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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/9480

Title: Structural analysis of the alcohol acyltransferase protein family from Cucumismelo shows that enzyme activity depends on an essential solvent channel
Authors: Galaz, S.
Morales-Quintana, L.
Moya-Leon, M.A.
Herrera, R.
Issue Date: Mar-2013
Publisher: WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Citation: FEBS JOURNAL Volume: 280 Issue: 5 Pages: 1344-1357 DOI: 10.1111/febs.12127
Abstract: Alcohol acyltransferases (AAT) play a key role in ester biosynthesis. In Cucumismelo var.cantalupensis, AATs are encoded by a gene family of four members (CmAAT14). CmAAT1, CmAAT3 and CmAAT4 are capable of synthesizing esters, with CmAAT1 the most active. CmAAT2 is inactive and has an Ala268 residue instead of a threonine which is present in all other active AATs, although the role of this residue is still unclear. The present work aims to understand the molecular mechanism involved in ester biosynthesis in melon fruit and to clarify the importance of the Ala268 residue. First, structural models for each protein were built by comparative modelling methodology. Afterwards, conformational interaction between the protein and several ligands, alcohols and acyl-CoAs was explored by molecular docking and molecular dynamics simulation. Structural analysis showed that CmAATs share a similar structure. Also, well-defined solvent channels were described in the CmAATs except for CmAAT2 which does not have a proper channel and instead has a small pocket around Ala268. Residues of the catalytic HxxxD motif interact with substrates within the solvent channel, with Ser363 also important. Strong binding interaction energies were described for the best substrate couple of each CmAAT (hexyl-, benzyl- and cinnamyl-acetate for CmAAT1, 3 and 4 respectively). CmAAT1 and CmAAT2 protein surfaces share similar electrostatic potentials; nevertheless the entrance channels for the substrates differ in location and electrostatic character, suggesting that Ala268 might be responsible for that. This could partly explain the major differences in activity reported for these two enzymes. Database Structural data have been deposited in the Protein Model Data Bank under the following accession numbers: CmAAT1 (PM0078514); CmAAT2 (PM0078515); CmAAT3 (PM0078516); CmAAT4 (PM0078517)
Description: Galaz, S (Galaz, Sebastian)[ 1 ] ; Morales-Quintana, L (Morales-Quintana, Luis)[ 1 ] ; Moya-Leon, MA (Alejandra Moya-Leon, Maria)[ 1 ] ; Herrera, R (Herrera, Raul)[ 1 ]
URI: http://dspace.utalca.cl/handle/1950/9480
ISSN: 1742-464X
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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