Induction of Positive Cooperativity by Amino Acid Replacements within the C-terminal Domain of Penicillium chrysogenum ATP Sulfurylase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
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3. The “regulatory” sulfhydryl group of Penicillium chrysogenum ATP sulfurylase
4. Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3'-phosphoadenosine-5'-phosphosulfate.
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1. Allosteric modulation of semicarbazide-sensitive amine oxidase activitiesin vitroby imidazoline receptor ligands;British Journal of Pharmacology;2004-10
2. Kinetic and Stability Properties of Penicillium chrysogenum ATP Sulfurylase Missing the C-terminal Regulatory Domain;Journal of Biological Chemistry;2004-02
3. Inversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements;Archives of Biochemistry and Biophysics;2004-01
4. A novel technique to evaluate interactions between Saccharomyces cerevisiae cell wall and mycotoxins: application to zearalenone;Biotechnology Letters;2003
5. Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum;Nature Structural Biology;2002-11-11
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