YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Gaetano Speciale; Y. Jin; Gideon J. Davies; Spencer J. Williams; Ethan D. Goddard-Borger

doi:10.1038/nchembio.2023

YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Gaetano Speciale, Y. Jin^*, Gideon J. Davies, Spencer J. Williams, Ethan D. Goddard-Borger

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	215–217
Number of pages	3
Journal	NATURE CHEMICAL BIOLOGY
Volume	12
Early online date	15 Feb 2016
DOIs	https://doi.org/10.1038/nchembio.2023
Publication status	Published - Apr 2016

Bibliographical note

Date of Acceptance: 31/12/2015
This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details

Access to Document

10.1038/nchembio.2023

Revised author upload PDF (almost)
This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details
Accepted author manuscript, 3.33 MBLicence: Unspecified

Cite this

@article{38cb81414eb1452d8c7e0fe5918f1192,

title = "YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids",

abstract = "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.",

author = "Gaetano Speciale and Y. Jin and Davies, {Gideon J.} and Williams, {Spencer J.} and Goddard-Borger, {Ethan D.}",

note = "Date of Acceptance: 31/12/2015 This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details ",

year = "2016",

month = apr,

doi = "10.1038/nchembio.2023",

language = "English",

volume = "12",

pages = "215–217",

journal = "NATURE CHEMICAL BIOLOGY",

issn = "1552-4450",

publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

AU - Speciale, Gaetano

AU - Jin, Y.

AU - Davies, Gideon J.

AU - Williams, Spencer J.

AU - Goddard-Borger, Ethan D.

N1 - Date of Acceptance: 31/12/2015 This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details

PY - 2016/4

Y1 - 2016/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84958078508&partnerID=8YFLogxK

U2 - 10.1038/nchembio.2023

DO - 10.1038/nchembio.2023

M3 - Article

AN - SCOPUS:84958078508

SN - 1552-4450

VL - 12

SP - 215

EP - 217

JO - NATURE CHEMICAL BIOLOGY

JF - NATURE CHEMICAL BIOLOGY

ER -

YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Abstract

Bibliographical note

Access to Document

Other files and links

Cite this