ORCID Profile
0000-0002-6927-4371
Current Organisations
The University of Manchester Manchester Institute of Biotechnology
,
University of Manchester
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Publisher: American Chemical Society (ACS)
Date: 08-11-2016
Publisher: Portland Press Ltd.
Date: 16-04-2018
DOI: 10.1042/BCJ20170947
Abstract: Bacterial sulfoglycolytic pathways catabolize sulfoquinovose (SQ), or glycosides thereof, to generate a three-carbon metabolite for primary cellular metabolism and a three-carbon sulfonate that is expelled from the cell. Sulfoglycolytic operons encoding an Embden–Meyerhof–Parnas-like or Entner–Doudoroff (ED)-like pathway harbor an uncharacterized gene (yihR in Escherichia coli PpSQ1_00415 in Pseudomonas putida) that is up-regulated in the presence of SQ, has been annotated as an aldose-1-epimerase and which may encode an SQ mutarotase. Our sequence analyses and structural modeling confirmed that these proteins possess mutarotase-like active sites with conserved catalytic residues. We overexpressed the homolog from the sulfo-ED operon of Herbaspirillum seropedicaea (HsSQM) and used it to demonstrate SQ mutarotase activity for the first time. This was accomplished using nuclear magnetic resonance exchange spectroscopy, a method that allows the chemical exchange of magnetization between the two SQ anomers at equilibrium. HsSQM also catalyzed the mutarotation of various aldohexoses with an equatorial 2-hydroxy group, including d-galactose, d-glucose, d-glucose-6-phosphate (Glc-6-P), and d-glucuronic acid, but not d-mannose. HsSQM displayed only 5-fold selectivity in terms of efficiency (kcat/KM) for SQ versus the glycolysis intermediate Glc-6-P however, its proficiency [kuncat/(kcat/KM)] for SQ was 17 000-fold better than for Glc-6-P, revealing that HsSQM preferentially stabilizes the SQ transition state.
Publisher: American Chemical Society (ACS)
Date: 23-02-2021
Publisher: American Chemical Society (ACS)
Date: 05-09-2018
Publisher: Springer Science and Business Media LLC
Date: 15-02-2016
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.
Publisher: American Chemical Society (ACS)
Date: 30-01-2020
Publisher: Royal Society of Chemistry (RSC)
Date: 2017
DOI: 10.1039/C7CC04977C
Abstract: The non-hydrolyzable S-linked azasugar 1,6-α-mannobiosylthioisofagomine effects potent inhibition of Bacillus circulans family 76 endo -1,6-α-mannanase through an atypical interaction involving the acid/base residue of the enzyme.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
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 Yi Jin.