The Enzyme Database

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EC 1.1.1.373     
Accepted name: sulfolactaldehyde 3-reductase
Reaction: (2S)-2,3-dihydroxypropane-1-sulfonate + NAD+ = (2S)-3-sulfolactaldehyde + NADH + H+
For diagram of sulphoglycolysis of sulfoquinovose, click here
Glossary: (2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate
(2S)-2,3-dihydroxypropane-1-sulfonic acid = (2S)-3-sulfopropanediol = (S)-DHPS
Other name(s): yihU (gene name)
Systematic name: (2S)-2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114–117. [DOI] [PMID: 24463506]
2.  Sharma, M., Abayakoon, P., Lingford, J.P., Epa, R., John, A., Jin, Y., Goddard-Borger, E.D., Davies, G.J. and Williams, S.J. Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase. ACS Catalysis 10 (2020) 2826–2836. [DOI]
[EC 1.1.1.373 created 2014]
 
 
EC 4.2.1.177     
Accepted name: (2S)-3-sulfopropanediol dehydratase
Reaction: (2S)-2,3-dihydroxypropane-1-sulfonate = 3-oxopropane-1-sulfonate + H2O
Glossary: (2S)-2,3-dihydroxypropane-1-sulfonic acid = (2S)-3-sulfopropanediol = (S)-DHPS
Other name(s): hpfG (gene name); (S)-DHPS dehydratase
Systematic name: (2S)-2,3-dihydroxypropane-1-sulfonate hydro-lyase
Comments: The enzyme, characterized from the bacterium Klebsiella oxytoca, participates in (2S)-2,3-dihydroxypropane-1-sulfonate degradation. The active form of the enzyme contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (AdoMet) and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, J., Wei, Y., Lin, L., Teng, L., Yin, J., Lu, Q., Chen, J., Zheng, Y., Li, Y., Xu, R., Zhai, W., Liu, Y., Liu, Y., Cao, P., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Two radical-dependent mechanisms for anaerobic degradation of the globally abundant organosulfur compound dihydroxypropanesulfonate. Proc. Natl. Acad. Sci. USA 117 (2020) 15599–15608. [DOI] [PMID: 32571930]
[EC 4.2.1.177 created 2021]
 
 
EC 4.4.1.41     
Accepted name: (2S)-3-sulfopropanediol sulfolyase
Reaction: (2S)-2,3-dihydroxypropane-1-sulfonate = hydroxyacetone + sulfite
Glossary: (2S)-2,3-dihydroxypropane-1-sulfonate = (2S)-3-sulfopropanediol
Other name(s): DHPS sulfolyase; hpsG (gene name)
Systematic name: (2S)-2,3-dihydroxypropane-1-sulfonate sulfite-lyase
Comments: The enzyme, characterized from the human gut bacterium Bilophila wadsworthia, contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (AdoMet) and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, J., Wei, Y., Lin, L., Teng, L., Yin, J., Lu, Q., Chen, J., Zheng, Y., Li, Y., Xu, R., Zhai, W., Liu, Y., Liu, Y., Cao, P., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Two radical-dependent mechanisms for anaerobic degradation of the globally abundant organosulfur compound dihydroxypropanesulfonate. Proc. Natl. Acad. Sci. USA 117 (2020) 15599–15608. [DOI] [PMID: 32571930]
[EC 4.4.1.41 created 2021]
 
 


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