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J. Biol. Chem., Vol. 281, Issue 16, 11028-11038, April 21, 2006

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Structure, Function, and Mechanism of the Phenylacetate Pathway Hot Dog-fold Thioesterase PaaI^*

Feng Song, Zhihao Zhuang¹, Lorenzo Finci, Debra Dunaway-Mariano², Ryan Kniewel, John A. Buglino, Veronica Solorzano, Jin Wu^¶, and Christopher D. Lima

From the Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131, Structural Biology Program, Sloan-Kettering Institute, New York, New York 10021, and ^¶Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021

The structure and biochemical function of the hot dog-fold thioesterase PaaI operative in the aerobic phenylacetate degradation pathway are examined. PaaI showed modest activity with phenylacetyl-coenzyme A, suggestive of a role in coenzyme A release from this pathway intermediate in the event of limiting downstream pathway enzymes. Minimal activity was observed with aliphatic acyl-coenzyme A thioesters, which ruled out PaaI function in the lower phenylacetate pathway. PaaI was most active with ring-hydroxylated phenylacetyl-coenzyme A thioesters. The x-ray crystal structure of the Escherichia coli thioesterase is reported and analyzed to define the structural basis of substrate recognition and catalysis. The contributions of catalytic and substrate binding residues, thus, identified were examined through steady-state kinetic analysis of site-directed mutant proteins.

Received for publication, December 30, 2005 , and in revised form, February 6, 2006.

The atomic coordinates and structure factors (code 2FS2) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by National Institutes of Health Grants GM28688 (to D. D.-M.) and 1P50 GM62529 (to C. D. L.) and by the Arnold and Mabel Beckman Foundation and Rita Allen Foundation (to C. D. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

¹ Present address: Dept. of Chemistry, 415 Wartik Laboratory, Pennsylvania State University, University Park, PA 16802.

² To whom correspondence should be addressed. Tel.: 505-277-3383; Fax: 505-277-6202; E-mail: dd39{at}unm.edu.

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