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Tytuł:
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Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation.
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Autorzy:
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Snášel J; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
Machová I; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
Šolínová V; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
Kašička V; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
Krečmerová M; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
Pichová I; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 2, 16610 Prague 6, Czech Republic.
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Źródło:
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International journal of molecular sciences [Int J Mol Sci] 2021 Feb 02; Vol. 22 (3). Date of Electronic Publication: 2021 Feb 02.
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Typ publikacji:
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Comparative Study; Journal Article
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Język:
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English
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Imprint Name(s):
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Original Publication: Basel, Switzerland : MDPI, [2000-
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MeSH Terms:
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Bacterial Proteins/*metabolism
Mycobacterium tuberculosis/*enzymology
Phosphofructokinases/*metabolism
Adenosine Diphosphate/metabolism ; Adenosine Diphosphate/pharmacology ; Adenosine Triphosphate/metabolism ; Adenosine Triphosphate/pharmacology ; Allosteric Regulation ; Bacterial Proteins/antagonists & inhibitors ; Catalysis ; Enzyme Induction ; Feedback, Physiological ; Fructosediphosphates/biosynthesis ; Fructosediphosphates/pharmacology ; Fructosephosphates/metabolism ; Fructosephosphates/pharmacology ; Gluconeogenesis ; Glycolysis ; Hexosephosphates/metabolism ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/metabolism ; Kinetics ; L-Lactate Dehydrogenase/metabolism ; Mycobacterium tuberculosis/drug effects ; Oxygen/pharmacology ; Phosphofructokinases/antagonists & inhibitors ; Pyruvate Kinase/metabolism ; Recombinant Proteins/metabolism ; Substrate Specificity
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References:
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Grant Information:
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CZ.02.1.01/0.0/16_019/000729 Ministerstvo Školství, Mládeže a Tělovýchovy; RVO 61388963 Akademie Věd České Republiky
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Contributed Indexing:
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Keywords: Mycobacterium tuberculosis; allosteric regulation; enzyme kinetics; glycolysis; phosphofructokinase A and B
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Substance Nomenclature:
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0 (Bacterial Proteins)
0 (Fructosediphosphates)
0 (Fructosephosphates)
0 (Hexosephosphates)
0 (Isoenzymes)
0 (Recombinant Proteins)
53798-20-2 (tagatose 6-phosphate)
61D2G4IYVH (Adenosine Diphosphate)
6814-87-5 (fructose-6-phosphate)
8L70Q75FXE (Adenosine Triphosphate)
EC 1.1.1.27 (L-Lactate Dehydrogenase)
EC 2.7.1 - (Phosphofructokinases)
EC 2.7.1.- (phosphofructokinase A protein, Mycobacterium tuberculosis)
EC 2.7.1.40 (Pyruvate Kinase)
M7522JYX1H (fructose-1,6-diphosphate)
S88TT14065 (Oxygen)
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Entry Date(s):
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Date Created: 20210205 Date Completed: 20210409 Latest Revision: 20231110
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Update Code:
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20240104
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PubMed Central ID:
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PMC7867265
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DOI:
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10.3390/ijms22031483
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PMID:
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33540748
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Tuberculosis (TB) remains one of the major health concerns worldwide. Mycobacterium tuberculosis (Mtb), the causative agent of TB, can flexibly change its metabolic processes during different life stages. Regulation of key metabolic enzyme activities by intracellular conditions, allosteric inhibition or feedback control can effectively contribute to Mtb survival under different conditions. Phosphofructokinase (Pfk) is one of the key enzymes regulating glycolysis. Mtb encodes two Pfk isoenzymes, Pfk A/Rv3010c and Pfk B/Rv2029c, which are differently expressed upon transition to the hypoxia-induced non-replicating state of the bacteria. While pfkB gene and protein expression are upregulated under hypoxic conditions, Pfk A levels decrease. Here, we present biochemical characterization of both Pfk isoenzymes, revealing that Pfk A and Pfk B display different kinetic properties. Although the glycolytic activity of Pfk A is higher than that of Pfk B, it is markedly inhibited by an excess of both substrates (fructose-6-phosphate and ATP), reaction products (fructose-1,6-bisphosphate and ADP) and common metabolic allosteric regulators. In contrast, synthesis of fructose-1,6-bisphosphatase catalyzed by Pfk B is not regulated by higher levels of substrates, and metabolites. Importantly, we found that only Pfk B can catalyze the reverse gluconeogenic reaction. Pfk B thus can support glycolysis under conditions inhibiting Pfk A function.