Structural insights for the substrate recognition mechanism of LL-diaminopimelate aminotransferase

The enzymes involved in the lysine biosynthetic pathway have long been considered to be attractive targets for novel antibiotics due to the absence of this pathway in humans. Recently, a novel pyridoxal 5′-phosphate (PLP) dependent enzyme called ll-diaminopimelate aminotransferase ( ll-DAP-AT) was i...

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Veröffentlicht in:	Biochimica et biophysica acta 2011-11, Vol.1814 (11), p.1528-1533
Hauptverfasser:	Watanabe, Nobuhiko, James, Michael N.G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminotransferase antibiotics Arabidopsis thaliana Bacterial Proteins - chemistry Bacterial Proteins - metabolism biochemical pathways Chlamydia crystal structure Crystallography, X-Ray Diaminopimelate enzymes enzymology glutamic acid humans lysine Lysine biosynthesis Models, Molecular Protein Conformation pyridoxal Pyridoxal-5′-phosphate Substrate Specificity Transaminases - chemistry Transaminases - metabolism
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