This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: 3-sulfolactate degradation II
|Superclasses:||Degradation/Utilization/Assimilation → Inorganic Nutrients Metabolism → Sulfur Compounds Metabolism → Sulfolactate Degradation|
Some taxa known to possess this pathway include : Roseovarius nubinhibens ISM
Expected Taxonomic Range:
Organosulfonate compounds are found in the environment as both natural products and xenobiotics. They are catabolized by microorganisms that utilize the carbon and sulfur moieties. Aliphatic C3 sulfonates are widespread natural products found in the environment and are derived from microbial, plant and animal sources. The bacterial catabolism of C3 sulfonates such as (RS)-3-sulfolactate (racemic sulfolactate), 3-sulfopyruvate, and L-cysteate has been studied. The work has focused on the catabolism of the carbon moiety, the fate of the sulfonate group, and the transport systems necessary for organosulfonates to cross the cell membrane. Bioinformatics analyses have shown a diversity in pathways of sulfonate degradation in bacteria from both marine and terrestrial environments (in [Denger10] and reviewed in [Cook06]).
To date, three desulfonation pathways have been proposed for the degradation of (RS)-3-sulfolactate including:
(1) sulfolactate degradation I: direct desulfonation of (2R)-3-sulfolactate by the enzyme R-sulfolactate sulfo-lyase, encoded by the suyA and suyB genes. (2S)-3-sulfolactate is isomerized to (2R)-3-sulfolactate via 3-sulfopyruvate by two dehydrogenases of opposite stereochemistry, encoded by slcC and comC.
(2) sulfolactate degradation II: oxidation of (RS)-3-sulfolactate to 3-sulfopyruvate by sulfolactate dehydrogenase (slcD), followed by decarboxylation of sulfopyruvate to sulfoacetaldehyde by the sulfopyruvate decarboxylase encoded by the comD and comE genes, desulfonation to acetyl phosphate by xsc, and conversion of acetyl phosphate to acetyl-CoA.
(3) sulfolactate degradation III: oxidation of (RS)-3-sulfolactate to 3-sulfopyruvate by sulfolactate dehydrogenase (slcD), transamination of 3-sulfopyruvate to L-cysteate, and desulfonation of L-cysteate to pyruvate by the product of the cuyA gene.
In all of these pathways the bisulfite or sulfite produced by the desulfonation reaction is proposed to be transported through the cell membrane and oxidized to sulfate by a periplasmic enzyme, possibly the product of genes sorAB in some organisms [Denger09, Mayer10, Cook06].
In each of these pathways a different enzymatic desulfonation mechanism is used. In sulfolactate degradation I desulfonation occurs via (2R)-3-sulfolactate by EC 18.104.22.168, sulfolactate sulfo-lyase (see 3-sulfolactate sulfo-lyase from Paracoccus pantotrophus NKNCYSA and R-sulfolactate sulfo-lyase from Chromohalobacter salexigens DSM 3043 for examples [Rein05].
In sulfolactate degradation II desulfonation occurs via sulfoacetaldehyde by EC 22.214.171.124, sulfoacetaldehyde acetyltransferase. See sulfoacetaldehyde acetyltransferase, encoded by the xsc gene in Roseovarius nubinhibens ISM for example [Denger09, Mayer10].
In sulfolactate degradation III desulfonation occurs via L-cysteate by EC 126.96.36.199, (S)-cysteate sulfo-lyase. See L-cysteate sulfo-lyase from Ruegeria pomeroyi DSS-3 and L-cysteate sulfo-lyase from Roseovarius nubinhibens ISM for examples [Denger09, Denger06].
Superpathways: superpathway of sulfolactate degradation
Denger06: Denger K, Smits TH, Cook AM (2006). "L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T)." Biochem J 394(Pt 3);657-64. PMID: 16302849
Denger09: Denger K, Mayer J, Buhmann M, Weinitschke S, Smits TH, Cook AM (2009). "Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfolyase." J Bacteriol 191(18);5648-56. PMID: 19581363
Denger10: Denger K, Cook AM (2010). "Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase." Microbiology 156(Pt 3);967-74. PMID: 20007648
Mayer10: Mayer J, Huhn T, Habeck M, Denger K, Hollemeyer K, Cook AM (2010). "2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase." Microbiology 156(Pt 5);1556-64. PMID: 20150239
Rein05: Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM (2005). "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA." Microbiology 151(Pt 3);737-47. PMID: 15758220
Atteia06: Atteia A, van Lis R, Gelius-Dietrich G, Adrait A, Garin J, Joyard J, Rolland N, Martin W (2006). "Pyruvate formate-lyase and a novel route of eukaryotic ATP synthesis in Chlamydomonas mitochondria." J Biol Chem 281(15);9909-18. PMID: 16452484
Bergmeyer63: Bergmeyer, H.U., Holz, G., Klotzsch, H., Lang, G. (1963). "[Phosphotransacetylase from Clostridium kluyveri. Culture of the bacterium, isolation, crystallization and properties of the enzyme.]." Biochem Z 338;114-21. PMID: 14087284
Bock99: Bock AK, Glasemacher J, Schmidt R, Schonheit P (1999). "Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima." J Bacteriol 1999;181(6);1861-7. PMID: 10074080
Bologna10: Bologna FP, Campos-Bermudez VA, Saavedra DD, Andreo CS, Drincovich MF (2010). "Characterization of Escherichia coli EutD: a phosphotransacetylase of the ethanolamine operon." J Microbiol 48(5);629-36. PMID: 21046341
CamposBermudez10: Campos-Bermudez VA, Bologna FP, Andreo CS, Drincovich MF (2010). "Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation." FEBS J 277(8);1957-66. PMID: 20236319
Chae11: Chae, Lee (2011). "The functional annotation of protein sequences was performed by the in-house Ensemble Enzyme Prediction Pipeline (E2P2, version 1.0). E2P2 systematically integrates results from three molecular function annotation algorithms using an ensemble classification scheme. For a given genome, all protein sequences are submitted as individual queries against the base-level annotation methods. The individual methods rely on homology transfer to annotate protein sequences, using single sequence (BLAST, E-value cutoff <= 1e-30, subset of SwissProt 15.3) and multiple sequence (Priam, November 2010; CatFam, version 2.0, 1% FDR profile library) models of enzymatic functions. The base-level predictions are then integrated into a final set of annotations using an average weighted integration algorithm, where the weight of each prediction from each individual method was determined via a 0.632 bootstrap process over 1000 rounds of testing. The training and testing data for E2P2 and the BLAST reference database were drawn from protein sequences with experimental support of existence, compiled from SwissProt release 15.3."
Denger01: Denger K, Ruff J, Rein U, Cook AM (2001). "Sulphoacetaldehyde sulpho-lyase (EC 188.8.131.52) from Desulfonispora thiosulfatigenes: purification, properties and primary sequence." Biochem J 357(Pt 2);581-6. PMID: 11439112
Denger04: Denger K, Ruff J, Schleheck D, Cook AM (2004). "Rhodococcus opacus expresses the xsc gene to utilize taurine as a carbon source or as a nitrogen source but not as a sulfur source." Microbiology 150(Pt 6);1859-67. PMID: 15184572
Drake81: Drake HL, Hu SI, Wood HG (1981). "Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase." J Biol Chem 1981;256(21);11137-44. PMID: 7287757
Glover: Glover V, Littlewood JT, Sandler M, Peatfield R, Petty R, Rose FC "Platelet monoamine oxidase activity and headache: relationship to personality and smoking." Psychopharmacol Bull NIL;20(3);536-8. PMID: 6473660
Graham09b: Graham DE, Taylor SM, Wolf RZ, Namboori SC (2009). "Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase." Biochem J 424(3);467-78. PMID: 19761441
Graupner00: Graupner M, Xu H, White RH (2000). "Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M." J Bacteriol 2000;182(17);4862-7. PMID: 10940029
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