| EC |
1.13.11.19 |
| Accepted name: |
cysteamine dioxygenase |
| Reaction: |
2-aminoethanethiol + O2 = hypotaurine |
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For diagram of taurine biosynthesis, click here |
| Other name(s): |
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. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 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, IUBMB, KEGG, 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. [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. [PMID: 1157952] |
| 4. |
Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410–415. [PMID: 3657558] |
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| [EC 1.13.11.19 created 1972, modified 2006] |
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