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, 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] |
|
[EC 1.1.1.373 created 2014] |
|
|
|
|
EC |
1.1.1.390 |
Accepted name: |
sulfoquinovose 1-dehydrogenase |
Reaction: |
sulfoquinovose + NAD+ = 6-deoxy-6-sulfo-D-glucono-1,5-lactone + NADH + H+ |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Glossary: |
sulfoquinovose = 6-deoxy-6-sulfo-D-glucopyranose |
Systematic name: |
6-deoxy-6-sulfo-D-glucopyranose:NAD+ 1-oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. Activity with NADP+ is only 4% of that with NAD+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [DOI] [PMID: 26195800] |
|
[EC 1.1.1.390 created 2015] |
|
|
|
|
EC |
1.1.1.432 |
Accepted name: |
6-dehydroglucose reductase |
Reaction: |
D-glucose + NADP+ = 6-dehydro-D-glucose + NADPH + H+ |
Glossary: |
quinovose = 6-deoxy-D-glucopyranose |
Other name(s): |
D-glucose 6-dehydrogenase; smoB (gene name); squF (gene name) |
Systematic name: |
D-glucose:NADP+ 6-oxidoreductase |
Comments: |
The enzyme, characterized from alphaproteobacteria, is involved in a D-sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sharma, M., Lingford, J.P., Petricevic, M., Snow, A.J.D., Zhang, Y., Jarva, M.A., Mui, J.W., Scott, N.E., Saunders, E.C., Mao, R., Epa, R., da Silva, B.M., Pires, D.E.V., Ascher, D.B., McConville, M.J., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Proc. Natl. Acad. Sci. USA 119 (2022) e2116022119. [DOI] [PMID: 35074914] |
2. |
Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI] |
|
[EC 1.1.1.432 created 2022] |
|
|
|
|
EC |
1.1.1.433 |
Accepted name: |
sulfoacetaldehyde reductase (NADH) |
Reaction: |
isethionate + NAD+ = 2-sulfoacetaldehyde + NADH + H+ |
Glossary: |
isethionate = 2-hydroxyethanesulfonate
2-sulfoacetaldehyde = 2-oxoethanesulfonate |
Other name(s): |
sarD (gene name); tauF (gene name); sqwF (gene name); BkTauF |
Systematic name: |
isethionate:NAD+ oxidoreductase |
Comments: |
The enzymes from the bacteria Bilophila wadsworthia and Clostridium sp. MSTE9 catalyse the reaction only in the reduction direction. In the bacterium Bifidobacterium kashiwanohense the optimal reaction pH for sulfoacetaldehyde reduction is 7.5, while that for isethionate oxidation is 10.0. cf. EC 1.1.1.313, sulfoacetaldehyde reductase (NADPH). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Peck, S.C., Denger, K., Burrichter, A., Irwin, S.M., Balskus, E.P. and Schleheck, D. A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia. Proc. Natl. Acad. Sci. USA 116 (2019) 3171–3176. [DOI] [PMID: 30718429] |
2. |
Xing, M., Wei, Y., Zhou, Y., Zhang, J., Lin, L., Hu, Y., Hua, G.,, N. Nanjaraj Urs, A., Liu, D., Wang, F., Guo, C., Tong, Y., Li, M., Liu, Y., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Radical-mediated C-S bond cleavage in C2 sulfonate degradation by anaerobic bacteria. Nat. Commun. 10:1609 (2019). [DOI] [PMID: 30962433] |
3. |
Zhou, Y., Wei, Y., Nanjaraj Urs, A.N., Lin, L., Xu, T., Hu, Y., Ang, E.L., Zhao, H., Yuchi, Z. and Zhang, Y. Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacterium Bifidobacterium kashiwanohense. Biosci. Rep. 39 (2019) . [DOI] [PMID: 31123167] |
4. |
Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI] |
|
[EC 1.1.1.433 created 2022] |
|
|
|
|
EC |
1.2.1.97 |
Accepted name: |
3-sulfolactaldehyde dehydrogenase |
Reaction: |
(2S)-3-sulfolactaldehyde + NAD(P)+ + H2O = (2S)-3-sulfolactate + NAD(P)H + H+ |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Glossary: |
(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate |
Other name(s): |
SLA dehydrogenase |
Systematic name: |
(2S)-3-sulfolactaldehyde:NAD(P)+ oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. Also acts on succinate semialdehyde. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [DOI] [PMID: 26195800] |
|
[EC 1.2.1.97 created 2015] |
|
|
|
|
EC |
1.14.14.181 |
Accepted name: |
sulfoquinovose monooxygenase |
Reaction: |
6-sulfo-D-quinovose + FMNH2 + O2 = 6-dehydro-D-glucose + FMN + sulfite + H2O |
Glossary: |
D-quinovose = 6-deoxy-D-glucopyranose
6-dehydro-D-glucose = 6-oxo-D-quinovose |
Other name(s): |
6-deoxy-6-sulfo-D-glucose monooxygenase; smoC (gene name); squD (gene name) |
Systematic name: |
6-sulfo-D-quinovose,FMNH2:oxygen oxidoreductase |
Comments: |
The enzyme, characterized from the bacteria Agrobacterium fabrum and Rhizobium oryzae, is involved in a D-sulfoquinovose degradation pathway. FMNH2 is provided by an associated FMN reductase [SmoA, EC 1.5.1.42, FMN reductase (NADH)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI] |
2. |
Sharma, M., Lingford, J.P., Petricevic, M., Snow, A.J.D., Zhang, Y., Jarva, M.A., Mui, J.W., Scott, N.E., Saunders, E.C., Mao, R., Epa, R., da Silva, B.M., Pires, D.E.V., Ascher, D.B., McConville, M.J., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Proc. Natl. Acad. Sci. USA 119 (2022) e2116022119. [DOI] [PMID: 35074914] |
|
[EC 1.14.14.181 created 20022] |
|
|
|
|
EC |
2.2.1.14 |
Accepted name: |
6-deoxy-6-sulfo-D-fructose transaldolase |
Reaction: |
6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + β-D-fructofuranose 6-phosphate |
Glossary: |
(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate |
Other name(s): |
sftT (gene name) |
Systematic name: |
6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glyceronetransferase |
Comments: |
The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose. The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Frommeyer, B., Fiedler, A.W., Oehler, S.R., Hanson, B.T., Loy, A., Franchini, P., Spiteller, D. and Schleheck, D. Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway. iScience 23:101510 (2020). [DOI] [PMID: 32919372] |
|
[EC 2.2.1.14 created 2021] |
|
|
|
|
EC |
2.2.1.15 |
Accepted name: |
6-deoxy-6-sulfo-D-fructose transketolase |
Reaction: |
(1) 6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde-3-phosphate = D-xylulose-5-phosphate + 4-deoxy-4-sulfo-D-erythrose (2) 4-deoxy-4-sulfo-D-erythrulose + D-glyceraldehyde-3-phosphate = D-xylulose-5-phosphate + sulfoacetaldehyde |
Other name(s): |
6-deoxy-6-sulfo-erythrulose transketolase; sqwGH (gene name) |
Systematic name: |
6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glycolaldehydetransferase |
Comments: |
The enzyme, characterized from the bacterium Clostridium sp. MSTE9, is involved in a D-sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI] |
|
[EC 2.2.1.15 created 2022] |
|
|
|
|
EC |
2.7.1.184 |
Accepted name: |
sulfofructose kinase |
Reaction: |
ATP + 6-deoxy-6-sulfo-D-fructose = ADP + 6-deoxy-6-sulfo-D-fructose 1-phosphate |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Other name(s): |
yihV (gene name) |
Systematic name: |
ATP:6-deoxy-6-sulfo-D-fructose 1-phosphotransferase |
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] |
|
[EC 2.7.1.184 created 2014] |
|
|
|
|
EC |
3.1.1.99 |
Accepted name: |
6-deoxy-6-sulfogluconolactonase |
Reaction: |
6-deoxy-6-sulfo-D-glucono-1,5-lactone + H2O = 6-deoxy-6-sulfo-D-gluconate |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Other name(s): |
SGL lactonase |
Systematic name: |
6-deoxy-6-sulfo-D-glucono-1,5-lactone lactonohydrolase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [DOI] [PMID: 26195800] |
|
[EC 3.1.1.99 created 2016] |
|
|
|
|
EC |
3.13.1.1 |
Accepted name: |
UDP-sulfoquinovose synthase |
Reaction: |
UDP-α-D-sulfoquinovopyranose + H2O = UDP-α-D-glucose + sulfite |
|
For diagram of UDP-glucose, UDP-galactose and UDP-glucuronate biosynthesis, click here |
Other name(s): |
sulfite:UDP-glucose sulfotransferase; UDPsulfoquinovose synthase; UDP-6-sulfo-6-deoxyglucose sulfohydrolase |
Systematic name: |
UDP-6-sulfo-6-deoxy-α-D-glucose sulfohydrolase |
Comments: |
Requires NAD+, which appears to oxidize UDP-α-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Essigmann, B., Gler, S., Narang, R.A., Linke, D. and Benning, C. Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 95 (1998) 1950–1955. [DOI] [PMID: 9465123] |
2. |
Essigmann, B., Hespenheide, B.M., Kuhn, L.A. and Benning, C. Prediction of the active-site structure and NAD+ binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis. Arch. Biochem. Biophys. 369 (1999) 30–41. [DOI] [PMID: 10462438] |
3. |
Mulichak, A.M., Theisen, M.J., Essigmann, B., Benning, C. and Garavito, R.M. Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose. Proc. Natl. Acad. Sci. USA 96 (1999) 13097–13102. [DOI] [PMID: 10557279] |
4. |
Sanda, S., Leustek, T., Theisen, M., Garavito, R.M. and Benning, C. Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro. J. Biol. Chem. 276 (2001) 3941–3946. [DOI] [PMID: 11073956] |
|
[EC 3.13.1.1 created 2001, modified 2010] |
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|
|
|
EC |
4.1.2.57 |
Accepted name: |
sulfofructosephosphate aldolase |
Reaction: |
6-deoxy-6-sulfo-D-fructose 1-phosphate = glycerone phosphate + (2S)-3-sulfolactaldehyde |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Glossary: |
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate |
Other name(s): |
yihT (gene name) |
Systematic name: |
6-deoxy-6-sulfofructose-1-phosphate (2S)-3-sulfolactaldehyde-lyase (glycerone-phosphate-forming) |
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] |
|
[EC 4.1.2.57 created 2014] |
|
|
|
|
EC |
4.1.2.58 |
Accepted name: |
2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase |
Reaction: |
2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate = (2S)-3-sulfolactaldehyde + pyruvate |
Glossary: |
(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate |
Other name(s): |
KDSG aldolase |
Systematic name: |
2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate (2S)-3-sulfolactaldehyde-lyase (pyruvate-forming) |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [DOI] [PMID: 26195800] |
|
[EC 4.1.2.58 created 2016] |
|
|
|
|
EC |
4.2.1.162 |
Accepted name: |
6-deoxy-6-sulfo-D-gluconate dehydratase |
Reaction: |
6-deoxy-6-sulfo-D-gluconate = 2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate + H2O |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Other name(s): |
SG dehydratase |
Systematic name: |
6-deoxy-6-sulfo-D-gluconate hydro-lyase (2-dehydro-3,6-dideoxy-6-sulfo-D-gluconate-forming) |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas putida SQ1, participates in a sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Felux, A.K., Spiteller, D., Klebensberger, J. and Schleheck, D. Entner-Doudoroff pathway for sulfoquinovose degradation in Pseudomonas putida SQ1. Proc. Natl. Acad. Sci. USA 112 (2015) E4298–E4305. [DOI] [PMID: 26195800] |
|
[EC 4.2.1.162 created 2016] |
|
|
|
|
EC |
5.1.3.43 |
Accepted name: |
sulfoquinovose mutarotase |
Reaction: |
6-sulfo-α-D-quinovose = 6-sulfo-β-D-quinovose |
Systematic name: |
6-sulfo-D-quinovose 1-epimerase |
Comments: |
The enzyme is found in bacteria that possess sulfoglycolytic pathways. The enzyme can also act on other aldohexoses such as D-galactose, D-glucose, D-glucose-6-phosphate, and D-glucuronate, but with lower efficiency. Does not act on D-mannose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Abayakoon, P., Lingford, J.P., Jin, Y., Bengt, C., Davies, G.J., Yao, S., Goddard-Borger, E.D. and Williams, S.J. Discovery and characterization of a sulfoquinovose mutarotase using kinetic analysis at equilibrium by exchange spectroscopy. Biochem. J. 475 (2018) 1371–1383. [PMID: 29535276] |
|
[EC 5.1.3.43 created 2019] |
|
|
|
|
EC |
5.3.1.31 |
Accepted name: |
sulfoquinovose isomerase |
Reaction: |
(1) β-sulfoquinovose = 6-deoxy-6-sulfo-D-fructose (2) β-sulfoquinovose = 6-sulfo-D-rhamnose |
|
For diagram of sulphoglycolysis of sulfoquinovose, click here |
Glossary: |
sulfoquinovose = 6-deoxy-6-sulfo-D-glucopyranose |
Other name(s): |
yihS (gene name) |
Systematic name: |
6-deoxy-6-sulfo-β-D-glucopyranose aldose-ketose-isomerase |
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., Epa, R., Jin, Y., Lingford, J.P., Shimada, T., Nakano, M., Mui, J.W., Ishihama, A., Goddard-Borger, E.D., Davies, G.J. and Williams, S.J. Molecular basis of sulfosugar selectivity in sulfoglycolysis. ACS Cent. Sci. 7 (2021) 476–487. [DOI] [PMID: 33791429] |
|
[EC 5.3.1.31 created 2014, modified 2022] |
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|
|
|
EC |
5.3.1.37 |
Accepted name: |
4-deoxy-4-sulfo-D-erythrose isomerase |
Reaction: |
4-deoxy-4-sulfo-D-erythrose = 4-deoxy-4-sulfo-D-erythrulose |
Other name(s): |
sqwI (gene name) |
Systematic name: |
4-deoxy-4-sulfo-D-erythrose ketose-aldose isomerase |
Comments: |
The enzyme, characterized from the bacterium Clostridium sp. MSTE9, is involved in a D-sulfoquinovose degradation pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. [DOI] |
|
[EC 5.3.1.37 created 2022] |
|
|
|
|