Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI Journal Article
| Authors: | Song, F.; Zhuang, Z.; Finci, L.; Dunaway-Mariano, D.; Kniewel, R.; Buglino, J. A.; Solorzano, V.; Wu, J.; Lima, C. D. |
| Article Title: | Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI |
| Abstract: | 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. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. |
| Keywords: | controlled study; mutation; nonhuman; protein conformation; protein function; proteins; steady state; enzyme activity; structure-activity relationship; dna; kinetics; enzyme analysis; escherichia coli; substrate specificity; temperature; crystal structure; models, molecular; crystallography, x-ray; mutagenesis, site-directed; protein structure, tertiary; binding sites; catalysis; protein folding; enzyme specificity; enzyme structure; catalytic domain; protein structure, quaternary; enzyme release; hydrolysis; models, chemical; enzymes; hydrogen-ion concentration; enzyme mechanism; escherichia coli proteins; esters; phenylacetic acid derivative; phenylacetates; thioesters; canis familiaris; biodegradation; acetyl coenzyme a; electrostatics; aliphatic acyl-coenzyme; phenylacetate pathway; thiol ester hydrolase; palmitoyl-coa hydrolase |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 281 |
| Issue: | 16 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2006-04-21 |
| Start Page: | 11028 |
| End Page: | 11038 |
| Language: | English |
| DOI: | 10.1074/jbc.M513896200 |
| PUBMED: | 16464851 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 21" - "Export Date: 4 June 2012" - "CODEN: JBCHA" - "Source: Scopus" |
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