<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1psu ConSurf].
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Revision as of 19:11, 8 February 2016
Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon
[PAAI_ECOLI] Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI.,Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
↑Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD. Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851 doi:https://dx.doi.org/10.1074/jbc.M513896200
↑Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD. Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI. J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851 doi:https://dx.doi.org/10.1074/jbc.M513896200
