Role of zinc ion for catalytic activity in d-serine dehydratase from Saccharomyces cerevisiae
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2011.08451.x/fullpdf
Reference25 articles.
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2. D-Serine dehydratase from Escherichia coli- DNA-sequence and identification of catalytically inactive glycine to aspartic-acid variants;Marceau;J Biol Chem,1988
3. The glycine-rich region of Escherichia coli D-serine dehydratase - altered interactions with pyridoxal 5’-phosphate produced by substitution of aspartic-acid for glycine;Marceau;J Biol Chem,1988
4. Disruption of active-site interactions with pyridoxal 5’-phosphate and substrates by conservative replacements in the glycine-rich loop of Escherichia coli D-serine dehydratase;Marceau;J Biol Chem,1990
5. Crystal structures of open and closed forms of D-serine deaminase from Salmonella typhimurium- implications on substrate specificity and catalysis;Bharath;FEBS J,2011
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