1H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.
Identifieur interne : 000966 ( Main/Exploration ); précédent : 000965; suivant : 0009671H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.
Auteurs : Caifang Yu [République populaire de Chine] ; Bin Xia ; Changwen JinSource :
- Biomolecular NMR assignments [ 1874-270X ] ; 2011.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Arsenate Reductases.
- enzymologie : Synechocystis.
- Données de séquences moléculaires, Hydrogène, Isotopes de l'azote, Isotopes du carbone, Résonance magnétique nucléaire biomoléculaire, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Arsenate Reductases.
- enzymology : Synechocystis.
- Amino Acid Sequence, Carbon Isotopes, Hydrogen, Molecular Sequence Data, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular.
Abstract
Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.
DOI: 10.1007/s12104-010-9273-2
PubMed: 20960080
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20960080</PMID><DateCompleted><Year>2011</Year><Month>06</Month><Day>21</Day></DateCompleted><DateRevised><Year>2016</Year><Month>05</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1874-270X</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>1</Issue><PubDate><Year>2011</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Biomolecular NMR assignments</Title><ISOAbbreviation>Biomol NMR Assign</ISOAbbreviation></Journal><ArticleTitle>1H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.</ArticleTitle><Pagination><MedlinePgn>85-7</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12104-010-9273-2</ELocationID><Abstract><AbstractText>Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. 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