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Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria.

Sharma M, Lingford JP, Petricevic M, Snow AJD, Zhang Y, Järvå MA, Mui JW, Scott NE, Saunders EC, Mao R, Epa R, da Silva BM, Pires DEV, Ascher DB, McConville MJ, Davies GJ, Williams SJ, Goddard-Borger ED
Proc Natl Acad Sci U S A 119 (2022)
Related entries: 7bby, 7bbz, 7bc0, 7bc1, 7nbz, 7ofx, 7ofy, 7oh2

Cited: 10 times
EuropePMC logo PMID: 35074914

Abstract

Catabolism of sulfoquinovose (SQ; 6-deoxy-6-sulfoglucose), the ubiquitous sulfosugar produced by photosynthetic organisms, is an important component of the biogeochemical carbon and sulfur cycles. Here, we describe a pathway for SQ degradation that involves oxidative desulfurization to release sulfite and enable utilization of the entire carbon skeleton of the sugar to support the growth of the plant pathogen Agrobacterium tumefaciens SQ or its glycoside sulfoquinovosyl glycerol are imported into the cell by an ATP-binding cassette transporter system with an associated SQ binding protein. A sulfoquinovosidase hydrolyzes the SQ glycoside and the liberated SQ is acted on by a flavin mononucleotide-dependent sulfoquinovose monooxygenase, in concert with an NADH-dependent flavin reductase, to release sulfite and 6-oxo-glucose. An NAD(P)H-dependent oxidoreductase reduces the 6-oxo-glucose to glucose, enabling entry into primary metabolic pathways. Structural and biochemical studies provide detailed insights into the recognition of key metabolites by proteins in this pathway. Bioinformatic analyses reveal that the sulfoquinovose monooxygenase pathway is distributed across Alpha- and Betaproteobacteria and is especially prevalent within the Rhizobiales order. This strategy for SQ catabolism is distinct from previously described pathways because it enables the complete utilization of all carbons within SQ by a single organism with concomitant production of inorganic sulfite.

Articles - 7olf mentioned but not cited (1)

  1. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Sharma M, Lingford JP, Petricevic M, Snow AJD, Zhang Y, Järvå MA, Mui JW, Scott NE, Saunders EC, Mao R, Epa R, da Silva BM, Pires DEV, Ascher DB, McConville MJ, Davies GJ, Williams SJ, Goddard-Borger ED. Proc Natl Acad Sci U S A 119 e2116022119 (2022)


Reviews citing this publication (2)

  1. Implications of hydrogen sulfide in colorectal cancer: Mechanistic insights and diagnostic and therapeutic strategies. Lin H, Yu Y, Zhu L, Lai N, Zhang L, Guo Y, Lin X, Yang D, Ren N, Zhu Z, Dong Q. Redox Biol 59 102601 (2023)
  2. New mechanisms for bacterial degradation of sulfoquinovose. Wei Y, Tong Y, Zhang Y. Biosci Rep 42 BSR20220314 (2022)

Articles citing this publication (7)

  1. Genome sequences of Arthrobacter spp. that use a modified sulfoglycolytic Embden-Meyerhof-Parnas pathway. Kaur A, van der Peet PL, Mui JW, Herisse M, Pidot S, Williams SJ. Arch Microbiol 204 193 (2022)
  2. Sulfoquinovose is a widespread organosulfur substrate for Roseobacter clade bacteria in the ocean. Liu L, Chen X, Ye J, Ma X, Han Y, He Y, Tang K. ISME J 17 393-405 (2023)
  3. A Variant of the Sulfoglycolytic Transketolase Pathway for the Degradation of Sulfoquinovose into Sulfoacetate. Chu R, Wei Y, Liu J, Li B, Zhang J, Zhou Y, Du Y, Zhang Y. Appl Environ Microbiol 89 e0061723 (2023)
  4. Oxygenolytic sulfoquinovose degradation by an iron-dependent alkanesulfonate dioxygenase. Ye Z, Wei Y, Jiang L, Zhang Y. iScience 26 107803 (2023)
  5. The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids. Snow AJD, Sharma M, Lingford JP, Zhang Y, Mui JW, Epa R, Goddard-Borger ED, Williams SJ, Davies GJ. Curr Res Struct Biol 4 51-58 (2022)
  6. A Broad-Spectrum α-Glucosidase of Glycoside Hydrolase Family 13 from Marinovum sp., a Member of the Roseobacter Clade. Li J, Mui JW, da Silva BM, Pires DEV, Ascher DB, Madiedo Soler N, Goddard-Borger ED, Williams SJ. Appl Biochem Biotechnol (2024)
  7. A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D. Xiao Z, Zha J, Yang X, Huang T, Huang S, Liu Q, Wang X, Zhong J, Zheng J, Liang R, Deng Z, Zhang J, Lin S, Dai S. Nat Commun 15 2128 (2024)


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