J Am Chem Soc. 2007 Jan 31;129(4):730-1.

Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase.

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Department of Chemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.

PMID:: 17243787; [PubMed - indexed for MEDLINE]

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Crystal structure of Escherichia coli enterobactin-specific isochorismate synthase (EntC) bound to its reaction product isochorismate: implications for the enzyme mechanism and differential activity of chorismate-utilizing enzymes. [J Mol Biol. 2010]
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Enzyme activity in the crowded milieu. [PLoS One. 2012]
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Three-dimensional stochastic off-lattice model of binding chemistry in crowded environments. [PLoS One. 2012]
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Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase.
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