Welcome to the Carme Rovira group web site
Our research is focused on the study of enzymatic reactions and ligand-protein interactions at atomic and electronic detail, using computer simulation. Currently, we are interested in:
Mechanisms of biosynthesis and degradation of carbohydrates
Activity-based probes for carbohydrate-active enzymes
Influence of sugar ring puckering in glycosidase catalysis
Catalytic mechanisms of metalloproteins
We participate in two EU H2020 projects:
MSCA IT Network Sweet Crosstalk. "Training interdisciplinary glycoscientists to get a molecular-level grip on glycocodes at the human mucosa-microbiota interface"
ERC Synergy Grant 951231 CARBOCENTRE. "Activity-Based Profiling of Glycoprocessing Enzymes for Human Health and a Sustainable Society"
Representative publications (see full list in Google Scholar)
Tezé et al. “A single point mutation converts GH84 O-GlcNAc hydrolases into phosphorylases. Experimental and theoretical evidence”. J. Am. Chem. Soc. 142, 2120-2124 (2020).
Rovira et al. "Mannosidase mechanism: At the intersection of conformation and catalysis". Curr. Opin. Struct. Biol. 62, 79-92 (2020).
Bilyard et al. "Palladium-mediated enzyme activation suggests multiphase initiation of glycogenesis". Nature, 563, 235–240 (2018). Press.
Iglesias-Fernández et al. “A Front-Face ‘SNi synthase’ engineered from a retaining ‘double-SN2’ hydrolase”. Nat. Chem. Biol. 13, 874–881 (2017).
Rojas-Cervellera et al. “The molecular mechanism of the ligand exchange reaction of an antibody against a glutathione-coated gold cluster”. Nanoscale, 9, 3121-3127 (2017).
Jin et al. “A β-mannannase with a lysozyme fold and a novel molecular catalytic mechanism”. ACS Cent. Sci., 2, 896–903 (2016).
Raich et al. A trapped covalent intermediate of a glycoside hydrolase on the pathwayto transglycosylation. Insights from experiments and quantum mechanics/molecular mechanics simulations. J. Am. Chem. Soc., 138, 3325−3332 (2016).
Ardèvol & Rovira. “Reaction mechanisms incarbohydrate-active enzymes: glycosyl hydrolases and glycosyltransferases. Insights from ab initio QM/MM molecular dynamics simulations.” J. Am. Chem. Soc. 137, 7528-7547 (2015). Perspective article. JACS Spotlight.
Loewen et al. “An ionizable triptophane residue imparts catalase activity to a peroxidase core”. J. Am. Chem. Soc. 136, 7249−7252 (2014). JACS Spotlight.
Lira-Navarrete et al. “Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulatesprotein O-glycosylation”. Nat. Commun. 6, 6937 (2015).
Thompson et al. “The reaction coordinateof a bacterial GH47 α-mannosidase: a combined quantum mechanical and structural approach”. Angew. Chem. Int. Ed. 51, 10997-11001 (2012). Editorial VIP. Highlighted in Chemistry Views.
Davies, Planas & Rovira. "Conformational analyses of the reaction coordinate of glycosidases”. Acc. Chem. Res. 45, 308–316 (2012).
Ardèvol & Rovira. “The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium ion-like species”. Angew. Chem. Int. Ed. 50, 10897-10901 (2011). Editorial VIP.