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] |
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|
|
|
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] |
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|
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|
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] |
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|
|
|
EC |
1.5.1.23 |
Accepted name: |
tauropine dehydrogenase |
Reaction: |
tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+ |
Glossary: |
tauropine = N2-(D-1-carboxyethyl)-2-aminoethanesulfonate |
Other name(s): |
2-N-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming) |
Systematic name: |
N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming) |
Comments: |
In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 104645-74-1 |
References: |
1. |
Gäde, G. Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa. Eur. J. Biochem. 160 (1986) 311–318. [DOI] [PMID: 3769931] |
|
[EC 1.5.1.23 created 1989] |
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|
|
|
EC
|
1.8.1.3
|
Deleted entry: | hypotaurine dehydrogenase. The reaction is now known to be catalyzed by EC 1.14.13.8, flavin-containing monooxygenase. |
[EC 1.8.1.3 created 1972, deleted 2022] |
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|
|
|
EC |
1.13.11.19 |
Accepted name: |
cysteamine dioxygenase |
Reaction: |
cysteamine + O2 = hypotaurine |
|
For diagram of taurine biosynthesis, click here |
Glossary: |
cysteamine = 2-aminoethanethiol |
Other name(s): |
ADO (gene name); persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase |
Systematic name: |
2-aminoethanethiol:oxygen oxidoreductase |
Comments: |
A non-heme iron protein that is involved in the biosynthesis of taurine. 3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-41-4 |
References: |
1. |
Cavallini, D., de Marco, C., Scandurra, R., Duprè, S. and Graziani, M.T. The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem. 241 (1966) 3189–3196. [PMID: 5912113] |
2. |
Wood, J.L. and Cavallini, D. Enzymic oxidation of cysteamine to hypotaurine in the absence of a
cofactor. Arch. Biochem. Biophys. 119 (1967) 368–372. [DOI] [PMID: 6052430] |
3. |
Cavallini, D., Federici, G., Ricci, G., Duprè, S. and Antonucci, A. The specificity of cysteamine oxygenase. FEBS Lett. 56 (1975) 348–351. [DOI] [PMID: 1157952] |
4. |
Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410–415. [DOI] [PMID: 3657558] |
5. |
Dominy, J.E., Jr., Simmons, C.R., Hirschberger, L.L., Hwang, J., Coloso, R.M. and Stipanuk, M.H. Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. J. Biol. Chem. 282 (2007) 25189–25198. [PMID: 17581819] |
|
[EC 1.13.11.19 created 1972, modified 2006] |
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|
|
|
EC |
1.13.11.20 |
Accepted name: |
cysteine dioxygenase |
Reaction: |
L-cysteine + O2 = 3-sulfinoalanine |
|
For diagram of taurine biosynthesis, click here |
Other name(s): |
cysteine oxidase |
Systematic name: |
L-cysteine:oxygen oxidoreductase |
Comments: |
Requires Fe2+ and NAD(P)H. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-59-0 |
References: |
1. |
Lombardini, J.B., Singer, T.P. and Boyer, P.D. Cystein oxygenase. II. Studies on the mechanism of the reaction with 18oxygen. J. Biol. Chem. 244 (1969) 1172–1175. [PMID: 5767301] |
|
[EC 1.13.11.20 created 1972, modified 1976] |
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EC |
1.14.11.17 |
Accepted name: |
taurine dioxygenase |
Reaction: |
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2 |
Other name(s): |
2-aminoethanesulfonate dioxygenase; α-ketoglutarate-dependent taurine dioxygenase |
Systematic name: |
taurine, 2-oxoglutarate:oxygen oxidoreductase (sulfite-forming) |
Comments: |
Requires FeII. The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 197809-75-9 |
References: |
1. |
Eichhorn, E., Van Der Poeg, J.R., Kertesz, M.A. and Leisinger, T. Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J. Biol. Chem. 272 (1997) 23031–23036. [DOI] [PMID: 9287300] |
|
[EC 1.14.11.17 created 2000] |
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EC
|
1.14.13.97
|
Transferred entry: | taurochenodeoxycholate 6α-hydroxylase. Now EC 1.14.14.57, taurochenodeoxycholate 6α-hydroxylase
|
[EC 1.14.13.97 created 2005, deleted 2018] |
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|
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|
EC |
1.14.14.5 |
Accepted name: |
alkanesulfonate monooxygenase |
Reaction: |
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O |
Glossary: |
an alkanesulfonate = R-CH2-SO3-
an aldehyde = R-CHO |
Other name(s): |
SsuD; sulfate starvation-induced protein 6; alkanesulfonate,reduced-FMN:oxygen oxidoreductase |
Systematic name: |
alkanesulfonate,FMNH2:oxygen oxidoreductase |
Comments: |
The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.38). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 256383-67-2 |
References: |
1. |
Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639–26646. [DOI] [PMID: 10480865] |
|
[EC 1.14.14.5 created 2002] |
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|
|
EC |
1.14.14.57 |
Accepted name: |
taurochenodeoxycholate 6α-hydroxylase |
Reaction: |
(1) taurochenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH—hemoprotein reductase] + H2O (2) lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH—hemoprotein reductase] + H2O |
|
For diagram of the biosynthesis of cholic-acid conjugates, click here |
Glossary: |
taurochenodeoxycholic acid = N-(3α,7α-dihydroxy-5β-cholan-24-oyl)taurine
taurohyocholic acid = N-(3α,6α,7α-trihydroxy-5β-cholan-24-oyl)taurine
hyodeoxycholate = 3α,6α-dihydroxy-5β-cholan-24-oate
lithocholate = 3α-hydroxy-5β-cholan-24-oate |
Other name(s): |
CYP3A4; CYP4A21; taurochenodeoxycholate 6α-monooxygenase |
Systematic name: |
taurochenodeoxycholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105669-85-0 |
References: |
1. |
Araya, Z. and Wikvall, K. 6α-Hydroxylation of taurochenodeoxycholic acid and lithocholic acid by CYP3A4 in human liver microsomes. Biochim. Biophys. Acta 1438 (1999) 47–54. [DOI] [PMID: 10216279] |
2. |
Araya, Z., Hellman, U. and Hansson, R. Characterisation of taurochenodeoxycholic acid 6α-hydroxylase from pig liver microsomes. Eur. J. Biochem. 231 (1995) 855–861. [DOI] [PMID: 7649186] |
3. |
Kramer, W., Sauber, K., Baringhaus, K.H., Kurz, M., Stengelin, S., Lange, G., Corsiero, D., Girbig, F., Konig, W. and Weyland, C. Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J. Biol. Chem. 276 (2001) 7291–7301. [DOI] [PMID: 11069906] |
4. |
Lundell, K., Hansson, R. and Wikvall, K. Cloning and expression of a pig liver taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21): a novel member of the CYP4A subfamily. J. Biol. Chem. 276 (2001) 9606–9612. [DOI] [PMID: 11113117] |
5. |
Lundell, K. and Wikvall, K. Gene structure of pig sterol 12α-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21). Biochim. Biophys. Acta 1634 (2003) 86–96. [DOI] [PMID: 14643796] |
6. |
Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708] |
|
[EC 1.14.14.57 created 2005 asEC 1.14.13.97, transferred 2018 to EC 1.14.14.57] |
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|
|
|
EC |
2.3.1.65 |
Accepted name: |
bile acid-CoA:amino acid N-acyltransferase |
Reaction: |
choloyl-CoA + glycine = CoA + glycocholate |
|
For diagram of the biosynthesis of cholic-acid conjugates, click here |
Glossary: |
choloyl-CoA = 3α,7α,12α-trihydroxy-5β-cholan-24-oyl-CoA |
Other name(s): |
glycine—taurine N-acyltransferase; amino acid N-choloyltransferase; BAT; glycine N-choloyltransferase; BACAT; cholyl-CoA glycine-taurine N-acyltransferase; cholyl-CoA:taurine N-acyltransferase |
Systematic name: |
choloyl-CoA:glycine N-choloyltransferase |
Comments: |
Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-β-alanine can act as substrates, but more slowly [4]. The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase [7]. Bile-acid—amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol [4]. This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7, cholate—CoA ligase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65979-40-0 |
References: |
1. |
Czuba, B. and Vessey, D.A. Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver. J. Biol. Chem. 255 (1980) 5296–5299. [PMID: 7372637] |
2. |
Jordan, T.W., Lee, R. and Lim, W.C. Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver. Biochem. Int. 1 (1980) 325–330. |
3. |
Vessey, D.A. The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver. J. Biol. Chem. 254 (1979) 2059–2063. [PMID: 422567] |
4. |
Johnson, M.R., Barnes, S., Kwakye, J.B. and Diasio, R.B. Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J. Biol. Chem. 266 (1991) 10227–10233. [PMID: 2037576] |
5. |
Falany, C.N., Xie, X., Wheeler, J.B., Wang, J., Smith, M., He, D. and Barnes, S. Molecular cloning and expression of rat liver bile acid CoA ligase. J. Lipid Res. 43 (2002) 2062–2071. [PMID: 12454267] |
6. |
He, D., Barnes, S. and Falany, C.N. Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization. J. Lipid Res. 44 (2003) 2242–2249. [DOI] [PMID: 12951368] |
7. |
O'Byrne, J., Hunt, M.C., Rai, D.K., Saeki, M. and Alexson, S.E. The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J. Biol. Chem. 278 (2003) 34237–34244. [DOI] [PMID: 12810727] |
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[EC 2.3.1.65 created 1983, modified 2005] |
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|
EC |
2.3.1.176 |
Accepted name: |
propanoyl-CoA C-acyltransferase |
Reaction: |
3α,7α,12α-trihydroxy-5β-cholanoyl-CoA + propanoyl-CoA = CoA + 3α,7α,12α-trihydroxy-24-oxo-5β-cholestanoyl-CoA |
|
For diagram of cholic acid biosynthesis (sidechain), click here |
Other name(s): |
SCP2 (gene name); peroxisomal thiolase 2; sterol carrier protein-χ; SCPχ; PTE-2 (ambiguous); propionyl-CoA C2-trimethyltridecanoyltransferase; 3-oxopristanoyl-CoA hydrolase; 3-oxopristanoyl-CoA thiolase; peroxisome sterol carrier protein thiolase; sterol carrier protein; oxopristanoyl-CoA thiolase; peroxisomal 3-oxoacyl coenzyme A thiolase; SCPx; 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA 2-C-4,8,12-trimethyltridecanoyltransferase |
Systematic name: |
3α,7α,12α-trihydroxy-5β-cholanoyl-CoA:propanoyl-CoA C-acyltransferase |
Comments: |
Also acts on dihydroxy-5β-cholestanoyl-CoA and other branched chain acyl-CoA derivatives. The enzyme catalyses the penultimate step in the formation of bile acids. The bile acid moiety is transferred from the acyl-CoA thioester (RCO-SCoA) to either glycine or taurine (NH2R′) by EC 2.3.1.65, bile acid-CoA:amino acid N-acyltransferase [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Pedersen, J.I. and Gustafsson, J. Conversion of 3α,7α,12α-trihydroxy-5β-cholestanoic acid into cholic acid by rat liver peroxisomes. FEBS Lett. 121 (1980) 345–348. [DOI] [PMID: 7461136] |
2. |
Kase, F., Björkhem, I. and Pedersen, J.I. Formation of cholic acid from 3α,7α,12α-trihydroxy-5β-cholestanoic acid by rat liver peroxisomes. J. Lipid Res. 24 (1983) 1560–1567. [PMID: 6668450] |
3. |
Falany, C.N., Johnson, M.R., Barnes, S. and Diasio, R.B. Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J. Biol. Chem. 269 (1994) 19375–19379. [PMID: 8034703] |
4. |
Seedorf, U., Brysch, P., Engel, T., Schrage, K. and Assmann, G. Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity. J. Biol. Chem. 269 (1994) 21277–21283. [PMID: 8063752] |
5. |
Wanders, R.J.A., Denis, S., Wouters, F., Wirtz, K.W.A. and Seedorf, U. Sterol carrier protein X (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochem. Biophys. Res. Commun. 236 (1997) 565–569. [DOI] [PMID: 9245689] |
6. |
Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708] |
|
[EC 2.3.1.176 created 2005 (EC 2.3.1.154 created 2000, incorporated 2015)] |
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|
|
|
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] |
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|
|
|
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] |
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|
|
|
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 |
3.5.1.24 |
Accepted name: |
choloylglycine hydrolase |
Reaction: |
glycocholate + H2O = cholate + glycine |
|
For diagram of cholic acid conjugates biosynthesis, click here |
Glossary: |
glycocholate = N-(3α,7α,12α-trihydroxy-5β-cholan-24-oyl)glycine
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate |
Other name(s): |
glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase |
Systematic name: |
glycocholate amidohydrolase |
Comments: |
Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-07-9 |
References: |
1. |
Nair, P.P., Gordon, M. and Reback, J. The enzymatic cleavage of the carbon-nitrogen bond in 3α,7α,12α-trihydroxy-5-β-cholan-24-oylglycine. J. Biol. Chem. 242 (1967) 7–11. [PMID: 6016335] |
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Stellwag, E.J. and Hylemon, P.B. Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452 (1976) 165–176. [DOI] [PMID: 10993] |
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[EC 3.5.1.24 created 1972] |
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EC |
3.5.1.74 |
Accepted name: |
chenodeoxycholoyltaurine hydrolase |
Reaction: |
chenodeoxycholoyltaurine + H2O = chenodeoxycholate + taurine |
Glossary: |
chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate |
Systematic name: |
chenodeoxycholoyltaurine amidohydrolase |
Comments: |
Some other taurine conjugates are hydrolysed, but not glycine conjugates of bile acids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125752-75-2 |
References: |
1. |
Kawamoto, K., Horibe, I. and Uchida, K. Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. (Tokyo) 106 (1989) 1049–1053. [PMID: 2628421] |
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[EC 3.5.1.74 created 1992] |
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EC
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3.6.3.36
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Transferred entry: | taurine-transporting ATPase. Now EC 7.6.2.7, taurine-transporting ATPase
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[EC 3.6.3.36 created 2000, deleted 2018] |
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EC |
4.1.1.29 |
Accepted name: |
sulfinoalanine decarboxylase |
Reaction: |
3-sulfino-L-alanine = hypotaurine + CO2 |
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For diagram of taurine biosynthesis, click here |
Other name(s): |
cysteine-sulfinate decarboxylase; L-cysteinesulfinic acid decarboxylase; cysteine-sulfinate decarboxylase; CADCase/CSADCase; CSAD; cysteic decarboxylase; cysteinesulfinic acid decarboxylase; cysteinesulfinate decarboxylase; sulfoalanine decarboxylase; 3-sulfino-L-alanine carboxy-lyase |
Systematic name: |
3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming) |
Comments: |
A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-10-9 |
References: |
1. |
Guion-Rain, M.C., Portemer, C. and Chatagner, F. Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties. Biochim. Biophys. Acta 384 (1975) 265–276. [DOI] [PMID: 236774] |
2. |
Jacobsen, J.G., Thomas, L.L. and Smith, L.H., Jr. Properties and distribution of mammalian L-cysteine sulfinate carboxy-lyases. Biochim. Biophys. Acta 85 (1964) 103–116. [PMID: 14159288] |
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[EC 4.1.1.29 created 1961, deleted 1972, reinstated 1976, modified 1983, modified 1999] |
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EC |
4.1.1.122 |
Accepted name: |
L-cysteate decarboxylase |
Reaction: |
L-cysteate = taurine + CO2 |
Other name(s): |
CAD |
Systematic name: |
L-cysteate carboxy-lyase (taurine-forming) |
Comments: |
Requires pyridoxal 5′-phosphate. The enzyme, characterized from chicken, is specific for L-cysteate and has poor activity with 3-sulfino-L-alanine. cf. EC 4.1.1.29, sulfinoalanine decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Malatesta, M., Mori, G., Acquotti, D., Campanini, B., Peracchi, A., Antin, P.B. and Percudani, R. Birth of a pathway for sulfur metabolism in early amniote evolution. Nat Ecol Evol 4 (2020) 1239–1246. [DOI] [PMID: 32601391] |
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[EC 4.1.1.122 created 2022] |
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EC |
4.4.1.10 |
Accepted name: |
cysteine lyase |
Reaction: |
L-cysteine + sulfite = L-cysteate + hydrogen sulfide |
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For diagram of taurine biosynthesis, click here |
Other name(s): |
cysteine (sulfite) lyase; L-cysteine hydrogen-sulfide-lyase (adding sulfite) |
Systematic name: |
L-cysteine hydrogen-sulfide-lyase (adding sulfite; L-cysteate-forming) |
Comments: |
A pyridoxal-phosphate protein. Can use a second molecule of cysteine (producing lanthionine), or other alkyl thiols, as a replacing agent. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9079-86-1 |
References: |
1. |
Tolosa, E.A., Chepurnova, N.K., Khomutov, R.M. and Severin, E.S. Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo. Biochim. Biophys. Acta 171 (1969) 369–371. [DOI] [PMID: 5813025] |
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[EC 4.4.1.10 created 1972] |
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EC |
4.4.1.38 |
Accepted name: |
isethionate sulfite-lyase |
Reaction: |
isethionate = acetaldehyde + sulfite |
Glossary: |
isethionate = 2-hydroxyethanesulfonate |
Other name(s): |
islA (gene name) |
Systematic name: |
isethionate sulfite-lyase |
Comments: |
The enzyme, characterized from the human gut bacterium Bilophila wadsworthia, participates in a taurine degradation pathway that leads to sulfide production. The active form of the enzyme contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (SAM) and a [4Fe-4S] cluster. |
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] |
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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] |
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[EC 4.4.1.38 created 2021] |
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EC |
7.6.2.7 |
Accepted name: |
ABC-type taurine transporter |
Reaction: |
ATP + H2O + taurine-[taurine-binding protein][side 1] = ADP + phosphate + taurine[side 2] + [taurine-binding protein][side 1] |
Other name(s): |
tauABC (gene names); taurine ABC transporter; taurine-transporting ATPase |
Systematic name: |
ATP phosphohydrolase (ABC-type, taurine-importing) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of taurine. In Escherichia coli the enzyme imports a range of sulfonates (including taurine) that can be used as a source of sulfur. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
van der Ploeg, J.R., Weiss, M.A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M.A. and Leisinger, T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178 (1996) 5438–5446. [DOI] [PMID: 8808933] |
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[EC 7.6.2.7 created 2000 as EC 3.6.3.36, transferred 2018 to EC 7.6.2.7] |
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