| EC |
1.1.1.373 |
| Accepted name: |
sulfolactaldehyde 3-reductase |
| Reaction: |
(2S)-2,3-dihydroxypropane-1-sulfonate + NAD+ = (2S)-3-sulfolactaldehyde + NADH + H+ |
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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, PDB |
| 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] |
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| [EC 1.1.1.373 created 2014] |
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| 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] |
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| [EC 4.2.1.177 created 2021] |
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| 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] |
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| [EC 4.4.1.41 created 2021] |
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