Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/17892
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Jiménez, Aurora | - |
dc.contributor.author | Clapés Saborit, Pere | - |
dc.contributor.author | Crehuet, Ramón | - |
dc.date.accessioned | 2009-10-21T11:06:46Z | - |
dc.date.available | 2009-10-21T11:06:46Z | - |
dc.date.issued | 2009-01-26 | - |
dc.identifier.citation | Chemistry - A European Journal 15(6): 1422-1428 (2009) | en_US |
dc.identifier.issn | 0947-6539 | - |
dc.identifier.uri | http://hdl.handle.net/10261/17892 | - |
dc.description | 7 pages, 5 figures, 2 tables.-- PMID: 19115296 [PubMed].-- Available online Dec 29, 2008. | en_US |
dc.description.abstract | The mobility of rhamnulose-1-phosphate aldolase (RhuA) was analysed with a normal mode description and high level calculations on models of the active site. We report the connection between the mobility and the chemical properties of the active site, and compare them to a closely related enzyme, fuculose-1-phosphate aldolase (FucA). Calculations show that the different coordination number for the zinc ion, reported in the crystal structures of RhuA and FucA, was due to a different spatial arrangement of the residues, not to their different chemical nature. Moreover, the metal coordination change is correlated with activity. The domain mobility of the enzyme can reshape the active site of RhuA into the arrangement found in the FucA structure, and vice-versa. This has a direct influence on the energy barrier for the aldol reaction catalyzed by these enzymes, thus showing a coupling of the domain movements and the catalytic effects. Hence domain movements and the coordination chemistry of the active site metal suggest an explanation of why these enzymes have similar experimental turnover rates. | en_US |
dc.description.sponsorship | R.C. thanks the Spanish Ramón y Cajal Program for financial support, and A.J. thanks the CSIC and the European Social Fund for her I3P fellowship. We acknowledge financial support from the MEC (Grant CTQ2006–01345/BQU) and the Generalitat de Catalunya (Grant 2005SGR00111). This research has been partly performed by using the CESCA resources. | en_US |
dc.format.extent | 918459 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | John Wiley & Sons | en_US |
dc.rights | closedAccess | en_US |
dc.subject | Density functional calculations | en_US |
dc.subject | Enzyme catalysis | en_US |
dc.subject | Metalloproteins | en_US |
dc.subject | Protein flexibility | en_US |
dc.subject | Reaction mechanisms | en_US |
dc.title | Protein flexibility and metal coordination changes in DHAP-dependent aldolases | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1002/chem.200801223 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1002/chem.200801223 | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
item.openairetype | artículo | - |
Aparece en las colecciones: | (IQAC) Artículos |
CORE Recommender
SCOPUSTM
Citations
6
checked on 12-abr-2024
WEB OF SCIENCETM
Citations
6
checked on 29-feb-2024
Page view(s)
416
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.