WhiteRotV1, Main, Exploration, bibRecord, 001391

Cloning of a cDNA encoding a NAD-dependent formate dehydrogenase involved in oxalic acid metabolism from the white-rot fungus Ceriporiopsis subvermispora and its gene expression analysis.

Identifieur interne : 001391 ( Main/Exploration ); précédent : 001390; suivant : 001392

Cloning of a cDNA encoding a NAD-dependent formate dehydrogenase involved in oxalic acid metabolism from the white-rot fungus Ceriporiopsis subvermispora and its gene expression analysis.

Auteurs : Tomoki Watanabe [Japon] ; Tadashi Fujiwara ; Toshiaki Umezawa ; Mikio Shimada ; Takefumi Hattori

Source :

FEMS microbiology letters [ 0378-1097 ] ; 2008.

RBID : pubmed:18177307

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Bacterial (chemistry), DNA, Bacterial (genetics), DNA, Complementary (genetics), Escherichia coli (genetics), Formate Dehydrogenases (chemistry), Formate Dehydrogenases (genetics), Formate Dehydrogenases (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Oxalic Acid (metabolism), Polyporales (enzymology), Polyporales (genetics), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , chemistry : DNA, Bacterial, Formate Dehydrogenases, Fungal Proteins.
- chemical , genetics : DNA, Bacterial, DNA, Complementary, Formate Dehydrogenases, Fungal Proteins, Recombinant Proteins.
- enzymology : Polyporales.
- genetics : Escherichia coli, Polyporales.
- chemical , metabolism : Formate Dehydrogenases, Fungal Proteins, Oxalic Acid, Recombinant Proteins.
- Amino Acid Sequence, Cloning, Molecular, Gene Expression, Molecular Sequence Data, Molecular Weight, Sequence Analysis, DNA, Sequence Homology, Amino Acid.

Abstract

The authors have proposed previously that intracellular degradation of oxalic acid via formate to CO(2) occurs in the white-rot fungus Ceriporiopsis subvermispora. The formate degradation is catalyzed by NAD-dependent formate dehydrogenase (CsFDH). In this study, two cDNAs named CsFDH1 and CsFDH2 encoding CsFDH were cloned. Each cDNA consisting of 1077 bp encodes a mature protein composed of 358 amino acid residues. The amino acid sequences of the deduced CsFDH1 and CsFDH2 showed 99% identity to each other. The predicted molecular mass for each was 39.3 kDa, which was similar to that of CsFDH purified from the vegetative mycelia of Ceriporiopsis subvermispora (purified-CsFDH). The recombinant CsFDH1 and CsFDH2 expressed by Escherichia coli showed FDH activity with similar characteristics to the purified CsFDH. However, the amount of CsFDH1 transcript from the vegetative mycelia was 236-691 times greater than that of CsFDH2. Therefore, the results strongly suggest that CsFDH1, as compared with CsFDH2, predominantly contributes to the production of the purified CsFDH.

DOI: 10.1111/j.1574-6968.2007.01022.x
PubMed: 18177307

Affiliations:

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Le document en format XML

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<author><name sortKey="Umezawa, Toshiaki" sort="Umezawa, Toshiaki" uniqKey="Umezawa T" first="Toshiaki" last="Umezawa">Toshiaki Umezawa</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>DNA, Bacterial (chemistry)</term>
<term>DNA, Bacterial (genetics)</term>
<term>DNA, Complementary (genetics)</term>
<term>Escherichia coli (genetics)</term>
<term>Formate Dehydrogenases (chemistry)</term>
<term>Formate Dehydrogenases (genetics)</term>
<term>Formate Dehydrogenases (metabolism)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Oxalic Acid (metabolism)</term>
<term>Polyporales (enzymology)</term>
<term>Polyporales (genetics)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Sequence Analysis, DNA (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (composition chimique)</term>
<term>ADN bactérien (génétique)</term>
<term>ADN complémentaire (génétique)</term>
<term>Acide oxalique (métabolisme)</term>
<term>Analyse de séquence d'ADN (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Escherichia coli (génétique)</term>
<term>Expression des gènes (MeSH)</term>
<term>Formate dehydrogenases (composition chimique)</term>
<term>Formate dehydrogenases (génétique)</term>
<term>Formate dehydrogenases (métabolisme)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Polyporales (enzymologie)</term>
<term>Polyporales (génétique)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Bacterial</term>
<term>Formate Dehydrogenases</term>
<term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Bacterial</term>
<term>DNA, Complementary</term>
<term>Formate Dehydrogenases</term>
<term>Fungal Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>ADN bactérien</term>
<term>Formate dehydrogenases</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Polyporales</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Polyporales</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
<term>Polyporales</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN bactérien</term>
<term>ADN complémentaire</term>
<term>Escherichia coli</term>
<term>Formate dehydrogenases</term>
<term>Polyporales</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Formate Dehydrogenases</term>
<term>Fungal Proteins</term>
<term>Oxalic Acid</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide oxalique</term>
<term>Formate dehydrogenases</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Cloning, Molecular</term>
<term>Gene Expression</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Sequence Analysis, DNA</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term>
<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Expression des gènes</term>
<term>Masse moléculaire</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The authors have proposed previously that intracellular degradation of oxalic acid via formate to CO(2) occurs in the white-rot fungus Ceriporiopsis subvermispora. The formate degradation is catalyzed by NAD-dependent formate dehydrogenase (CsFDH). In this study, two cDNAs named CsFDH1 and CsFDH2 encoding CsFDH were cloned. Each cDNA consisting of 1077 bp encodes a mature protein composed of 358 amino acid residues. The amino acid sequences of the deduced CsFDH1 and CsFDH2 showed 99% identity to each other. The predicted molecular mass for each was 39.3 kDa, which was similar to that of CsFDH purified from the vegetative mycelia of Ceriporiopsis subvermispora (purified-CsFDH). The recombinant CsFDH1 and CsFDH2 expressed by Escherichia coli showed FDH activity with similar characteristics to the purified CsFDH. However, the amount of CsFDH1 transcript from the vegetative mycelia was 236-691 times greater than that of CsFDH2. Therefore, the results strongly suggest that CsFDH1, as compared with CsFDH2, predominantly contributes to the production of the purified CsFDH.</div>
</front>
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Cloning of a cDNA encoding a NAD-dependent formate dehydrogenase involved in oxalic acid metabolism from the white-rot fungus Ceriporiopsis subvermispora and its gene expression analysis.

Cloning of a cDNA encoding a NAD-dependent formate dehydrogenase involved in oxalic acid metabolism from the white-rot fungus Ceriporiopsis subvermispora and its gene expression analysis.

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Descripteurs français

English descriptors

Abstract

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