Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Capece, Luciana | - |
| dc.creator | Lewis-Ballester, Ariel | - |
| dc.creator | Marti, Marcelo Adrian | - |
| dc.creator | Estrin, Dario Ariel | - |
| dc.creator | Yeh, Syun-Ru | - |
| dc.date | 2019-01-28T15:01:35Z | - |
| dc.date | 2019-01-28T15:01:35Z | - |
| dc.date | 2011-11-23 | - |
| dc.date | 2019-01-09T14:20:57Z | - |
| dc.date.accessioned | 2019-04-29T15:43:41Z | - |
| dc.date.available | 2019-04-29T15:43:41Z | - |
| dc.date.issued | 2019-01-28T15:01:35Z | - |
| dc.date.issued | 2019-01-28T15:01:35Z | - |
| dc.date.issued | 2011-11-23 | - |
| dc.date.issued | 2019-01-09T14:20:57Z | - |
| dc.identifier | Capece, Luciana; Lewis-Ballester, Ariel; Marti, Marcelo Adrian; Estrin, Dario Ariel; Yeh, Syun-Ru; Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase; American Chemical Society; Biochemistry; 50; 50; 23-11-2011; 10910-10918 | - |
| dc.identifier | 0006-2960 | - |
| dc.identifier | http://hdl.handle.net/11336/68712 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/300461 | - |
| dc.description | Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to Nformylkynurenine.<br />While human IDO is able to oxidize both Land D-Trp, human TDO (hTDO) displays major specificity for L-Trp. In this work, we aim to interrogate the molecular basis for the substrate stereoselectivity of hTDO. Our previous molecular dynamics simulation studies of Xanthomonas campestris TDO (xcTDO) showed that a hydrogen bond between T254 (T342 in hTDO) and the ammonium group of the substrate is present in the L-Trp-bound enzyme, but not in the D-Trp-bound enzyme. The fact that this is the only notable structural alteration induced by the change in the stereo structure of the substrate prompted us to produce and characterize the T342A mutant of hTDO to evaluate the structural role of T342 in controlling the substrate stereoselectivity of the enzyme. The experimental results indicate that the mutation only slightly perturbs the global structural properties of the enzyme but totally abolishes the substrate stereoselectivity. Molecular dynamics simulations of xcTDO show that T254 controls the substrate stereoselectivity of the enzyme by (i) modulating the hydrogen bonding interaction between the NH3+ group and epoxide oxygen of the ferryl−indole 2,3-epoxide intermediate of the enzyme and (ii) regulating the dynamics of two active site loops,<br />loop250−260 and loop117−130, critical for substrate binding. | - |
| dc.description | Fil: Capece, Luciana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina | - |
| dc.description | Fil: Lewis-Ballester, Ariel. Yeshiva University; Estados Unidos | - |
| dc.description | Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina | - |
| dc.description | Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina | - |
| dc.description | Fil: Yeh, Syun-Ru. Yeshiva University; Estados Unidos | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | American Chemical Society | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi201439m | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi201439m | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237892/ | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | INDEOLAMINE DIOXYGENASE | - |
| dc.subject | TRYPTOPHANE DIOXYGENASE | - |
| dc.subject | COMPUTER SIMULATION | - |
| dc.subject | Otras Ciencias Químicas | - |
| dc.subject | Ciencias Químicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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