Reference on EC 2.7.2.8 - acetylglutamate kinase and Organism(s) Synechococcus elongatus and UniProt Accession Q6V1L5

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Maheswaran, M.; Urbanke, C.; Forchhammer, K.

Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942

J. Biol. Chem.

279

55202-55210

2004

Synechococcus elongatus

Llacer, J.L.; Contreras, A.; Forchhammer, K.; Marco-Marin, C.; Gil-Ortiz, F.; Maldonado, R.; Fita, I.; Rubio, V.

The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine

Proc. Natl. Acad. Sci. USA

104

17644-17649

2007

Synechococcus elongatus (Q6V1L5), Synechococcus elongatus

Beez, S.; Fokina, O.; Herrmann, C.; Forchhammer, K.

N-acetyl-L-glutamate kinase (NAGK) from oxygenic phototrophs: P(II) signal transduction across domains of life reveals novel insights in NAGK control

J. Mol. Biol.

389

748-758

2009

Synechococcus elongatus, Arabidopsis thaliana (Q9SCL7), Arabidopsis thaliana

Fokina, O.; Chellamuthu, V.R.; Zeth, K.; Forchhammer, K.

A novel signal transduction protein P(II) variant from Synechococcus elongatus PCC 7942 indicates a two-step process for NAGK-P(II) complex formation

J. Mol. Biol.

399

410-421

2010

Synechococcus elongatus