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David R. J. Palmer | doi.page

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David R. J. Palmer

Harvard University(US)University of Saskatchewan(CA)

Publications by Year

Research Areas

Enzyme Structure and Function, Enzyme Production and Characterization, Biochemical and Molecular Research, Phytase and its Applications, Carbohydrate Chemistry and Synthesis

Most-Cited Works

→ The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids(1996)304 cited
→ Unexpected Divergence of Enzyme Function and Sequence: “N-Acylamino Acid Racemase” Is o-Succinylbenzoate Synthase(1999)115 cited
→ Evolution of Enzymatic Activities in the Enolase Superfamily: Characterization of the (D)-Glucarate/Galactarate Catabolic Pathway in Escherichia coli(1998)84 cited
→ Succinylphosphonate Esters Are Competitive Inhibitors of MenD That Show Active-Site Discrimination between Homologous α-Ketoglutarate-Decarboxylating Enzymes(2010)43 cited
→ Methanogen Homoaconitase Catalyzes Both Hydrolyase Reactions in Coenzyme B Biosynthesis(2008)40 cited
→ A Previously Unrecognized Kanosamine Biosynthesis Pathway in Bacillus subtilis(2013)39 cited

→ The Lesser “Burden Borne” by o-Succinylbenzoate Synthase: An “Easy” Reaction Involving a Carboxylate Carbon Acid(2001)

33 cited

→ Steady-State Kinetics and Molecular Evolution of Escherichia coli MenD [(1R,6R)-2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate Synthase], an Anomalous Thiamin Diphosphate-Dependent Decarboxylase−Carboligase(2003)32 cited

→ Evolution of Enzymatic Activities in the Enolase Superfamily: Crystal Structure of (D)-Glucarate Dehydratase from Pseudomonas putida,(1998)26 cited

→ Biomimetic Design Results in a Potent Allosteric Inhibitor of Dihydrodipicolinate Synthase from Campylobacter jejuni(2016)25 cited