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Pregled bibliografske jedinice broj: 430975

Strombine dehydrogenase in the demosponge Suberites domuncula: Characterization and kinetic properties of the enzyme crucial for anaerobic metabolism


Pleše, Bruna; Schröder, Heinz C.; Grebenjuk, Vladislav A.; Wegener, Gerhard; Brandt, David; Natalio, Filipe; Müller, Werner E. G.
Strombine dehydrogenase in the demosponge Suberites domuncula: Characterization and kinetic properties of the enzyme crucial for anaerobic metabolism // Comparative Biochemistry and Physiology Part B, Biochemistry and Molecular Biology, 154 (2009), 1; 102-107 doi:10.1016/j.cbpb.2009.05.008 (međunarodna recenzija, članak, znanstveni)


Naslov
Strombine dehydrogenase in the demosponge Suberites domuncula: Characterization and kinetic properties of the enzyme crucial for anaerobic metabolism

Autori
Pleše, Bruna ; Schröder, Heinz C. ; Grebenjuk, Vladislav A. ; Wegener, Gerhard ; Brandt, David ; Natalio, Filipe ; Müller, Werner E. G.

Izvornik
Comparative Biochemistry and Physiology Part B, Biochemistry and Molecular Biology (1096-4959) 154 (2009), 1; 102-107

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Anaerobic metabolism; Demospongiae; Opine dehydrogenase; Strombine dehydrogenase; Suberites domuncula

Sažetak
Previously, the cDNA and the respective gene for a presumed tauropine dehydrogenase (TaDH) from Suberites domuncula (GenBank accession nos. AM712888, AM712889) had been annotated. The conclusion that the sequences encode a TaDH had been inferred from the 68% identity with the TaDH protein from the marine demosponge Halichondria japonica. However, subsequent enzymatic assays shown here indicate that the presumed S. domuncula opine dehydrogenase is in fact a strombine dehydrogenase (StDH). The enzyme StDH is highly specific for glycine and is inhibited by an excess of the substrate pyruvate. Besides kinetic data, we report in this study also on the predicted tertiary and quaternary structure of the sponge StDH. It is concluded that the dimer (75 kDa) has a novel structure, distinguishing it from other known marine invertebrate OpDHs that exist as monomers.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



POVEZANOST RADA


Ustanove
Institut "Ruđer Bošković", Zagreb

Autor s matičnim brojem:
Bruna Pleše, (315612)

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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