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Titolo:
Characterization of sulfate assimilation in marine algae focusing on the enzyme 5 '-adenylylsulfate reductase
Autore:
Gao, Y; Schofield, OME; Leustek, T;
Indirizzi:
Rutgers State Univ, Biotechnol Ctr Agr & Environm, New Brunswick, NJ 08901USA Rutgers State Univ New Brunswick NJ USA 08901 New Brunswick, NJ 08901USA Rutgers State Univ, Inst Marine & Coastal Sci, New Brunswick, NJ 08901 USARutgers State Univ New Brunswick NJ USA 08901 New Brunswick, NJ 08901 USA
Titolo Testata:
PLANT PHYSIOLOGY
fascicolo: 3, volume: 123, anno: 2000,
pagine: 1087 - 1096
SICI:
0032-0889(200007)123:3<1087:COSAIM>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIATOM SKELETONEMA-COSTATUM; NITROGEN; PLANTS; SYNTHETASE; TRANSPORT; SEEDLINGS; NITRATE; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Gao, Y Rutgers State Univ, Biotechnol Ctr Agr & Environm, New Brunswick, NJ 08901USA Rutgers State Univ New Brunswick NJ USA 08901 unswick, NJ 08901USA
Citazione:
Y. Gao et al., "Characterization of sulfate assimilation in marine algae focusing on the enzyme 5 '-adenylylsulfate reductase", PLANT PHYSL, 123(3), 2000, pp. 1087-1096

Abstract

5'-Adenylylsulfate (APS) reductase was characterized in diverse marine algae. A cDNA encoding APS reductase from Enteromorpha intestinalis (EAPR) wascloned by functional complementation of an Escherichia coli cysH mutant. The deduced amino acid sequence shows high homology with APS reductase (APR)from flowering plants. Based on the probable transit peptide cleavage sitethe mature protein is 45.7 kD. EAPR expressed as a His-tagged recombinant protein catalyzes reduced glutathione-dependent reduction of APS to sulfite, exhibiting a specific activity of approximately 40 mu mol min(-1) mg protein(-1) and Michealis-Menten kinetic constants of approximately 1.4 mM for reduced glutathione and approximately 6.5 mu M for APS. APR activity and expression were studied in relation to the production of 3-dimethylsulfoniopropionate (DMSP), a sulfonium compound produced by many marine algae. A diverse group of DMSP-producing species showed extremely high enzyme activity (up to 400 times that found in flowering plants). Antibodies raised against a conserved peptide of APR strongly cross-reacted with a protein of 45 kD in several chlorophytes but insignificantly with chromophytes. Ln the chlorophyte Tetraselmis sp., APR activity varies significantly during the culturecycle and does not follow the changes in cellular DMSP content. However, apositive correlation was found between cell-based APR activity and specific growth rate.

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Documento generato il 20/09/20 alle ore 09:20:46