ExplorEnz: Search Results

Your query returned 19 entries. Printable version

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]

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]

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:

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]

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]

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]

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]

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:

[EC 1.14.14.181 created 20022]

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:

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]

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]

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:

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]

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]

3.2.1.199

Accepted name:

sulfoquinovosidase

Reaction:

a 6-sulfo-α-D-quinovosyl diacylglycerol + H₂O = 6-sulfo-α-D-quinovose + a 1,2-diacylglycerol

Glossary:

quinovose = 6-deoxy-D-glucopyranose

Other name(s):

yihQ (gene name); 6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase

Systematic name:

6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase (configuration-retaining)

Comments:

The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyses terminal non-reducing α-sulfoquinovoside residues in α-sulfoquinovosyl diacylglycerides and α-sulfoquinovosyl glycerol using a retaining mechanism. The enzyme belongs to the glycosyl hydrolase GH31 family.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Shibuya, I. and Benson, A. A. Hydrolysis of α-sulphoquinovosides by β-galactosidase. Nature 192 (1961) 1186–1187. [DOI]
2.	Speciale, G., Jin, Y., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat. Chem. Biol. 12 (2016) 215–217. [DOI] [PMID: 26878550]

[EC 3.2.1.199 created 2016]

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]

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:

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]

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]

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]

4.3.1.30

Accepted name:

dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase

Reaction:

dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor = dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose + NH₃ + L-methionine + 5′-deoxyadenosine + acceptor

For diagram of dTDP-D-desosamine biosynthesis, click here

Other name(s):

desII (gene name); eryCV (gene name); MegCV

Systematic name:

dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose ammonia lyase (dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose-forming)

Comments:

The enzyme, which is a member of the ’AdoMet radical’ (radical SAM) family, is involved in biosynthesis of TDP-α-D-desosamine. The reaction starts by the transfer of an electron from the reduced form of the enzyme’s [4Fe-4S] cluster to S-adenosyl-L-methionine, spliting it into methionine and the radical 5-deoxyadenosin-5′-yl, which attacks the sugar substrate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Szu, P.H., Ruszczycky, M.W., Choi, S.H., Yan, F. and Liu, H.W. Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine. J. Am. Chem. Soc. 131 (2009) 14030–14042. [DOI] [PMID: 19746907]
2.	Ruszczycky, M.W., Choi, S.H. and Liu, H.W. Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII. J. Am. Chem. Soc. 132 (2010) 2359–2369. [DOI] [PMID: 20121093]
3.	Ruszczycky, M.W., Choi, S.H., Mansoorabadi, S.O. and Liu, H.W. Mechanistic studies of the radical S-adenosyl-L-methionine enzyme DesII: EPR characterization of a radical intermediate generated during its catalyzed dehydrogenation of TDP-D-quinovose. J. Am. Chem. Soc. 133 (2011) 7292–7295. [DOI] [PMID: 21513273]

[EC 4.3.1.30 created 2011]

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]

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:

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]

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]