Welcome to the Carme Rovira group web site

We work at the Chemistry Department and the Institute of Theoretical and Computational Chemistry (IQTCUB) of the University of Barcelona (UB). Our research is focused on the modeling 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:

glycoside hydrolases (GHs), glycosyltransferases (GTs), polysaccharide lyases (PLs) and lytic polysaccharide monooxygenases (LPMOs).

Activity-based profiling of carbohydrate-active enzymes (CAZymes), particularly in the context of their biomedical and biotechnological applications.

See us on @CRovira_Bcelona and @roviralab.bsky.social

Current projects

"GLYCOprotein N-glycosylation from non-life to eukaryotes" HORIZON-MSCA-DN (GLYCO-N).

"Activity-Based Profiling of Glycoprocessing Enzymes for Human Health and a Sustainable Society. ERC-SyG (CARBOCENTRE).
"Computer Simulation of the Molecular Basis of Substrate Recognition and Catalysis in Glycoprocessing Enzymes" MICIU/AEI. PID2023-147939NB-I00 (SimMolGly).

Representative publications (see full list in Google Scholar)

J. Rivas-Fernández et al. “Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation”. Nat. Commun. 2670 (2025). UB press release.
B. Piniello et al. “Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.” Nat. Commun. 14, 5785 (2023).
Sobala et al. “An epoxide intermediate in glycosidase catalysis”. ACS Cent. Sci. 6, 5, 760–770 (2020). Commented by D. J. Vocadlo in ACS Cent. Sci. (see also press release by Univ. Melbourne).
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.