NAD + -dependent Formate Dehydrogenase from Plants
Identifieur interne : 000F99 ( Ncbi/Checkpoint ); précédent : 000F98; suivant : 001000NAD + -dependent Formate Dehydrogenase from Plants
Auteurs : A. A. Alekseeva ; S. S. Savin ; V. I. TishkovSource :
- Acta Naturae [ 2075-8251 ] ; 2011.
Abstract
NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochondria. Formate dehydrogenase activity was first discovered as early as in 1921 in plant; however, until the past decade FDHs from plants had been considerably less studied than the enzymes from microorganisms. This review summarizes the recent results on studying the physiological role, properties, structure, and protein engineering of plant formate dehydrogenases.
Url:
PubMed: 22649703
PubMed Central: 3347622
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">NAD <sup>+</sup> -dependent Formate Dehydrogenase from Plants
</title><author><name sortKey="Alekseeva, A A" sort="Alekseeva, A A" uniqKey="Alekseeva A" first="A. A." last="Alekseeva">A. A. Alekseeva</name><affiliation><nlm:aff id="AF1">Chemistry Department, Lomonosov Moscow State University</nlm:aff><wicri:noCountry code="subfield">Lomonosov Moscow State University</wicri:noCountry></affiliation><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author><author><name sortKey="Savin, S S" sort="Savin, S S" uniqKey="Savin S" first="S. S." last="Savin">S. S. Savin</name><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author><author><name sortKey="Tishkov, V I" sort="Tishkov, V I" uniqKey="Tishkov V" first="V. I." last="Tishkov">V. I. Tishkov</name><affiliation><nlm:aff id="AF1">Chemistry Department, Lomonosov Moscow State University</nlm:aff><wicri:noCountry code="subfield">Lomonosov Moscow State University</wicri:noCountry></affiliation><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22649703</idno><idno type="pmc">3347622</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347622</idno><idno type="RBID">PMC:3347622</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">001347</idno><idno type="wicri:Area/Pmc/Curation">001345</idno><idno type="wicri:Area/Pmc/Checkpoint">000E27</idno><idno type="wicri:Area/Ncbi/Merge">000F99</idno><idno type="wicri:Area/Ncbi/Curation">000F99</idno><idno type="wicri:Area/Ncbi/Checkpoint">000F99</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">NAD <sup>+</sup> -dependent Formate Dehydrogenase from Plants
</title><author><name sortKey="Alekseeva, A A" sort="Alekseeva, A A" uniqKey="Alekseeva A" first="A. A." last="Alekseeva">A. A. Alekseeva</name><affiliation><nlm:aff id="AF1">Chemistry Department, Lomonosov Moscow State University</nlm:aff><wicri:noCountry code="subfield">Lomonosov Moscow State University</wicri:noCountry></affiliation><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author><author><name sortKey="Savin, S S" sort="Savin, S S" uniqKey="Savin S" first="S. S." last="Savin">S. S. Savin</name><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author><author><name sortKey="Tishkov, V I" sort="Tishkov, V I" uniqKey="Tishkov V" first="V. I." last="Tishkov">V. I. Tishkov</name><affiliation><nlm:aff id="AF1">Chemistry Department, Lomonosov Moscow State University</nlm:aff><wicri:noCountry code="subfield">Lomonosov Moscow State University</wicri:noCountry></affiliation><affiliation><nlm:aff id="AF2">Innovations and High Technologies MSU Ltd</nlm:aff></affiliation><affiliation><nlm:aff id="AF3">Bach Institute of Biochemistry, Russian Academy of Sciences</nlm:aff><wicri:noCountry code="subfield">Russian Academy of Sciences</wicri:noCountry></affiliation></author></analytic><series><title level="j">Acta Naturae</title><idno type="ISSN">2075-8251</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>NAD<sup>+</sup>-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs
in nature. FDH consists of two identical subunits and contains neither
prosthetic groups nor metal ions. This type of FDH was found in different
microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and
plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs
localize in mitochondria. Formate dehydrogenase activity was first discovered as
early as in 1921 in plant; however, until the past decade FDHs from plants had
been considerably less studied than the enzymes from microorganisms. This review
summarizes the recent results on studying the physiological role, properties,
structure, and protein engineering of plant formate dehydrogenases.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Rodionov, Yu V" uniqKey="Rodionov Y">Yu.V. Rodionov</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ferry, J G" uniqKey="Ferry J">J.G. Ferry</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Vinals, C" uniqKey="Vinals C">C. Vinals</name></author><author><name sortKey="Depiereux, E" uniqKey="Depiereux E">E. Depiereux</name></author><author><name sortKey="Feytmans, E" uniqKey="Feytmans E">E. Feytmans</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tishkov, V I" uniqKey="Tishkov V">V.I. Tishkov</name></author><author><name sortKey="Galkin, A G" uniqKey="Galkin A">A.G. Galkin</name></author><author><name sortKey="Egorov, A M" uniqKey="Egorov A">A.M. 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Savin</name><name sortKey="Tishkov, V I" sort="Tishkov, V I" uniqKey="Tishkov V" first="V. I." last="Tishkov">V. I. Tishkov</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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