PoplarV1, Main, Exploration, bibRecord, 000D89

Mechanism(s) of action of heavy metals to investigate the regulation of plastidic glucose-6-phosphate dehydrogenase.

Identifieur interne : 000D89 ( Main/Exploration ); précédent : 000D88; suivant : 000D90

Mechanism(s) of action of heavy metals to investigate the regulation of plastidic glucose-6-phosphate dehydrogenase.

Auteurs : Alessia De Lillo [Italie] ; Manuela Cardi [Italie] ; Simone Landi [Italie] ; Sergio Esposito [Italie]

Source :

Scientific reports [ 2045-2322 ] ; 2018.

RBID : pubmed:30194387

Descripteurs français

KwdFr :
- Cinétique (MeSH), Glucose 6-phosphate dehydrogenase (composition chimique), Glucose 6-phosphate dehydrogenase (génétique), Métaux lourds (composition chimique), NADP (composition chimique), Populus (enzymologie), Populus (génétique), Protéines chloroplastiques (composition chimique), Protéines chloroplastiques (génétique), Sites de fixation (MeSH).
MESH :
- composition chimique : Glucose 6-phosphate dehydrogenase, Métaux lourds, NADP, Protéines chloroplastiques.
- enzymologie : Populus.
- génétique : Glucose 6-phosphate dehydrogenase, Populus, Protéines chloroplastiques.
- Cinétique, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites (MeSH), Chloroplast Proteins (chemistry), Chloroplast Proteins (genetics), Glucosephosphate Dehydrogenase (chemistry), Glucosephosphate Dehydrogenase (genetics), Kinetics (MeSH), Metals, Heavy (chemistry), NADP (chemistry), Populus (enzymology), Populus (genetics).
MESH :
- chemical , chemistry : Chloroplast Proteins, Glucosephosphate Dehydrogenase, Metals, Heavy, NADP.
- chemical , genetics : Chloroplast Proteins, Glucosephosphate Dehydrogenase.
- enzymology : Populus.
- genetics : Populus.
- Binding Sites, Kinetics.

Abstract

The regulation of recombinant plastidic glucose-6P dehydrogenase from Populus trichocarpa (PtP2-G6PDH - EC 1.1.1.49) was investigated by exposing wild type and mutagenized isoforms to heavy metals. Nickel and Cadmium caused a marked decrease in PtP2-G6PDH WT activity, suggesting their poisoning effect on plant enzymes; Lead (Pb⁺⁺) was substantially ineffective. Copper (Cu⁺⁺) and Zinc (Zn⁺⁺) exposition resulted in strongest decrease in enzyme activity, thus suggesting a physiological competition with Magnesium, a well-known activator of G6PDH activity. Kinetic analyses confirmed a competitive inhibition by Copper, and a mixed inhibition by (Cd⁺⁺). Mutagenized enzymes were differently affected by HMs: the reduction of disulfide (C¹⁷⁵-C¹⁸³) exposed the NADP⁺ binding sites to metals; C¹⁴⁵ participates to NADP⁺ cofactor binding; C¹⁹⁴ and C²⁴² are proposed to play a role in the regulation of NADP⁺/NADPH binding. Copper (and possibly Zinc) is able to occupy competitively Magnesium (Mg⁺⁺) sites and/or bind to NADP⁺, resulting in a reduced access of NADP⁺ sites on the enzyme. Hence, heavy metals could be used to describe specific roles of cysteine residues present in the primary protein sequence; these results are discussed to define the biochemical mechanism(s) of inhibition of plant plastidic G6PDH.

DOI: 10.1038/s41598-018-31348-y
PubMed: 30194387
PubMed Central: PMC6128849

Affiliations:

Italie

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000C69
to stream Main, to step Curation: 000C69

Le document en format XML

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<term>Glucosephosphate Dehydrogenase (genetics)</term>
<term>Kinetics (MeSH)</term>
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<term>Populus (génétique)</term>
<term>Protéines chloroplastiques (composition chimique)</term>
<term>Protéines chloroplastiques (génétique)</term>
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<front><div type="abstract" xml:lang="en">The regulation of recombinant plastidic glucose-6P dehydrogenase from Populus trichocarpa (PtP2-G6PDH - EC 1.1.1.49) was investigated by exposing wild type and mutagenized isoforms to heavy metals. Nickel and Cadmium caused a marked decrease in PtP2-G6PDH WT activity, suggesting their poisoning effect on plant enzymes; Lead (Pb<sup>++</sup>
) was substantially ineffective. Copper (Cu<sup>++</sup>
) and Zinc (Zn<sup>++</sup>
) exposition resulted in strongest decrease in enzyme activity, thus suggesting a physiological competition with Magnesium, a well-known activator of G6PDH activity. Kinetic analyses confirmed a competitive inhibition by Copper, and a mixed inhibition by (Cd<sup>++</sup>
). Mutagenized enzymes were differently affected by HMs: the reduction of disulfide (C<sup>175</sup>
-C<sup>183</sup>
) exposed the NADP<sup>+</sup>
 binding sites to metals; C<sup>145</sup>
 participates to NADP<sup>+</sup>
 cofactor binding; C<sup>194</sup>
 and C<sup>242</sup>
 are proposed to play a role in the regulation of NADP<sup>+</sup>
/NADPH binding. Copper (and possibly Zinc) is able to occupy competitively Magnesium (Mg<sup>++</sup>
) sites and/or bind to NADP<sup>+</sup>
, resulting in a reduced access of NADP<sup>+</sup>
 sites on the enzyme. Hence, heavy metals could be used to describe specific roles of cysteine residues present in the primary protein sequence; these results are discussed to define the biochemical mechanism(s) of inhibition of plant plastidic G6PDH.</div>
</front>
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<Abstract><AbstractText>The regulation of recombinant plastidic glucose-6P dehydrogenase from Populus trichocarpa (PtP2-G6PDH - EC 1.1.1.49) was investigated by exposing wild type and mutagenized isoforms to heavy metals. Nickel and Cadmium caused a marked decrease in PtP2-G6PDH WT activity, suggesting their poisoning effect on plant enzymes; Lead (Pb<sup>++</sup>
) was substantially ineffective. Copper (Cu<sup>++</sup>
) and Zinc (Zn<sup>++</sup>
) exposition resulted in strongest decrease in enzyme activity, thus suggesting a physiological competition with Magnesium, a well-known activator of G6PDH activity. Kinetic analyses confirmed a competitive inhibition by Copper, and a mixed inhibition by (Cd<sup>++</sup>
). Mutagenized enzymes were differently affected by HMs: the reduction of disulfide (C<sup>175</sup>
-C<sup>183</sup>
) exposed the NADP<sup>+</sup>
 binding sites to metals; C<sup>145</sup>
 participates to NADP<sup>+</sup>
 cofactor binding; C<sup>194</sup>
 and C<sup>242</sup>
 are proposed to play a role in the regulation of NADP<sup>+</sup>
/NADPH binding. Copper (and possibly Zinc) is able to occupy competitively Magnesium (Mg<sup>++</sup>
) sites and/or bind to NADP<sup>+</sup>
, resulting in a reduced access of NADP<sup>+</sup>
 sites on the enzyme. Hence, heavy metals could be used to describe specific roles of cysteine residues present in the primary protein sequence; these results are discussed to define the biochemical mechanism(s) of inhibition of plant plastidic G6PDH.</AbstractText>
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Mechanism(s) of action of heavy metals to investigate the regulation of plastidic glucose-6-phosphate dehydrogenase.

Mechanism(s) of action of heavy metals to investigate the regulation of plastidic glucose-6-phosphate dehydrogenase.

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