The Enzyme Database

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EC 1.1.1.313     
Accepted name: sulfoacetaldehyde reductase (NADPH)
Reaction: isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+
Glossary: isethionate = 2-hydroxyethanesulfonate
2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): isfD (gene name)
Systematic name: isethionate:NADP+ oxidoreductase
Comments: Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433, sulfoacetaldehyde reductase (NADH).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Krejcik, Z., Hollemeyer, K., Smits, T.H. and Cook, A.M. Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase. Microbiology 156 (2010) 1547–1555. [DOI] [PMID: 20133363]
[EC 1.1.1.313 created 2011, modified 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 1.2.1.73     
Accepted name: sulfoacetaldehyde dehydrogenase
Reaction: 2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): SafD
Systematic name: 2-sulfoacetaldehyde:NAD+ oxidoreductase
Comments: This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A.M. and Smits, T.H.M. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190 (2008) 159–168. [DOI] [PMID: 18506422]
[EC 1.2.1.73 created 2008]
 
 
EC 1.2.1.81     
Accepted name: sulfoacetaldehyde dehydrogenase (acylating)
Reaction: 2-sulfoacetaldehyde + CoA + NADP+ = sulfoacetyl-CoA + NADPH + H+
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): SauS
Systematic name: 2-sulfoacetaldehyde:NADP+ oxidoreductase (CoA-acetylating)
Comments: The enzyme is involved in degradation of sulfoacetate. In this pathway the reaction is catalysed in the reverse direction. The enzyme is specific for sulfoacetaldehyde and NADP+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Weinitschke, S., Hollemeyer, K., Kusian, B., Bowien, B., Smits, T.H. and Cook, A.M. Sulfoacetate is degraded via a novel pathway involving sulfoacetyl-CoA and sulfoacetaldehyde in Cupriavidus necator H16. J. Biol. Chem. 285 (2010) 35249–35254. [DOI] [PMID: 20693281]
[EC 1.2.1.81 created 2011]
 
 
EC 1.4.99.2     
Accepted name: taurine dehydrogenase
Reaction: taurine + H2O + acceptor = 2-sulfoacetaldehyde + NH3 + reduced acceptor
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): taurine:(acceptor) oxidoreductase (deaminating)
Systematic name: taurine:acceptor oxidoreductase (deaminating)
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 50812-14-1
References:
1.  Kondo, H., Kagotani, K., Oshima, M. and Ishimoto, M. Purification and some properties of taurine dehydrogenase from a bacterium. J. Biochem. (Tokyo) 73 (1973) 1269–1278. [PMID: 4724302]
[EC 1.4.99.2 created 1976]
 
 
EC 2.3.3.15     
Accepted name: sulfoacetaldehyde acetyltransferase
Reaction: acetyl phosphate + sulfite = 2-sulfoacetaldehyde + phosphate
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): Xsc
Systematic name: acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2-oxoethyl-forming)
Comments: The reaction occurs in the reverse direction to that shown above. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56941-15-2
References:
1.  Ruff, J., Denger, K. and Cook, A.M. Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. Biochem. J. 369 (2003) 275–285. [DOI] [PMID: 12358600]
[EC 2.3.3.15 created 2003]
 
 
EC 2.6.1.55     
Accepted name: taurine—2-oxoglutarate transaminase
Reaction: taurine + 2-oxoglutarate = 2-sulfoacetaldehyde + L-glutamate
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): taurine aminotransferase; taurine transaminase; taurine—α-ketoglutarate aminotransferase; taurine—glutamate transaminase
Systematic name: taurine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on D,L-3-amino-isobutanoate, β-alanine and 3-aminopropanesulfonate. Involved in the microbial utilization of β-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-52-2
References:
1.  Toyama, S., Misono, H. and Soda, K. Crystalline taurine:α-ketoglutarate aminotransferase from Achromobacter superficialis. Biochem. Biophys. Res. Commun. 46 (1972) 1374–1379. [DOI] [PMID: 5012173]
2.  Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1–6. [DOI] [PMID: 12471498]
[EC 2.6.1.55 created 1976, modified 2003]
 
 
EC 2.6.1.77     
Accepted name: taurine—pyruvate aminotransferase
Reaction: taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
For diagram of reaction, click here
Glossary: taurine = 2-aminoethanesulfonate
hypotaurine = 2-aminoethanesulfinate
2-sulfoacetaldehyde = 2-oxoethanesulfonate
2-sulfinoacetaldehyde = 2-oxoethanesulfinate
Other name(s): Tpa
Systematic name: taurine:pyruvate aminotransferase
Comments: The enzyme from the bacterium Bilophila wadsworthia requires pyridoxal 5′-phosphate as a cofactor, and catalyses a reversible reaction that starts an anaerobic taurine degradation pathway. β-Alanine is also a significant amino group donor. The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyses to sulfite and acetaldehyde. Unlike, EC 2.6.1.55, taurine—2-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51901-18-9
References:
1.  Laue, H. and Cook, A.M. Biochemical and molecular characterization of taurine:pyruvate transaminase from the anaerobe Bilophila wadsworthia. Eur. J. Biochem. 267 (2000) 6841–6848. [DOI] [PMID: 11082195]
2.  Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1–6. [DOI] [PMID: 12471498]
3.  Masepohl, B., Fuhrer, F. and Klipp, W. Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source. FEMS Microbiol. Lett. 205 (2001) 105–111. [DOI] [PMID: 11728723]
4.  Felux, A.K., Denger, K., Weiss, M., Cook, A.M. and Schleheck, D. Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination followed by spontaneous desulfination to yield acetaldehyde and, finally, acetate for growth. J. Bacteriol. 195 (2013) 2921–2930. [DOI] [PMID: 23603744]
[EC 2.6.1.77 created 2003]
 
 
EC 4.1.1.79     
Accepted name: sulfopyruvate decarboxylase
Reaction: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO2
For diagram of coenzyme-M biosynthesis, click here
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
2-sulfoacetaldehyde = 2-oxoethanesulfonate
Other name(s): sulfopyruvate carboxy-lyase
Systematic name: 3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming)
Comments: Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 303155-97-7
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 182 (2000) 4862–4867. [DOI] [PMID: 10940029]
[EC 4.1.1.79 created 2002]
 
 


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