Marie-Line Garron

ORCID: 0000-0001-5846-1246
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About
Contact & Profiles
Research Areas
  • Enzyme Production and Characterization
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Microbial Metabolites in Food Biotechnology
  • Proteoglycans and glycosaminoglycans research
  • Cell Adhesion Molecules Research
  • Biofuel production and bioconversion
  • Polysaccharides and Plant Cell Walls
  • Microbial metabolism and enzyme function
  • Monoclonal and Polyclonal Antibodies Research
  • Enzyme Structure and Function
  • Ubiquitin and proteasome pathways
  • Legume Nitrogen Fixing Symbiosis
  • Heparin-Induced Thrombocytopenia and Thrombosis
  • Signaling Pathways in Disease
  • Genomics and Phylogenetic Studies
  • RNA Research and Splicing
  • Microbial Metabolic Engineering and Bioproduction
  • Biochemical and Molecular Research
  • Metabolism and Genetic Disorders
  • Fibroblast Growth Factor Research
  • Protein Kinase Regulation and GTPase Signaling
  • 14-3-3 protein interactions
  • Seaweed-derived Bioactive Compounds
  • HER2/EGFR in Cancer Research

Aix-Marseille Université
2014-2024

Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement
2021-2024

Centre National de la Recherche Scientifique
2007-2021

Architecture et Fonction des Macromolécules Biologiques
2016-2019

Institut National de la Recherche Agronomique du Niger
2016

McGill University
2009-2011

Centre de Biologie Structurale
2007-2008

Inserm
2007-2008

Université de Montpellier
2007-2008

National Research Council Canada
2007

Thirty years have elapsed since the emergence of classification carbohydrate-active enzymes in sequence-based families that became CAZy database over 20 ago, freely available for browsing and download at www.cazy.org. In era large scale sequencing high-throughput Biology, it is important to examine position this specialist deeply rooted human curation. The three primary tasks curators are (i) maintain update family class enzymes, (ii) classify sequences newly released by GenBank Protein Data...

10.1093/nar/gkab1045 article EN cc-by-nc Nucleic Acids Research 2021-10-15

Abstract The Carbohydrate-Active enZYme database (CAZy; www.cazy.org) has been providing the reference classification of carbohydrate-active enzymes (CAZymes) for >30 years. Based on literature survey, sequence-based families CAZymes are enriched with functional data by using International Union Biochemistry and Molecular Biology Enzyme Commission (EC) number system. However, this system was not developed to search or compare information. To better harness information, we have CAZac...

10.1093/nar/gkae1045 article EN cc-by Nucleic Acids Research 2024-11-11

Heparin lyase I (heparinase I) specifically depolymerizes heparin, cleaving the glycosidic linkage next to iduronic acid. Here, we show crystal structures of heparinase from Bacteroides thetaiotaomicron at various stages reaction with heparin oligosaccharides before and just after cleavage product disaccharide. The structure is comprised a beta-jellyroll domain harboring long deep substrate binding groove an unusual thumb-resembling extension. This thumb, decorated many basic residues,...

10.1074/jbc.m109.025338 article EN cc-by Journal of Biological Chemistry 2009-10-04

In the vast number of random mutagenesis experiments that have targeted protein thermostability, single amino acid substitutions increase apparent melting temperature (Tm) enzyme more than 1 to 2 degrees C are rare and often require creation a large library mutated genes. Here we present case where beneficial mutation (R236F) hemp fiber-processing pectate lyase Xanthomonas campestris origin (PL(Xc)) produced 6 in Tm 23-fold half-life at 45 without compromising enzyme's catalytic efficiency....

10.1128/aem.02220-07 article EN Applied and Environmental Microbiology 2007-12-22

Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans through a β-elimination mechanism. Recently, we determined the crystal structure of HepII from Pedobacter heparinus (previously known as Flavobacterium heparinum) in complex with disaccharide product, identified location its active site. Here present complexed proving same binding/active site responsible for degradation uronic acid epimers containing substrates. The key...

10.1074/jbc.m110.101071 article EN cc-by Journal of Biological Chemistry 2010-04-20

Glycosaminoglycans (GAGs) are linear polysaccharides comprised of disaccharide repeat units, a hexuronic acid, glucuronic acid or iduronic linked to hexosamine, N-acetylglucosamine (GlcNAc) N-acetylgalactosamine. GAGs undergo further modification such as epimerization and sulfation. These abundant in the extracellular matrix connective tissues. function stabilization fibrillar matrix, control hydration, regulation tissue, organism development by controlling cell cycle, behavior...

10.1093/glycob/cww096 article EN Glycobiology 2016-09-12

In the Carbohydrate-Active Enzyme (CAZy) database, glycoside hydrolase family 5 (GH5) is a large with more than 6,000 sequences. Among 51 described GH5 subfamilies, subfamily GH5_26 contains members that display either endo-β(1,4)-glucanase or β(1,3;1,4)-glucanase activities. this study, we focused on enzyme fromSaccharophagus degradans(SdGluc5_26A), marine bacterium known for its capacity to degrade wide diversity of complex polysaccharides.SdGluc5_26A displays lichenase activity toward...

10.1074/jbc.m115.695999 article EN cc-by Journal of Biological Chemistry 2016-01-12

Heparin and heparan sulfate contain a rare 3‐ O ‐sulfoglucosamine residue critical for anticoagulation virus recognition, respectively. The glycosidic linkage proximate to this is resistant cleavage by all heparin lyases (Heps). HepII has broad specificity. crystal structure of the wild type identified its active site showed close spatial proximity between Asn405 3‐OH group bound glucosamine residue. In study, we mutated less sterically demanding Ala405 or Gly405, which broadened substrate...

10.1016/j.febslet.2011.06.023 article EN FEBS Letters 2011-07-06

Pyrroloquinoline quinone (PQQ) is an ortho-quinone cofactor of several prokaryotic oxidases. Widely available in the diet and necessary for correct growth mice, PQQ has been suspected to be a vitamin eukaryotes. However, no PQQ-dependent eukaryotic enzyme had identified use until 2014, when basidiomycete catalyzing saccharide dehydrogenation using as was characterized served define auxiliary activity family 12 (AA12). Here we report biochemical characterization AA12 encoded by genome...

10.1128/aem.00964-19 article EN cc-by Applied and Environmental Microbiology 2019-10-11
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