EC
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1.8.1.1
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Deleted entry: | cysteamine dehydrogenase |
[EC 1.8.1.1 created 1961, deleted 1972] |
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EC |
1.8.3.7 |
Accepted name: |
formylglycine-generating enzyme |
Reaction: |
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O |
Glossary: |
3-oxo-L-alanine = formylglycine = Cα-formylglycine = FGly |
Other name(s): |
sulfatase-modifying factor 1; Cα-formylglycine-generating enzyme 1; SUMF1 (gene name) |
Systematic name: |
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming) |
Comments: |
Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Dierks, T., Schmidt, B. and von Figura, K. Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 94 (1997) 11963–11968. [DOI] [PMID: 9342345] |
2. |
Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273 (1998) 25560–25564. [DOI] [PMID: 9748219] |
3. |
Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, S.L., Mutenda, K., Wenzel, D., von Figura, K. and Dierks, T. Molecular characterization of the human Cα-formylglycine-generating enzyme. J. Biol. Chem. 280 (2005) 14900–14910. [DOI] [PMID: 15657036] |
4. |
Roeser, D., Preusser-Kunze, A., Schmidt, B., Gasow, K., Wittmann, J.G., Dierks, T., von Figura, K. and Rudolph, M.G. A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc. Natl. Acad. Sci. USA 103 (2006) 81–86. [DOI] [PMID: 16368756] |
5. |
Carlson, B.L., Ballister, E.R., Skordalakes, E., King, D.S., Breidenbach, M.A., Gilmore, S.A., Berger, J.M. and Bertozzi, C.R. Function and structure of a prokaryotic formylglycine-generating enzyme. J. Biol. Chem. 283 (2008) 20117–20125. [DOI] [PMID: 18390551] |
6. |
Holder, P.G., Jones, L.C., Drake, P.M., Barfield, R.M., Banas, S., de Hart, G.W., Baker, J. and Rabuka, D. Reconstitution of formylglycine-generating enzyme with copper(II) for aldehyde tag conversion. J. Biol. Chem. 290 (2015) 15730–15745. [DOI] [PMID: 25931126] |
7. |
Knop, M., Engi, P., Lemnaru, R. and Seebeck, F.P. In vitro reconstitution of formylglycine-generating enzymes requires copper(I). ChemBioChem 16 (2015) 2147–2150. [DOI] [PMID: 26403223] |
8. |
Knop, M., Dang, T.Q., Jeschke, G. and Seebeck, F.P. Copper is a cofactor of the formylglycine-generating enzyme. ChemBioChem 18 (2017) 161–165. [DOI] [PMID: 27862795] |
9. |
Meury, M., Knop, M. and Seebeck, F.P. Structural basis for copper-oxygen mediated C-H bond activation by the formylglycine-generating enzyme. Angew. Chem. Int. Ed. Engl. (2017) . [DOI] [PMID: 28544744] |
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[EC 1.8.3.7 created 2014] |
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EC |
1.13.11.19 |
Accepted name: |
cysteamine dioxygenase |
Reaction: |
cysteamine + O2 = hypotaurine |
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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] |
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[EC 1.13.11.19 created 1972, modified 2006] |
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EC |
3.5.1.92 |
Accepted name: |
pantetheine hydrolase |
Reaction: |
(R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol |
Other name(s): |
pantetheinase; vanin; vanin-1 |
Systematic name: |
(R)-pantetheine amidohydrolase |
Comments: |
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56093-18-6 |
References: |
1. |
Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262–267. [PMID: 440106] |
2. |
Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175–181. [DOI] [PMID: 6549111] |
3. |
Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149–152. [DOI] [PMID: 10567687] |
4. |
Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus
homing. Immunity 5 (1996) 391–405. [DOI] [PMID: 8934567] |
5. |
Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Duprè, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149–154. [DOI] [PMID: 11042271] |
6. |
Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode
isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296–306. [PMID: 11491533] |
7. |
Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.. [PMID: 11380987] |
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[EC 3.5.1.92 created 2006] |
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EC |
5.3.3.14 |
Accepted name: |
trans-2-decenoyl-[acyl-carrier protein] isomerase |
Reaction: |
a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein] |
Other name(s): |
β-hydroxydecanoyl thioester dehydrase; trans-2-cis-3-decenoyl-ACP isomerase; trans-2,cis-3-decenoyl-ACP isomerase; trans-2-decenoyl-ACP isomerase; FabM; decenoyl-[acyl-carrier-protein] Δ2-trans-Δ3-cis-isomerase |
Systematic name: |
decenoyl-[acyl-carrier protein] Δ2-trans-Δ3-cis-isomerase |
Comments: |
While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-80-2 |
References: |
1. |
Brock, D.J.H., Kass, L.R. and Bloch, K. β-Hydroxydecanoyl thioester dehydrase. II. Mode of action. J. Biol. Chem. 242 (1967) 4432–4440. [PMID: 4863740] |
2. |
Bloch, K. Enzymatic synthesis of monounsaturated fatty acids. Acc. Chem. Res. 2 (1969) 193–202. |
3. |
Marrakchi, H., Choi, K.H. and Rock, C.O. A new mechanism for anaerobic unsaturated fatty acid formation in
Streptococcus pneumoniae. J. Biol. Chem. 277 (2002) 44809–44816. [DOI] [PMID: 12237320] |
4. |
Cronan, J.E., Jr. and Rock, C.O. Biosynthesis of membrane lipids. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn, vol. 1, ASM Press, Washington, DC, 1996, pp. 612–636. |
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[EC 5.3.3.14 created 2006] |
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