PhanerochaeteV1, Main, Exploration, bibRecord, 000315

Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium.

Identifieur interne : 000315 ( Main/Exploration ); précédent : 000314; suivant : 000316

Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium.

Auteurs : Zhongshan Wang [République populaire de Chine] ; Guangjun Wang ; Quanju Xiang ; Yizheng Zhang ; Haiyan Wang

Source :

Biotechnology letters [ 1573-6776 ] ; 2014.

RBID : pubmed:24557072

Descripteurs français

English descriptors

KwdEn :
- Adenosine Triphosphatases (MeSH), Amino Acid Sequence (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Protein Structure, Tertiary (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Sulfurtransferases (chemistry), Sulfurtransferases (genetics), Sulfurtransferases (metabolism).
MESH :
- chemical , chemistry : Fungal Proteins, Recombinant Proteins, Sulfurtransferases.
- chemical , genetics : Fungal Proteins, Recombinant Proteins, Sulfurtransferases.
- chemical , metabolism : Fungal Proteins, Recombinant Proteins, Sulfurtransferases.
- chemical : Adenosine Triphosphatases.
- enzymology : Phanerochaete.
- genetics : Escherichia coli, Phanerochaete, Protein Structure, Tertiary.
- metabolism : Escherichia coli.
- Amino Acid Sequence, Molecular Sequence Data, Mutagenesis, Site-Directed, Sequence Alignment.

Abstract

A sulfurtransferase gene (PcSft) with a coding region of 546 bp was cloned from the filamentous white-rot fungus Phanerochaere chrysosporium. The 181-amino acid protein contains a highly conserved "Rhodanese-like" domain and an ATP-binding site, with a molecular weight of 20.68 kDa. Semi-quantitative RT-PCR showed that the selective expression of PcSft was involved in secondary metabolism. The recombinant PcSFT protein was expressed in E. coli BL21 (DE3) and purified by Ni(2+)-chelating and size-exclusion chromatography. Its ATPase and sulfurtransferase (SFT) activities were indentified and characterized. PcSFT exhibited optimal SFT activity at pH 8 and 30 °C as well as stability at 20 °C and pH 8. The enzyme's stability under different temperature and pH P. indicates a potential usefulness for the detoxification of cyanide in the environment.

DOI: 10.1007/s10529-013-1444-7
PubMed: 24557072

Affiliations:

République populaire de Chine

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

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Le document en format XML

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<author><name sortKey="Xiang, Quanju" sort="Xiang, Quanju" uniqKey="Xiang Q" first="Quanju" last="Xiang">Quanju Xiang</name>
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<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
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<front><div type="abstract" xml:lang="en">A sulfurtransferase gene (PcSft) with a coding region of 546 bp was cloned from the filamentous white-rot fungus Phanerochaere chrysosporium. The 181-amino acid protein contains a highly conserved "Rhodanese-like" domain and an ATP-binding site, with a molecular weight of 20.68 kDa. Semi-quantitative RT-PCR showed that the selective expression of PcSft was involved in secondary metabolism. The recombinant PcSFT protein was expressed in E. coli BL21 (DE3) and purified by Ni(2+)-chelating and size-exclusion chromatography. Its ATPase and sulfurtransferase (SFT) activities were indentified and characterized. PcSFT exhibited optimal SFT activity at pH 8 and 30 °C as well as stability at 20 °C and pH 8. The enzyme's stability under different temperature and pH P. indicates a potential usefulness for the detoxification of cyanide in the environment.</div>
</front>
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<Abstract><AbstractText>A sulfurtransferase gene (PcSft) with a coding region of 546 bp was cloned from the filamentous white-rot fungus Phanerochaere chrysosporium. The 181-amino acid protein contains a highly conserved "Rhodanese-like" domain and an ATP-binding site, with a molecular weight of 20.68 kDa. Semi-quantitative RT-PCR showed that the selective expression of PcSft was involved in secondary metabolism. The recombinant PcSFT protein was expressed in E. coli BL21 (DE3) and purified by Ni(2+)-chelating and size-exclusion chromatography. Its ATPase and sulfurtransferase (SFT) activities were indentified and characterized. PcSFT exhibited optimal SFT activity at pH 8 and 30 °C as well as stability at 20 °C and pH 8. The enzyme's stability under different temperature and pH P. indicates a potential usefulness for the detoxification of cyanide in the environment.</AbstractText>
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Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium.

Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki