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==A bacterial protein structure in glycoside hydrolase family 31== | ==A bacterial protein structure in glycoside hydrolase family 31== | ||
<StructureSection load='5aee' size='340' side='right' caption='[[5aee]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5aee' size='340' side='right' caption='[[5aee]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/YIHQ_ECOLI YIHQ_ECOLI]] Exhibits hydrolysis activity against alpha-glucosyl fluoride, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed.<ref>PMID:15294295</ref> | [[http://www.uniprot.org/uniprot/YIHQ_ECOLI YIHQ_ECOLI]] Exhibits hydrolysis activity against alpha-glucosyl fluoride, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed.<ref>PMID:15294295</ref> | ||
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== Publication Abstract from PubMed == | |||
Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 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. | |||
YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.,Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550<ref>PMID:26878550</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:00, 2 March 2016
A bacterial protein structure in glycoside hydrolase family 31A bacterial protein structure in glycoside hydrolase family 31
Structural highlights
Function[YIHQ_ECOLI] Exhibits hydrolysis activity against alpha-glucosyl fluoride, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed.[1] Publication Abstract from PubMedSulfoquinovose is produced by photosynthetic organisms at a rate of 1010 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. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.,Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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