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Titolo:
Glutamine synthetase in marine algae: New surprises from an old enzyme
Autore:
Robertson, DL; Smith, GJ; Alberte, RS;
Indirizzi:
Clark Univ, Dept Biol, Worcester, MA 01610 USA Clark Univ Worcester MA USA 01610 niv, Dept Biol, Worcester, MA 01610 USA Moss Landing Marine Labs, Moss Landing, CA 95039 USA Moss Landing Marine Labs Moss Landing CA USA 95039 Landing, CA 95039 USA PhycoGen Inc, Portland, ME 04101 USA PhycoGen Inc Portland ME USA 04101PhycoGen Inc, Portland, ME 04101 USA
Titolo Testata:
JOURNAL OF PHYCOLOGY
fascicolo: 5, volume: 37, anno: 2001,
pagine: 793 - 795
SICI:
0022-3646(200110)37:5<793:GSIMAN>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIATOM SKELETONEMA-COSTATUM; GLNN GENE; SEQUENCE;
Keywords:
diatoms; evolution; glutamine synthetase; nitrogen metabolism; Skeletonema costatum;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Robertson, DL Clark Univ, Dept Biol, 950 Main St, Worcester, MA 01610 USA Clark Univ 950 Main St Worcester MA USA 01610 , MA 01610 USA
Citazione:
D.L. Robertson et al., "Glutamine synthetase in marine algae: New surprises from an old enzyme", J PHYCOLOGY, 37(5), 2001, pp. 793-795

Abstract

Glutamine synthetase (GS), which catalyzes the formation of glutamine fromammonium and glutamate in the presence of ATP, is encoded by three distinct gene families: GSI, GSII, and GSIII. Genes encoding GSI are found in the Bacteria and Archaea, whereas GSII genes are found in eukaryotes and a few species of Bacteria. Members of the third family, GSIII, have been described from a limited number of bacteria; however, recent biochemical and molecular data suggest that this type of enzyme is broadly distributed among the algae. Peptide fragments obtained from GS purified from the marine diatom Skeletonema costatum (Greville) Cleve are 77% identical to a partial sequence of GSIII from Chaetoceros compressum Lauder, which permits the unambiguous assignment of the biochemically characterized enzyme to the GSIII gene family. The N-terminal sequence was 43% identical to the GSIII-like enzyme purified from the haptophyte Emiliania huxleyi (Lohm. ) Hay et Miller and several residues were conserved among bacterial and eukaryotic GSIII enzymes. The presence of genes encoding GSIII in diatoms and haptophytes indicates that this enzyme family is more broadly distributed in eukaryotes than previously suspected.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 10:08:47