title: YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.
abstract: Sulfoquinovose is produced by photosynthetic organisms at a rate of 10(10) tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life.
authors.affiliation: School of Chemistry, University of Melbourne, Parkville, Victoria, Australia.|Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
authors.forename: Gaetano
authors.initials: G
authors.lastname: Speciale
authors.affiliation: Department of Chemistry, University of York, Heslington, York, UK.
authors.forename: Yi
authors.identifier: http://orcid.org/0000-0002-6927-4371
authors.initials: Y
authors.lastname: Jin
authors.affiliation: Department of Chemistry, University of York, Heslington, York, UK.
authors.forename: Gideon J
authors.identifier: http://orcid.org/0000-0002-7343-776X
authors.initials: GJ
authors.lastname: Davies
authors.affiliation: School of Chemistry, University of Melbourne, Parkville, Victoria, Australia.|Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
authors.forename: Spencer J
authors.identifier: http://orcid.org/0000-0001-6341-4364
authors.initials: SJ
authors.lastname: Williams
authors.affiliation: ACRF Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.|Department of Medical Biology, University of Melbourne, Parkville, Victoria, Australia.
authors.forename: Ethan D
authors.initials: ED
authors.lastname: Goddard-Borger
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D006017:Glycolipids / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006031:Glycosylation; D006868:Hydrolysis; D008055:Lipids / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011485:Protein Binding; D018724:Spinacia oleracea / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D006017:Glycolipids; D008055:Lipids; C503201:YihQ protein, E coli; C015518:sulfolipids; C013694:sulfoquinovosyl diglyceride