Phosphofructokinase in the mantle of the sea mussel <i>Mytilus galloprovincialis</i> Lmk.

Villamarı́n, J.Antonio; Rodríguez-Torres, Ana María; Ibarguren, Izaskun; Ramos-Martı́nez, Juan Ignacio

doi:10.1002/jez.1402550304

Cited by 13 publications

(3 citation statements)

References 18 publications

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“…Auxiliary enzymes were desalted as described (3). After two minutes, the reaction was started by the addition of 5-10 ~1 of purified phosphofructokinase, and the activity was determined by measuring the linear decrease in absorbance at 340 nm using a Philips PU 8700 spectrophotometer.…”

Section: Introductionmentioning

confidence: 99%

“…However, the enzyme from the mollusc is not affected by a number of classic mammalian PFK modulators, such Correpondence to: J.A. Villamarin (3,4). In addition to its allosteric regulation, phosphofructokinase from mussel mantle tissue can be phosphorylated in vitro by cAMP-dependent protein kinase (cAPK) from bovine heart, which notably alters its kinetic and regulatory properties (5).…”

Section: Introductionmentioning

confidence: 99%

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cAMP‐dependent phosphorylation activates phosphofructokinase from mantle tissue of the mollusc Mytilus galloprovincialis. Identification of the phosphorylated site

et al. 1997

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Phosphofructokinase from mantle tissue of the sea mussel Mytilus galloprovincialis was phosphorylated in vitro by a protein kinase isolated from the same tissue, homologous to mammalian cAMP‐dependent protein kinase; the maximal level of phosphorylation achieved was around 1 mol of Pi/mol of phosphofructokinase subunit. The covalent incorporation of phosphate leads to a notable increase in the enzyme activity assayed at near‐physiological concentrations of substrates and allosteric modulators and neutral pH. Tryptic digestion of labeled phosphofructokinase released a phosphopeptide whose sequence was Lys‐Asp‐Ser(P)‐Ile‐Trp‐Ile‐Gln‐Thr‐Gly‐Arg. This sequence showed high homology with the phosphopeptides from other invertebrates whose phosphofructokinase is also activated by cAMP‐dependent phosphorylation.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

cAMP‐dependent phosphorylation activates phosphofructokinase from mantle tissue of the mollusc Mytilus galloprovincialis. Identification of the phosphorylated site

et al. 1997

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“…Moreover, ammonium ions act as an activator of the PFK from mantle-tissue of M. galloprovincialis (Villamarin 1990) and from other sources (Uyeda 1979).…”

Section: Introductionmentioning

confidence: 99%

Effect of fructose 2,6-bisphosphate and ammonium ions on AMP-mediated activation of phosphofructokinase from the posterior adductor muscle of the sea musselMytilus galloprovincialis

Villamarín

Ramos-Martı́nez

1990

Mar. Biol.

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Abstract.The effects of different modulators on the phosphofructokinase (PFK) activity from the posterior adductor muscle of the sea mussel Mytilus galloprovincialis Lmk. were studied in mussels collected from N.W. Spain in spring/summer, 1988. Adenosine monophosphate (AMP), fructose 2,6-bisphosphate (Fru 2,6-P2) and ammonium ions individually activated PFK. AMP and Fru 2,6-P 2 reduced ATP-mediated inhibition and the value of S0.5 [concentration of fructose 6-phosphate (Fru 6-P) for half-maximum velocity], whereas ammonium ions increased Vma x (the rate at the saturating concentrations of Fru 6-P). Fru 2,6-P2 and ammonium ions both enhanced the effect of AMP, but in different ways: Fru 2,6-P e reduced apparent K m for AMP (concentration of AMP for half-maximum activation) without affecting Vma x, whereas ammonium ions only altered the latter. The sharp increases in the values of S0.5 for Fru 6-P and of apparent K,, for AMP that are caused by a drop in pH were reduced by the presence of Fru 2,6-P z, but not by ammonium ions. The results shows that Fru 2,6-P2 may contribute to maintain the PFK activity during hypoxia periods, whereas ammonium ions (in the presence of high AMP concentrations) may activate the enzyme during the first few hours of post-hypoxia re-immersion.

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In VivoPhosphorylation of Phosphofructokinase from the Bivalve MolluskMytilus galloprovincialis

Fernández

Cao

1998

Archives of Biochemistry and Biophysics

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Phosphofructokinase in the mantle of the sea mussel Mytilus galloprovincialis Lmk.

Cited by 13 publications

References 18 publications

cAMP‐dependent phosphorylation activates phosphofructokinase from mantle tissue of the mollusc Mytilus galloprovincialis. Identification of the phosphorylated site

cAMP‐dependent phosphorylation activates phosphofructokinase from mantle tissue of the mollusc Mytilus galloprovincialis. Identification of the phosphorylated site

Effect of fructose 2,6-bisphosphate and ammonium ions on AMP-mediated activation of phosphofructokinase from the posterior adductor muscle of the sea musselMytilus galloprovincialis

In VivoPhosphorylation of Phosphofructokinase from the Bivalve MolluskMytilus galloprovincialis

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