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1.1.1.313

Accepted name:

sulfoacetaldehyde reductase

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

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]

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:

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]

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]

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, EXPASY, KEGG, MetaCyc, UM-BBD, 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]

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]

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]

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]

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]