Blanchard, R. L., Freimuth, R. R., Buck, J., Weinshilboum, R. M. & Coughtrie, M. W. H. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 14, 199–211 (2004).
Men, P. et al. Biosynthesis mechanism, genome mining and artificial construction of echinocandin O-sulfonation. Metab. Eng. 74, 160–167 (2022).
Zhang, Z. et al. Mechanistic and structural insights into the specificity and biological functions of bacterial sulfoglycosidases. ACS Catal. 13, 824–836 (2023).
Luis, A. S. et al. Sulfated glycan recognition by carbohydrate sulfatases of the human gut microbiota. Nat. Chem. Biol. 18, 841–849 (2022).
Malojcić, G. et al. A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli. Proc. Natl Acad. Sci. USA 105, 19217–19222 (2008).
Liu, F., Yang, H., Wang, L. & Yu, B. Biosynthesis of the high-value plant secondary product benzyl isothiocyanate via functional expression of multiple heterologous enzymes in Escherichia coli. ACS Synth. Biol. 5, 1557–1565 (2016).
Muthukumar, J., Chidambaram, R. & Sukumaran, S. Sulfated polysaccharides and its commercial applications in food industries—A review. J. Food Sci. Technol. 58, 2453–2466 (2021).
Huang, L., Shen, M., Morris, G. A. & Xie, J. Sulfated polysaccharides: Immunomodulation and signaling mechanisms. Trends Food Sci. Technol. 92, 1–11 (2019).
Chen, Y. et al. Unleashing the potential of noncanonical amino acid biosynthesis to create cells with precision tyrosine sulfation. Nat. Commun. 13, 5434 (2022).
Yang, Y. S. et al. Tyrosine sulfation as a protein post-translational modification. Molecules 20, 2138–2164 (2015).
Thompson, R. E. et al. Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors. Nat. Chem. 9, 909–917 (2017).
Mauvais-Jarvis, F., Clegg, D. J. & Hevener, A. L. The role of estrogens in control of energy balance and glucose homeostasis. Endocr. Rev. 34, 309–338 (2013).
Radka, C. D., Miller, D. J., Frank, M. W. & Rock, C. O. Biochemical characterization of the first step in sulfonolipid biosynthesis in Alistipes finegoldii. J. Biol. Chem. 298, 102195 (2022).
Bojarová, P. & Williams, S. J. Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination. Curr. Opin. Chem. Eng. 12, 573–581 (2008).
Klaassen, C. D. & Boles, J. W. Sulfation and sulfotransferases 5: the importance of 3’-phosphoadenosine 5’-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J. 11, 404–418 (1997).
van den Boom, J., Heider, D., Martin, S. R., Pastore, A. & Mueller, J. W. 3′-Phosphoadenosine 5′-phosphosulfate (PAPS) synthases, naturally fragile enzymes specifically stabilized by nucleotide binding. J. Biol. Chem. 287, 17645–17655 (2012).
Burkart, M. D., Izumi, M. & Wong, C. H. Enzymatic regeneration of 3’-phosphoadenosine-5’-phosphosulfate using aryl sulfotransferase for the preparative enzymatic synthesis of sulfated carbohydrates. Angew. Chem. Int. Ed. 38, 2747–2750 (1999).
Zhou, Z. et al. A microbial-enzymatic strategy for producing chondroitin sulfate glycosaminoglycans. Biotechnol. Bioeng. 115, 1561–1570 (2018).
Zhou, Z. et al. Secretory expression of the rat aryl sulfotransferases IV with improved catalytic efficiency by molecular engineering. 3 Biotechnol. 9, 246 (2019).
Datta, P. et al. Expression of enzymes for 3’-phosphoadenosine-5’-phosphosulfate (PAPS) biosynthesis and their preparation for PAPS synthesis and regeneration. Appl. Microbiol. Biotechnol. 104, 7067–7078 (2020).
Zhang, Y. et al. Synthesis of bioengineered heparin by recombinant yeast Pichia pastoris. Green. Chem. 24, 3180–3192 (2022).
Bhaskar, U. et al. Combinatorial one-pot chemoenzymatic synthesis of heparin. Carbohydr. Polym. 122, 399–407 (2015).
Xi, X. et al. Improvement of the stability and catalytic efficiency of heparan sulfate N-sulfotransferase for preparing N-sulfated heparosan. J. Ind. Microbiol. Biotechnol. 50, kuad012 (2023).
Kang, Z. et al. Bio-based strategies for producing glycosaminoglycans and their oligosaccharides. Trends Biotechnol. 36, 806–818 (2018).
DeAngelis, P. L., Liu, J. & Linhardt, R. J. Chemoenzymatic synthesis of glycosaminoglycans: re-creating, re-modeling and re-designing nature’s longest or most complex carbohydrate chains. Glycobiology 23, 764–777 (2013).
Zhou, X., Chandarajoti, K., Pham, T. Q., Liu, R. & Liu, J. Expression of heparan sulfate sulfotransferases in Kluyveromyces lactis and preparation of 3’-phosphoadenosine-5’-phosphosulfate. Glycobiology 21, 771–780 (2011).
Bao, F. et al. Hydrolysis of by-product adenosine diphosphate from 3’-phosphoadenosine-5’-phosphosulfate preparation using Nudix hydrolase NudJ. Appl. Microbiol. Biotechnol. 99, 10771–10778 (2015).
An, C., Zhao, L., Wei, Z. & Zhou, X. Chemoenzymatic synthesis of 3’-phosphoadenosine-5’-phosphosulfate coupling with an ATP regeneration system. Appl. Microbiol. Biotechnol. 101, 7535–7544 (2017).
Cai, T. et al. Cell-free chemoenzymatic starch synthesis from carbon dioxide. Science 373, 1523–1527 (2021).
Petchey, M. R., Rowlinson, B., Lloyd, R. C., Fairlamb, I. J. S. & Grogan, G. Biocatalytic synthesis of moclobemide using the amide bond synthetase McbA coupled with an ATP recycling system. ACS Catal. 10, 4659–4663 (2020).
Gottschalk, J., Blaschke, L., Aßmann, M., Kuballa, J. & Elling, L. Integration of a nucleoside triphosphate regeneration system in the one-pot synthesis of UDP-sugars and hyaluronic acid. ChemSusChem 13, 3074–3083 (2021).
Xu, R. et al. Closed-loop system driven by ADP phosphorylation from pyrophosphate affords equimolar transformation of ATP to 3′-phosphoadenosine-5′-phosphosulfate. ACS Catal. 11, 10405–10415 (2021).
Hatzios, S. K. et al. The Mycobacterium tuberculosis CysQ phosphatase modulates the biosynthesis of sulfated glycolipids and bacterial growth. Bioorg. Med. Chem. Lett. 21, 4956–4959 (2011).
Chapman, E., Best, M. D., Hanson, S. R. & Wong, C. H. Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew. Chem. Int. Ed. 43, 3526–3548 (2004).
Jin, X. et al. Optimizing the sulfation-modification system for scale preparation of chondroitin sulfate A. Carbohydr. Polym. 246, 116570 (2020).
Günal, S., Hardman, R., Kopriva, S. & Mueller, J. W. Sulfation pathways from red to green. J. Biol. Chem. 294, 12293–12312 (2019).
Motomura, K. et al. A new subfamily of polyphosphate kinase 2 (class III PPK2) catalyzes both nucleoside monophosphate phosphorylation and nucleoside diphosphate phosphorylation. Appl. Environ. Microbiol. 80, 2602–2608 (2014).
Ishige, K., Zhang, H. & Kornberg, A. Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP. Proc. Natl Acad. Sci. USA 99, 16684–16688 (2002).
Mougous, J. D. et al. Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 11, 721–729 (2004).
Zhang, W. et al. Enzymatic production of chondroitin oligosaccharides and its sulfate derivatives. Front Bioeng. Biotechnol. 10, 951740 (2022).
Morciano, G. et al. Use of luciferase probes to measure ATP in living cells and animals. Nat. Protoc. 12, 1542–1562 (2017).
Duffel, M. W., Marshal, A. D., McPhie, P., Sharma, V. & Jakoby, W. B. Enzymatic aspects of the phenol (aryl) sulfotransferases. Drug Metab. Rev. 33, 369–395 (2001).
Li, F. L., Zhou, Q., Wei, W., Gao, J. & Zhang, Y. W. Switching the substrate specificity from NADH to NADPH by a single mutation of NADH oxidase from Lactobacillus rhamnosus. Int. J. Biol. Macromol. 135, 328–336 (2019).
Nakamura, M., Bhatnagar, A. & Sadoshima, J. Overview of pyridine nucleotides review series. Circ. Res. 111, 604–610 (2012).
Hallé, F., Fin, A., Rovira, A. R. & Tor, Y. Emissive synthetic cofactors: enzymatic interconversions of tzA analogues of ATP, NAD+, NADH, NADP+, and NADPH. Angew. Chem. Int. Ed. Engl. 57, 1087–1090 (2018).
Rath, V. L., Verdugo, D. & Hemmerich, S. Sulfotransferase structural biology and inhibitor discovery. Drug Discov. Today 9, 1003–1011 (2004).
Huq, A. H. et al. Dopamine 4-sulfate: effects on isolated perfused rat heart and role of atria. Life Sci. 43, 1599–1606 (1988).
Chen, B. et al. Sulfation modification of dopamine in brain regulates aggregative behavior of animals. Natl Sci. Rev. 9, nwab163 (2022).
Everett, J.R. Applications of metabolic phenotyping in pharmaceutical research and development, The Handbook of Metabolic Phenotyping. (eds. J. C. Lindon, J. K. Nicholson & E. Holmes) 407–447 (Elsevier, 2019).
Ye, D. et al. Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase. J. Biol. Chem. 276, 37630–37639 (2001).
Barbosa, A. C. S., Feng, Y., Yu, C., Huang, M. & Xie, W. Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases. Expert. Opin. Drug. Metab. Toxicol. 15, 329–339 (2019).
Kakuta, Y., Pedersen, L. G., Pedersen, L. C. & Negishi, M. Conserved structural motifs in the sulfotransferase family. Trends Biochem. Sci. 23, 129–130 (1998).
Xie, L. et al. Combinatorial biosynthesis of sulfated benzenediol lactones with a phenolic sulfotransferase from Fusarium graminearum PH-1. mSphere 5, e00949–00920 (2020).
Burkart, M. D., Izumi, M., Chapman, E., Lin, C. H. & Wong, C. H. Regeneration of PAPS for the enzymatic synthesis of sulfated oligosaccharides. J. Org. Chem. 65, 5565–5574 (2000).
Xu, Y. et al. Chemoenzymatic synthesis of homogeneous ultralow molecular weight heparins. Science 334, 498–501 (2011).
Badri, A., Williams, A., Xia, K., Linhardt, R. J. & Koffas, M. A. G. Increased 3’-phosphoadenosine-5’-phosphosulfate levels in engineered Escherichia coli cell lysate facilitate the in vitro synthesis of chondroitin sulfate A. Biotechnol. J. 14, e1800436 (2019).
Parnell, A. E. et al. Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures. Proc. Natl Acad. Sci. USA 115, 3350–3355 (2018).
Nocek, B. P. et al. Structural insights into substrate selectivity and activity of bacterialpolyphosphate kinases. ACS Catal. 8, 10746–10760 (2018).
Erickson, A. I., Sarsam, R. D. & Fisher, A. J. Crystal structures of Mycobacterium tuberculosis CysQ, with substrate and products bound. Biochemistry 54, 6830–6841 (2015).
Neuwald, A. F. et al. cysQ, a gene needed for cysteine synthesis in Escherichia coli K-12 only during aerobic growth. J. Bacteriol. 174, 415–425 (1992).
Bounaga, A. et al. Microbial transformations by sulfur bacteria can recover value from phosphogypsum: a global problem and a possible solution. Biotechnol. Adv. 57, 107949 (2022).
Hatzios, S. K. & Bertozzi, C. R. The regulation of sulfur metabolism in Mycobacterium tuberculosis. PLoS Pathog. 7, e1002036 (2011).
Paritala, H. & Carroll, K. S. New targets and inhibitors of mycobacterial sulfur metabolism. Infect. Disord. Drug Targets 13, 85–115 (2013).
Xia, Y. et al. T5 exonuclease-dependent assembly offers a low-cost method for efficient cloning and site-directed mutagenesis. Nucleic Acids Res. 47, e15 (2019).
Zhu, X. et al. Combining CRISPR–Cpf1 and recombineering facilitates fast and efficient genome editing in Escherichia coli. ACS Synth. Biol. 11, 1897–1907 (2022).
Robert, X. & Gouet, P. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320–W324 (2014).
Kumar, S., Stecher, G., Li, M., Knyaz, C. & Tamura, K. MEGA X: molecular evolutionary genetics analysis across computing platforms. Mol. Biol. Evol. 35, 1547–1549 (2018).
Huang, H. et al. Structure and cleavage pattern of a hyaluronate 3-glycanohydrolase in the glycoside hydrolase 79 family. Carbohydr. Polym. 277, 118838 (2022).
Qu, G., Li, A., Acevedo-Rocha, C. G., Sun, Z. & Reetz, M. T. The crucial role of methodology development in directed evolution of selective enzymes. Angew. Chem. Int. Ed. 59, 13204–13231 (2020).
Xu, R. et al. Engineering sulfonate group donor regeneration systems to boost biosynthesis of sulfated compounds. Figshare. https://doi.org/10.6084/m9.figshare.24449563 (2023).
- SEO Powered Content & PR Distribution. Get Amplified Today.
- PlatoData.Network Vertical Generative Ai. Empower Yourself. Access Here.
- PlatoAiStream. Web3 Intelligence. Knowledge Amplified. Access Here.
- PlatoESG. Carbon, CleanTech, Energy, Environment, Solar, Waste Management. Access Here.
- PlatoHealth. Biotech and Clinical Trials Intelligence. Access Here.
- Source: https://www.nature.com/articles/s41467-023-43195-1