ORCID Profile
0000-0003-0500-5946
Current Organisation
Sorbonne Université
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Publisher: American Chemical Society (ACS)
Date: 17-01-2017
DOI: 10.1021/JACS.6B10075
Publisher: American Chemical Society (ACS)
Date: 04-09-2019
DOI: 10.26434/CHEMRXIV.9745388.V1
Abstract: Retaining glycoside hydrolases cleave their substrates through stereochemical retention at the anomeric position. Typically, this involves two-step mechanisms using either an enzymatic nucleophile via a covalent glycosyl enzyme intermediate, or neighboring group participation by a substrate-borne 2-acetamido neighboring group via an oxazoline intermediate no enzymatic mechanism with participation of the sugar 2-hydroxyl has been reported. Here, we detail structural, computational and kinetic evidence for neighboring group participation by a mannose 2-hydroxyl in glycoside hydrolase family 99 endo-α-1,2-mannanases. We present a series of crystallographic snapshots of key species along the reaction coordinate: a Michaelis complex with a tetrasaccharide substrate complexes with intermediate mimics, β-1,2-aziridine and β-1,2-epoxide and a product complex. The 1,2-epoxide intermediate mimic displayed hydrolytic and transfer reactivity analogous to that expected for the 1,2-anhydro sugar intermediate supporting its catalytic equivalence. Quantum mechanics/molecular mechanics modelling of the reaction coordinate predicted a reaction pathway through a 1,2-anhydro sugar via a transition state in an unprecedented flattened, envelope ( E 3 ) conformation. Kinetic isotope effects for anomeric- 2 H and anomeric- 13 C support an oxocarbenium ion-like transition state and that for C2- 18 O (1.052 ± 0.006) directly implicates nucleophilic participation by the C2-hydroxyl. Collectively, these data substantiate this unprecedented and long-imagined enzymatic mechanism.
Publisher: American Chemical Society (ACS)
Date: 16-04-2020
Publisher: American Chemical Society (ACS)
Date: 21-01-2010
DOI: 10.1021/JA908908Q
Abstract: The enzymatic hydrolysis of alpha-L-fucosides is of importance in cancer, bacterial infections, and fucosidosis, a neurodegenerative lysosomal storage disorder. Here we show a series of snapshots along the reaction coordinate of a glycoside hydrolase family GH29 alpha-L-fucosidase unveiling a Michaelis (ES) complex in a (1)C(4) (chair) conformation and a covalent glycosyl-enzyme intermediate in (3)S(1) (skew-boat). First principles metadynamics simulations on isolated alpha-L-fucose strongly support a (1)C(4) (3)H(4) (3)S(1) conformational itinerary for the glycosylation step of the reaction mechanism and indicate a strong "preactivation" of the (1)C(4) complex to nucleophilic attack as reflected by free energy, C1-O1/O5-C1 bond length elongation/reduction, C1-O1 bond orientation, and positive charge development around the anomeric carbon. Analysis of an imino sugar inhibitor is consistent with tight binding of a chair-conformed charged species.
Publisher: Royal Society of Chemistry (RSC)
Date: 2023
DOI: 10.1039/D2SC05672K
Abstract: This review presents discrete metal complexes that catalyse or photocatalyse reactions within living cells or living organisms.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Matthieu Sollogoub.