1zoi

<table><tr><td colspan='2'>[[1zoi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOI FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zoi OCA], [https://pdbe.org/1zoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zoi RCSB], [https://www.ebi.ac.uk/pdbsum/1zoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zoi ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Esterase (EST) from Pseudomonas putida IFO12996 catalyzes the stereoselective hydrolysis of methyl dl-beta-acetylthioisobutyrate (dl-MATI) to produce d-beta-acetylthioisobutyric acid (DAT), serving as a key intermediate for the synthesis of angiotensin-converting enzyme inhibitors. The EST gene was cloned and expressed in Escherichia coli; the recombinant protein is a non-disulfide-linked homotrimer with a monomer molecular weight of 33,000 in both solution and crystalline states, indicating that these ESTs function as trimers. EST hydrolyzed dl-MATI to produce DAT with a degree of conversion of 49.5% and an enantiomeric excess value of 97.2% at an optimum pH of about 8 to 10 and an optimum temperature of about 57 to 67 degrees C. The crystal structure of EST has been determined by X-ray diffraction to a resolution of 1.6 A, confirming that EST is a member of the alpha/beta hydrolase fold superfamily of enzymes and includes a catalytic triad of Ser97, Asp227, and His256. The active site is located approximately in the middle of the molecule at the end of a pocket approximately 12 A deep. EST can hydrolyze the methyl ester group without affecting the acetylthiol ester moiety in dl-MATI. The examination of substrate specificity of EST toward other linear esters revealed that the enzyme showed specific activity toward methyl esters and that it recognized the configuration at C-2.

Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis.,Elmi F, Lee HT, Huang JY, Hsieh YC, Wang YL, Chen YJ, Shaw SY, Chen CJ J Bacteriol. 2005 Dec;187(24):8470-6. PMID:16321951<ref>PMID:16321951</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1zoi" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Chen, C J]]

[[Category: Chen, Y J]]

[[Category: Elmi, F]]

[[Category: Hsieh, Y C]]

[[Category: Huang, J Y]]

[[Category: Lee, H T]]

[[Category: Shaw, S Y]]

[[Category: Wang, Y L]]

[[Category: Alpha/beta hydrolase fold]]

[[Category: Esterase]]

[[Category: Hydrolase]]