YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Speciale, Gaetano; Jin, Yi; Davies, G.J.; Williams, Spencer J.; Goddard‐Borger, Ethan D.

doi:10.1038/nchembio.2023

Cited by 73 publications

(92 citation statements)

References 28 publications

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“…(Benning and Somerville, 1992a). A sulfoquinovosidase (yihQ) identified in Escherichia coli catalyzes the hydrolysis of SQDG to SQ, which is the gateway enzyme for SQ degradation (Speciale et al, 2016). SQ has been shown to be degraded by certain aerobic as well as anaerobic bacteria (Roy et al, 2003;Denger et al, 2012Denger et al, , 2014Felux et al, 2015;Burrichter et al, 2018) and two major sulfoglycolytic pathways, the sulfo-Embden-Meyerhof-Parnas pathway (originally found in E. coli) and the sulfo-Entner-Doudoroff pathway (originally found in Pseudomonas putida SQ1) have been described (Denger et al, 2014;Felux et al, 2015).…”

Section: Sulfonate Metabolismsmentioning

confidence: 99%

Chemical Diversity and Biochemical Transformation of Biogenic Organic Sulfur in the Ocean

Tang

2020

Front. Mar. Sci.

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Organic sulfur compounds are not only essential for organismal survival but also indispensable for the sulfur cycle. Over the past few decades, dimethylsulfoniopropionate (DMSP) and dimethyl sulfide (DMS) cycling in the upper ocean have been well characterized from the genetic to the ecosystem level. Recent advances in the study of marine sulfonate transformation have indicated that phytoplankton and microbes play key roles in oceanic sulfur and carbon fluxes. This review provides biochemical details of the major sulfur metabolites, and presents an interlinked reaction network with genetic information on the microbial transformation and mineralization of sulfur compounds. This review also discusses future prospects for the discovery and characterization of novel substrates and enzymes involved in organosulfur cycling, as well as for investigations of deep sea and sedimentary organic sulfur.

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Section: Sulfonate Metabolismsmentioning

confidence: 99%

Chemical Diversity and Biochemical Transformation of Biogenic Organic Sulfur in the Ocean

Tang

2020

Front. Mar. Sci.

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“…The chromogenic substrate 4-nitrophenyl α-sulfoquinovoside (PNPSQ), which was designed as an analogue of the natural substrate SQGro, results in release of the chromophore 4-nitrophenolate, which can be detected using UV-visible spectrophotometry at 400 nm. 23, 24 Rl -SRDI565 was grown to mid-logarithmic phase in Y 5% M and Y 5% SQ media, and the harvested cells used to prepare a cell-free lysate containing soluble proteins. Incubation of Y 5% M and Y 5% SQ-derived lysates with PNPSQ both resulted in production of 4-nitrophenolate at similar rates.…”

Section: Resultsmentioning

confidence: 99%

A sulfoglycolytic Entner-Doudoroff pathway inRhizobium leguminosarumbv.trifoliiSRDI565

Li¹,

Epa²,

Scott

et al. 2019

Preprint

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32Rhizobia are nitrogen fixing bacteria that engage in symbiotic relationships with plant hosts 33 but can also persist as free-living bacteria with the soil and rhizosphere. Here we show that free 34 living Rhizobium leguminosarum SRDI565 can grow on the sulfosugar sulfoquinovose (SQ) 35 using a sulfoglycolytic Entner-Doudoroff (sulfo-ED) pathway resulting in production of 36 sulfolactate (SL) as the major metabolic end-product. Comparative proteomics supports the 37 involvement of a sulfo-ED operon encoding an ABC transporter cassette, sulfo-ED enzymes 38 and an SL exporter. Consistent with an oligotrophic lifestyle, proteomics data revealed little 39 change in expression of the sulfo-ED proteins during growth on SQ versus mannitol, a result 40 confirmed through biochemical assay of sulfoquinovosidase activity in cell lysates (data are 41 available via ProteomeXchange with identifier PXD015822). Metabolomics analysis showed 42 that growth on SQ involves gluconeogenesis to satisfy metabolic requirements for glucose-6-43 phosphate and fructose-6-phosphate. Metabolomics analysis also revealed the unexpected 44 production of small amounts of sulfofructose and 2,3-dihydroxypropanesulfonate, which are 45 proposed to arise from promiscuous activities of the glycolytic enzyme phosphoglucose 46 isomerase and a non-specific aldehyde reductase, respectively. This work shows that rhizobial 47 metabolism of the abundant sulfosugar SQ may contribute to persistence of the bacteria in the 48 soil and to mobilization of sulfur in the pedosphere. 49 50 Results 127Analysis of the genome of Rl-SRDI565 revealed a sulfo-ED operon that had the same 128 genes, but no synteny with the P. putida SQ1 operon (Figure 1). Genes with high homology to 129 the P. putida proteins included a putative SQase, SQ dehydrogenase, SL lactonase, SG 130 dehydratase, KDSG aldolase and SLA dehydrogenase, and an SL exporter (see Figures S1-S6). 131The Rl-SRDI565 operon contains some important differences compared to that of P. putida 132 SQ1. In particular, it lacks a putative SQ mutarotase, 20 and appears to use an ABC transporter 133 cassette to import SQ/SQGro in place of an SQ/SQGro importer/permease. The putative sulfo-134 ED pathway in Rl-SRDI565 is consistent with the proposed protein functions outlined in Figure 135 1b, with a comparison to the classical ED pathway in Figure 1c. 136

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“…The purified fraction was also enzymatically hydrolysed using a lipase from the fungus Rhizopus arrhizus (capable of a regioselective cleavage of the acyl group at the sn 1 position) providing the respective SQMG, whose structures were also confirmed by NMR. Note that a sulfoquinovosidase has been identified in Escherichia coli YihQ, yet significant amounts of this enzyme are not available …”

Section: Introductionmentioning

confidence: 99%

Unambiguous regiochemical assignment of sulfoquinovosyl mono‐ and diacylglycerols in parsley and spinach leaves by liquid chromatography/electrospray ionization sequential mass spectrometry assisted by regioselective enzymatic hydrolysis

Granafei

Losito

Palmisano

et al. 2017

Rapid Comm Mass Spectrometry

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YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

Cited by 73 publications

References 28 publications

Chemical Diversity and Biochemical Transformation of Biogenic Organic Sulfur in the Ocean

Chemical Diversity and Biochemical Transformation of Biogenic Organic Sulfur in the Ocean

A sulfoglycolytic Entner-Doudoroff pathway inRhizobium leguminosarumbv.trifoliiSRDI565

Unambiguous regiochemical assignment of sulfoquinovosyl mono‐ and diacylglycerols in parsley and spinach leaves by liquid chromatography/electrospray ionization sequential mass spectrometry assisted by regioselective enzymatic hydrolysis

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