Sumit Chakraborty

Affiliations: 
Weill Cornell Medical College, New York, NY, United States 
Area:
tuberculosis, enzyme catalysis
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"Sumit Chakraborty"
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Publications

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Chakraborty S, Gruber T, Barry CE, et al. (2013) Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis. Science (New York, N.Y.). 339: 88-91
Balakrishnan A, Nemeria NS, Chakraborty S, et al. (2012) Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step. Journal of the American Chemical Society. 134: 18644-55
Balakrishnan A, Paramasivam S, Chakraborty S, et al. (2012) Solid-state nuclear magnetic resonance studies delineate the role of the protein in activation of both aromatic rings of thiamin. Journal of the American Chemical Society. 134: 665-72
Li P, Chakraborty S, Stubbe J. (2009) Detection of covalent and noncovalent intermediates in the polymerization reaction catalyzed by a C149S class III polyhydroxybutyrate synthase. Biochemistry. 48: 9202-11
Nemeria NS, Chakraborty S, Balakrishnan A, et al. (2009) Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps. The Febs Journal. 276: 2432-46
Brandt GS, Kneen MM, Chakraborty S, et al. (2009) Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57
Chakraborty S, Nemeria NS, Balakrishnan A, et al. (2009) Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94
Brandt GS, Nemeria N, Chakraborty S, et al. (2008) Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43
Chakraborty S, Nemeria N, Yep A, et al. (2008) Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry. 47: 3800-9
Nemeria N, Chakraborty S, Baykal A, et al. (2007) The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proceedings of the National Academy of Sciences of the United States of America. 104: 78-82
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