Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.

The replacement of Arg-54 by Ala in the active site of Escherichia coli aspartate transcarbamoylase causes a 17,000-fold loss of activity but does not significantly influence the binding of substrates or substrate analogs (Stebbins, J.W., Xu, W., & Kantrowitz, E.R., 1989, Biochemistry 28, 2592-2...

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Hlavní autoři: Stebbins, J. W., Robertson, D. E., Roberts, M. F., Stevens, R. C., Lipscomb, W. N., Kantrowitz, E. R.
Médium: Artigo
Jazyk:Inglês
Vydáno: Cold Spring Harbor Laboratory Press 1992
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Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142124/
https://ncbi.nlm.nih.gov/pubmed/1303763
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