Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	793 proteins
Enzyme class ^help_outline	EC 1.1.1.373 sulfolactaldehyde 3-reductase
GO Molecular Function ^help_outline	GO:0061596 3-sulfolactaldehyde reductase activity

Reaction participants Show >> << Hide

Name ^help_outline (2S)-3-sulfopropanediol Identifier CHEBI:176527 Charge -1 Formula C3H7O5S InChIKey^help_outline YPFUJZAAZJXMIP-VKHMYHEASA-M SMILES^help_outline OC[C@H](O)CS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NAD⁺ Identifier CHEBI:57540 (Beilstein: 3868403) ^help_outline Charge -1 Formula C21H26N7O14P2 InChIKey^help_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILES^help_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline (2S)-3-sulfolactaldehyde Identifier CHEBI:90109 Charge -1 Formula C3H5O5S InChIKey^help_outline GVEIZEMJOBQMCQ-VKHMYHEASA-M SMILES^help_outline [O-]S(C[C@H](C(=O)[H])O)(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) ^help_outline Charge -2 Formula C21H27N7O14P2 InChIKey^help_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILES^help_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,073 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:40511	RHEA:40512	RHEA:40513	RHEA:40514
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	793 proteins		3 proteins
EC numbers ^help_outline	1.1.1.373
Gene Ontology ^help_outline	GO:0061596
KEGG ^help_outline				R10719
MetaCyc ^help_outline			RXN-15299
EcoCyc ^help_outline			RXN-15299

Publications

Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle.

Denger K., Weiss M., Felux A.K., Schneider A., Mayer C., Spiteller D., Huhn T., Cook A.M., Schleheck D.

Sulphoquinovose (SQ, 6-deoxy-6-sulphoglucose) has been known for 50 years as the polar headgroup of the plant sulpholipid in the photosynthetic membranes of all higher plants, mosses, ferns, algae and most photosynthetic bacteria. It is also found in some non-photosynthetic bacteria, and SQ is par ... >> More

Sulphoquinovose (SQ, 6-deoxy-6-sulphoglucose) has been known for 50 years as the polar headgroup of the plant sulpholipid in the photosynthetic membranes of all higher plants, mosses, ferns, algae and most photosynthetic bacteria. It is also found in some non-photosynthetic bacteria, and SQ is part of the surface layer of some Archaea. The estimated annual production of SQ is 10,000,000,000 tonnes (10 petagrams), thus it comprises a major portion of the organo-sulphur in nature, where SQ is degraded by bacteria. However, despite evidence for at least three different degradative pathways in bacteria, no enzymic reaction or gene in any pathway has been defined, although a sulphoglycolytic pathway has been proposed. Here we show that Escherichia coli K-12, the most widely studied prokaryotic model organism, performs sulphoglycolysis, in addition to standard glycolysis. SQ is catabolised through four newly discovered reactions that we established using purified, heterologously expressed enzymes: SQ isomerase, 6-deoxy-6-sulphofructose (SF) kinase, 6-deoxy-6-sulphofructose-1-phosphate (SFP) aldolase, and 3-sulpholactaldehyde (SLA) reductase. The enzymes are encoded in a ten-gene cluster, which probably also encodes regulation, transport and degradation of the whole sulpholipid; the gene cluster is present in almost all (>91%) available E. coli genomes, and is widespread in Enterobacteriaceae. The pathway yields dihydroxyacetone phosphate (DHAP), which powers energy conservation and growth of E. coli, and the sulphonate product 2,3-dihydroxypropane-1-sulphonate (DHPS), which is excreted. DHPS is mineralized by other bacteria, thus closing the sulphur cycle within a bacterial community. << Less

Nature 507:114-117(2014) [PubMed] [EuropePMC]

This publication is cited by 3 other entries.

Comments

Published in: 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:10.1021/acscatal.9b04427