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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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Binding Sites
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Crystallography, X-Ray
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Escherichia coli / enzymology*
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Escherichia coli / metabolism
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Escherichia coli Proteins* / chemistry
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Escherichia coli Proteins* / genetics
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Glycolipids / chemistry*
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Glycolipids / genetics
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Glycolipids / metabolism
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Glycosylation
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Hydrolysis
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Lipids / chemistry*
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Mutation
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Protein Binding
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Spinacia oleracea / chemistry
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Substrate Specificity
Substances
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Escherichia coli Proteins
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Glycolipids
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Lipids
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YihQ protein, E coli
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sulfolipids
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sulfoquinovosyl diglyceride
Associated data
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PubChem-Substance/295369317
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PubChem-Substance/295369318
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PubChem-Substance/295369319
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PubChem-Substance/295369320
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PubChem-Substance/295369321
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PubChem-Substance/295369322
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PubChem-Substance/295369323
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PubChem-Substance/295369324
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PubChem-Substance/295369325