Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1
The phosphotriesterase from Sphingobium sp. TCM1 (Sb-PTE) is notable for its ability to hydrolyze organophosphates that are not substrates for other enzymes. In an attempt to determine the catalytic properties of Sb-PTE for hydrolysis of chiral phosphotriesters, we discovered that multiple phosphodi...
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| Veröffentlicht in: | Biochemistry (Easton) 2018-03, Vol.57 (12), p.1842-1846 |
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| creator | Bigley, Andrew N Narindoshvili, Tamari Xiang, Dao Feng Raushel, Frank M |
| description | The phosphotriesterase from Sphingobium sp. TCM1 (Sb-PTE) is notable for its ability to hydrolyze organophosphates that are not substrates for other enzymes. In an attempt to determine the catalytic properties of Sb-PTE for hydrolysis of chiral phosphotriesters, we discovered that multiple phosphodiester products are formed from a single substrate. For example, Sb-PTE catalyzes the hydrolysis of the R P-enantiomer of methyl cyclohexyl p-nitrophenyl phosphate with exclusive formation of methyl cyclohexyl phosphate. However, the enzyme catalyzes hydrolysis of the S P-enantiomer of this substrate to an equal mixture of methyl cyclohexyl phosphate and cyclohexyl p-nitrophenyl phosphate products. The ability of this enzyme to catalyze the hydrolysis of a methyl ester at the same rate as the hydrolysis of a p-nitrophenyl ester contained within the same substrate is remarkable. The overall scope of the stereoselective properties of this enzyme is addressed with a library of chiral and prochiral substrates. |
| doi_str_mv | 10.1021/acs.biochem.8b00145 |
| format | Article |
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The ability of this enzyme to catalyze the hydrolysis of a methyl ester at the same rate as the hydrolysis of a p-nitrophenyl ester contained within the same substrate is remarkable. 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TCM1</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The phosphotriesterase from Sphingobium sp. TCM1 (Sb-PTE) is notable for its ability to hydrolyze organophosphates that are not substrates for other enzymes. In an attempt to determine the catalytic properties of Sb-PTE for hydrolysis of chiral phosphotriesters, we discovered that multiple phosphodiester products are formed from a single substrate. For example, Sb-PTE catalyzes the hydrolysis of the R P-enantiomer of methyl cyclohexyl p-nitrophenyl phosphate with exclusive formation of methyl cyclohexyl phosphate. However, the enzyme catalyzes hydrolysis of the S P-enantiomer of this substrate to an equal mixture of methyl cyclohexyl phosphate and cyclohexyl p-nitrophenyl phosphate products. The ability of this enzyme to catalyze the hydrolysis of a methyl ester at the same rate as the hydrolysis of a p-nitrophenyl ester contained within the same substrate is remarkable. The overall scope of the stereoselective properties of this enzyme is addressed with a library of chiral and prochiral substrates.</description><subject>Bacterial Proteins - chemistry</subject><subject>Catalysis</subject><subject>catalytic activity</subject><subject>Hydrolysis</subject><subject>Organophosphonates - chemistry</subject><subject>organophosphorus compounds</subject><subject>phosphates</subject><subject>Phosphoric Diester Hydrolases - chemistry</subject><subject>phosphoric triester hydrolases</subject><subject>Sphingomonadaceae - enzymology</subject><subject>Sphingomonas</subject><subject>stereoselectivity</subject><issn>0006-2960</issn><issn>1520-4995</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EokvhCZCQj1yynUkcb3xEK6BIrVrRco5sx25cJXGwncM-CO-Lt9n2CCd75O__xzM_IR8RtgglXkgdt8p53Ztx2ygAZPUrssG6hIIJUb8mGwDgRSk4nJF3MT7mksGOvSVnpaixEk25IX-ulyG5eTD0p5E6OT_R2-C7RadIbfAjTb2hl4cu-OEQXaTe0n3vghyonLojqtfqJjzIyc-9j3Mvk6F3i4op5Fuk6vBkcvv05lNwJiYTZDRrg7u5d9ODV24ZaZy39H5_je_JGyuHaD6cznPy69vX-_1lcXXz_cf-y1UhWVmlohMVE8oCV3bHFFouQHYgOp1H7pRSKGvFFUepJWtQ1agRLFbMKGMN32F1Tj6vvnPwv5f8r3Z0UZthkJPxS2xLRC4q3kD9fxQw06xqdhmtVlQHH2Mwtp2DG2U4tAjtMbo2R9eeomtP0WXVp1ODRY2me9E8Z5WBixU4qh_9Eqa8mn9a_gVJEKrt</recordid><startdate>20180327</startdate><enddate>20180327</enddate><creator>Bigley, Andrew N</creator><creator>Narindoshvili, Tamari</creator><creator>Xiang, Dao Feng</creator><creator>Raushel, Frank M</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-5918-3089</orcidid></search><sort><creationdate>20180327</creationdate><title>Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1</title><author>Bigley, Andrew N ; Narindoshvili, Tamari ; Xiang, Dao Feng ; Raushel, Frank M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a423t-d9349bf06bf74b1f690ad09dc960dbbb1a5b6b61aca481b51c10f134ebefe6713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Catalysis</topic><topic>catalytic activity</topic><topic>Hydrolysis</topic><topic>Organophosphonates - chemistry</topic><topic>organophosphorus compounds</topic><topic>phosphates</topic><topic>Phosphoric Diester Hydrolases - chemistry</topic><topic>phosphoric triester hydrolases</topic><topic>Sphingomonadaceae - enzymology</topic><topic>Sphingomonas</topic><topic>stereoselectivity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bigley, Andrew N</creatorcontrib><creatorcontrib>Narindoshvili, Tamari</creatorcontrib><creatorcontrib>Xiang, Dao Feng</creatorcontrib><creatorcontrib>Raushel, Frank M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bigley, Andrew N</au><au>Narindoshvili, Tamari</au><au>Xiang, Dao Feng</au><au>Raushel, Frank M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2018-03-27</date><risdate>2018</risdate><volume>57</volume><issue>12</issue><spage>1842</spage><epage>1846</epage><pages>1842-1846</pages><issn>0006-2960</issn><issn>1520-4995</issn><eissn>1520-4995</eissn><abstract>The phosphotriesterase from Sphingobium sp. TCM1 (Sb-PTE) is notable for its ability to hydrolyze organophosphates that are not substrates for other enzymes. In an attempt to determine the catalytic properties of Sb-PTE for hydrolysis of chiral phosphotriesters, we discovered that multiple phosphodiester products are formed from a single substrate. For example, Sb-PTE catalyzes the hydrolysis of the R P-enantiomer of methyl cyclohexyl p-nitrophenyl phosphate with exclusive formation of methyl cyclohexyl phosphate. However, the enzyme catalyzes hydrolysis of the S P-enantiomer of this substrate to an equal mixture of methyl cyclohexyl phosphate and cyclohexyl p-nitrophenyl phosphate products. The ability of this enzyme to catalyze the hydrolysis of a methyl ester at the same rate as the hydrolysis of a p-nitrophenyl ester contained within the same substrate is remarkable. The overall scope of the stereoselective properties of this enzyme is addressed with a library of chiral and prochiral substrates.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>29513982</pmid><doi>10.1021/acs.biochem.8b00145</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-5918-3089</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemistry (Easton), 2018-03, Vol.57 (12), p.1842-1846 |
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| source | ACS Publications; MEDLINE |
| subjects | Bacterial Proteins - chemistry Catalysis catalytic activity Hydrolysis Organophosphonates - chemistry organophosphorus compounds phosphates Phosphoric Diester Hydrolases - chemistry phosphoric triester hydrolases Sphingomonadaceae - enzymology Sphingomonas stereoselectivity |
| title | Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1 |
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