GlutaredoxinV1, Main, Exploration, bibRecord, 000C46

The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity.

Identifieur interne : 000C46 ( Main/Exploration ); précédent : 000C45; suivant : 000C47

The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity.

Auteurs : Sung-Kun Kim [États-Unis] ; Varinnia Gomes ; Yu Gao ; Kala Chandramouli ; Michael K. Johnson ; David B. Knaff ; Thomas Leustek

Source :

Biochemistry [ 0006-2960 ] ; 2007.

RBID : pubmed:17209569

Descripteurs français

English descriptors

KwdEn :
- Algal Proteins (chemistry), Algal Proteins (genetics), Algal Proteins (metabolism), Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Base Sequence (MeSH), DNA, Algal (genetics), DNA, Bacterial (genetics), Kinetics (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases Acting on Sulfur Group Donors (chemistry), Oxidoreductases Acting on Sulfur Group Donors (genetics), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Protein Structure, Tertiary (MeSH), Pseudomonas aeruginosa (enzymology), Pseudomonas aeruginosa (genetics), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Spectrophotometry (MeSH), Ulva (enzymology), Ulva (genetics).
MESH :
- chemical , chemistry : Algal Proteins, Bacterial Proteins, Oxidoreductases Acting on Sulfur Group Donors, Recombinant Fusion Proteins.
- chemical , genetics : Algal Proteins, Bacterial Proteins, DNA, Algal, DNA, Bacterial, Oxidoreductases Acting on Sulfur Group Donors, Recombinant Fusion Proteins.
- chemical , metabolism : Algal Proteins, Bacterial Proteins, Oxidoreductases Acting on Sulfur Group Donors, Recombinant Fusion Proteins.
- enzymology : Pseudomonas aeruginosa, Ulva.
- genetics : Pseudomonas aeruginosa, Ulva.
- Amino Acid Sequence, Base Sequence, Kinetics, Models, Biological, Molecular Sequence Data, Oxidation-Reduction, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Spectrophotometry.

Abstract

5'-Adenylylsulfate (APS) reductase from Enteromorpha intestinalis (EiAPR) is composed of two domains that function together to reduce APS to sulfite. The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons from glutathione to the APS reduction site on the amino-terminal domain. To study the basis for the interdomain interaction, a heterologous system was constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR, was found to use both thioredoxin and glutathione as an electron donor for APS reduction. The ability to use glutathione was enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR. When the C domain was added as a separate component, it was much less efficient in conferring PaAPR with the ability to use glutathione as an electron donor, despite the fact that the separately expressed C domain functioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and electron donation to ribonucleotide reductase. These results suggest that the physical connection of the reductase and C domain on a single polypeptide is critical for the electron-transfer reaction. Moreover, the effect of Na2SO4 suggests that a water-ordering component of the reaction milieu is critical for the catalytic function of plant-type APS reductases by promoting the interdomain interaction.

DOI: 10.1021/bi0618971
PubMed: 17209569

Affiliations:

États-Unis

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

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Le document en format XML

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<term>Algal Proteins (genetics)</term>
<term>Algal Proteins (metabolism)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Base Sequence (MeSH)</term>
<term>DNA, Algal (genetics)</term>
<term>DNA, Bacterial (genetics)</term>
<term>Kinetics (MeSH)</term>
<term>Models, Biological (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (chemistry)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (genetics)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (metabolism)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Pseudomonas aeruginosa (enzymology)</term>
<term>Pseudomonas aeruginosa (genetics)</term>
<term>Recombinant Fusion Proteins (chemistry)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Ulva (enzymology)</term>
<term>Ulva (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (génétique)</term>
<term>ADN des algues (génétique)</term>
<term>Cinétique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Oxidoreductases acting on sulfur group donors (composition chimique)</term>
<term>Oxidoreductases acting on sulfur group donors (génétique)</term>
<term>Oxidoreductases acting on sulfur group donors (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Protéines d'algue (composition chimique)</term>
<term>Protéines d'algue (génétique)</term>
<term>Protéines d'algue (métabolisme)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Pseudomonas aeruginosa (enzymologie)</term>
<term>Pseudomonas aeruginosa (génétique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
<term>Ulva (enzymologie)</term>
<term>Ulva (génétique)</term>
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<term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Fusion Proteins</term>
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<term>Bacterial Proteins</term>
<term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Fusion Proteins</term>
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<term>Protéines d'algue</term>
<term>Protéines de fusion recombinantes</term>
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<term>ADN des algues</term>
<term>Oxidoreductases acting on sulfur group donors</term>
<term>Protéines bactériennes</term>
<term>Protéines d'algue</term>
<term>Protéines de fusion recombinantes</term>
<term>Pseudomonas aeruginosa</term>
<term>Ulva</term>
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<term>Protéines bactériennes</term>
<term>Protéines d'algue</term>
<term>Protéines de fusion recombinantes</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Kinetics</term>
<term>Models, Biological</term>
<term>Molecular Sequence Data</term>
<term>Oxidation-Reduction</term>
<term>Protein Structure, Tertiary</term>
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<term>Spectrophotometry</term>
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<term>Données de séquences moléculaires</term>
<term>Modèles biologiques</term>
<term>Oxydoréduction</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Spectrophotométrie</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">5'-Adenylylsulfate (APS) reductase from Enteromorpha intestinalis (EiAPR) is composed of two domains that function together to reduce APS to sulfite. The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons from glutathione to the APS reduction site on the amino-terminal domain. To study the basis for the interdomain interaction, a heterologous system was constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR, was found to use both thioredoxin and glutathione as an electron donor for APS reduction. The ability to use glutathione was enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR. When the C domain was added as a separate component, it was much less efficient in conferring PaAPR with the ability to use glutathione as an electron donor, despite the fact that the separately expressed C domain functioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and electron donation to ribonucleotide reductase. These results suggest that the physical connection of the reductase and C domain on a single polypeptide is critical for the electron-transfer reaction. Moreover, the effect of Na2SO4 suggests that a water-ordering component of the reaction milieu is critical for the catalytic function of plant-type APS reductases by promoting the interdomain interaction.</div>
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<Abstract><AbstractText>5'-Adenylylsulfate (APS) reductase from Enteromorpha intestinalis (EiAPR) is composed of two domains that function together to reduce APS to sulfite. The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons from glutathione to the APS reduction site on the amino-terminal domain. To study the basis for the interdomain interaction, a heterologous system was constructed in which the C domain of EiAPR was fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (PaAPR), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR, was found to use both thioredoxin and glutathione as an electron donor for APS reduction. The ability to use glutathione was enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR. When the C domain was added as a separate component, it was much less efficient in conferring PaAPR with the ability to use glutathione as an electron donor, despite the fact that the separately expressed C domain functioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and electron donation to ribonucleotide reductase. These results suggest that the physical connection of the reductase and C domain on a single polypeptide is critical for the electron-transfer reaction. Moreover, the effect of Na2SO4 suggests that a water-ordering component of the reaction milieu is critical for the catalytic function of plant-type APS reductases by promoting the interdomain interaction.</AbstractText>
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<tree><noCountry><name sortKey="Chandramouli, Kala" sort="Chandramouli, Kala" uniqKey="Chandramouli K" first="Kala" last="Chandramouli">Kala Chandramouli</name>
<name sortKey="Gao, Yu" sort="Gao, Yu" uniqKey="Gao Y" first="Yu" last="Gao">Yu Gao</name>
<name sortKey="Gomes, Varinnia" sort="Gomes, Varinnia" uniqKey="Gomes V" first="Varinnia" last="Gomes">Varinnia Gomes</name>
<name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name>
<name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name>
<name sortKey="Leustek, Thomas" sort="Leustek, Thomas" uniqKey="Leustek T" first="Thomas" last="Leustek">Thomas Leustek</name>
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<country name="États-Unis"><noRegion><name sortKey="Kim, Sung Kun" sort="Kim, Sung Kun" uniqKey="Kim S" first="Sung-Kun" last="Kim">Sung-Kun Kim</name>
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{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:17209569
   |texte=   The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity.
}}

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Serveur d'exploration sur la glutarédoxine

The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity.

The two-domain structure of 5'-adenylylsulfate (APS) reductase from Enteromorpha intestinalis is a requirement for efficient APS reductase activity.

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