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Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain.
Cross PJ, Allison TM, Dobson RC, Jameson GB, Parker EJ. Cross PJ, et al. Proc Natl Acad Sci U S A. 2013 Feb 5;110(6):2111-6. doi: 10.1073/pnas.1217923110. Epub 2013 Jan 23. Proc Natl Acad Sci U S A. 2013. PMID: 23345433 Free PMC article.
The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition.
Castell A, Short FL, Evans GL, Cookson TV, Bulloch EM, Joseph DD, Lee CE, Parker EJ, Baker EN, Lott JS. Castell A, et al. Biochemistry. 2013 Mar 12;52(10):1776-87. doi: 10.1021/bi301387m. Epub 2013 Feb 28. Biochemistry. 2013. PMID: 23363292
Amino-acid substitutions at the domain interface affect substrate and allosteric inhibitor binding in α-isopropylmalate synthase from Mycobacterium tuberculosis.
Huisman FH, Squire CJ, Parker EJ. Huisman FH, et al. Biochem Biophys Res Commun. 2013 Apr 5;433(2):249-54. doi: 10.1016/j.bbrc.2013.02.092. Epub 2013 Mar 13. Biochem Biophys Res Commun. 2013. PMID: 23500460
Neisseria meningitidis expresses a single 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine.
Cross PJ, Pietersma AL, Allison TM, Wilson-Coutts SM, Cochrane FC, Parker EJ. Cross PJ, et al. Protein Sci. 2013 Aug;22(8):1087-99. doi: 10.1002/pro.2293. Epub 2013 Jun 27. Protein Sci. 2013. PMID: 23754471 Free PMC article.
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