The acid phosphatase Pho5 of Saccharomyces cerevisiae is not involved in polyphosphate breakdown

Андреева, Н. И.; Ledova, L. A.; Ryasanova, L. P.; Kulakovskaya, T. V.; Eldarov, M. A.

doi:10.1007/s12223-019-00702-6

Cited by 6 publications

(3 citation statements)

References 33 publications

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“…Previous experimental studies reported that the type 5 repressible APs like K. lactis AP recycled P i from extracellular nucleotides but had negligible reactivity toward polyP chains. , Accordingly, our simulations revealed the absence of a water molecule in the active site of K. lactis AP to mediate the formation of the precatalytic complex with polyP, despite the interaction of polyP with the positively charged active site residues (R58 and R62 and H338) in both yeast APs (i.e., K.…”

Section: Resultsmentioning

confidence: 56%

“…60 Previous experimental studies reported that the type 5 repressible APs like K. lactis AP recycled P i from extracellular nucleotides but had negligible reactivity toward polyP chains. 61,62 Accordingly, our simulations revealed the absence of a water molecule in the active site of K. lactis AP to mediate the formation of the precatalytic complex with polyP, despite the interaction of polyP with the positively charged active site residues (R58 and R62 and H338) in both yeast APs (i.e., K. lactis AP and S. cerevisiae AP) (Figure 4C and Supporting Information, Appendix G). However, in the S. cerevisiae AP, a favorable precatalytic complex was formed due to the close distance (<4.5 Å) of a middle phosphate in polyP to the His nuc and Asp PD and a water molecule (Figure 4C and Supporting Information, Appendix G).…”

Section: Molecular Simulations Reveal Substrate Orientation In the Ac...mentioning

confidence: 99%

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Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases

Solhtalab

Moller

et al. 2022

Environ. Sci. Technol.

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Among ubiquitous phosphorus (P) reserves in environmental matrices are ribonucleic acid (RNA) and polyphosphate (polyP), which are, respectively, organic and inorganic P-containing biopolymers. Relevant to P recycling from these biopolymers, much remains unknown about the kinetics and mechanisms of different acid phosphatases (APs) secreted by plants and soil microorganisms. Here we investigated RNA and polyP dephosphorylation by two common APs, a plant purple AP (PAP) from sweet potato and a fungal phytase from Aspergillus niger. Trends of δ18O values in released orthophosphate during each enzyme-catalyzed reaction in 18O-water implied a different extent of reactivity. Subsequent enzyme kinetics experiments revealed that A. niger phytase had 10-fold higher maximum rate for polyP dephosphorylation than the sweet potato PAP, whereas the sweet potato PAP dephosphorylated RNA at a 6-fold faster rate than A. niger phytase. Both enzymes had up to 3 orders of magnitude lower reactivity for RNA than for polyP. We determined a combined phosphodiesterase-monoesterase mechanism for RNA and terminal phosphatase mechanism for polyP using high-resolution mass spectrometry and 31P nuclear magnetic resonance, respectively. Molecular modeling with eight plant and fungal AP structures predicted substrate binding interactions consistent with the relative reactivity kinetics. Our findings implied a hierarchy in enzymatic P recycling from P-polymers by phosphatases from different biological origins, thereby influencing the relatively longer residence time of RNA versus polyP in environmental matrices. This research further sheds light on engineering strategies to enhance enzymatic recycling of biopolymer-derived P, in addition to advancing environmental predictions of this P recycling by plants and microorganisms.

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Section: Resultsmentioning

confidence: 56%

Section: Molecular Simulations Reveal Substrate Orientation In the Ac...mentioning

confidence: 99%

Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases

Solhtalab

Moller

et al. 2022

Environ. Sci. Technol.

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“…All four APases share a high homology (over 80% at the amino acid level). Pho5p, a major phosphate‐repressible APase, dephosphorylates a wide range of low‐molecular‐weight compounds, such as glucose 6‐phosphate, nucleotides, and ATP [13,14]. Pho3p has a high affinity for thiamine phosphate and produces orthophosphate (orthoP) and thiamine as substrates for uptake [15].…”

Section: Figmentioning

confidence: 99%

Secreted acid phosphatases maintain replicative lifespan via inositol polyphosphate metabolism in budding yeast

et al. 2021

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Secreted acid phosphatases (APases) dephosphorylate extracellular organic phosphate compounds to supply inorganic phosphate (Pi) to maintain cellular functions. Here, we show that APases are necessary to maintain a normal replicative lifespan in Saccharomyces cerevisiae. Deletion of all four APase genes shortened the lifespan in yeast strains on synthetic media (irrespective of the concentrations of Pi in the media), but it did not affect the intracellular ortho‐ and polyphosphate levels. Deletion of inositol‐pentakisphosphate 2‐kinase (IPK1), which encodes inositol‐pentakisphosphate 2‐kinase, restored the lifespan in APase‐null mutants, and IPK1 overexpression shortened the lifespan in wild‐type strains. Overexpression of inositol hexakisphosphate (IP6) and heptakisphosphate kinases, KCS1 and VIP1, recovered the lifespan in APase‐null mutants. Thus, yeast APases modulate the replicative lifespan, probably through dephosphorylation of intracellular IP6.

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Quantitative analysis of phosphate accumulation in PHO regulatory system-mutant strains of Saccharomyces cerevisiae

et al. 2023

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The acid phosphatase Pho5 of Saccharomyces cerevisiae is not involved in polyphosphate breakdown

Cited by 6 publications

References 33 publications

Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases

Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases

Secreted acid phosphatases maintain replicative lifespan via inositol polyphosphate metabolism in budding yeast

Quantitative analysis of phosphate accumulation in PHO regulatory system-mutant strains of Saccharomyces cerevisiae

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