and either CO2 fixation or malate synthesis appears obligatory in the Mycoplasma species.

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Partial purification and characterization of pyruvate, orthophosphate dikinase from Rhodospirillum rubrum

Cited by 14 publications

References 27 publications

Increased pyruvate orthophosphate dikinase activity results in an alternative gluconeogenic pathway in Rhizobium (Sinorhizobium) meliloti

Increased pyruvate orthophosphate dikinase activity results in an alternative gluconeogenic pathway in Rhizobium (Sinorhizobium) meliloti

The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism

Presence of Anaplerotic Reactions and Transamination, and the Absence of the Tricarboxylic Acid Cycle in Mollicutes

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