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The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.

The X-ray structure of the Escherichia coli aspartate transcarbamoylase with the bisubstrate analog phosphonacetyl-L-aspartate (PALA) bound shows that PALA interacts with Lys84 from an adjacent catalytic chain. To probe the function of Lys84, site-specific mutagenesis was used to convert Lys84 to al...

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Bibliografiset tiedot
Päätekijät: Macol, C., Dutta, M., Stec, B., Tsuruta, H., Kantrowitz, E. R.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: Cold Spring Harbor Laboratory Press 1999
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Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144362/
https://ncbi.nlm.nih.gov/pubmed/10386880
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