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Chemical Compound Review

pantetheine     2,4-dihydroxy-3,3-dimethyl-N- [2-(2...

Synonyms: pantotheine, D-Pantetheine, HMDB03426, LS-47637, CTK8I8721, ...
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Disease relevance of pantetheine

  • The plant ACP expressed in E. coli contains pantetheine and approximately 50% is present in vivo as acyl-ACP [1].
  • The separation of the half-molecular weight, nonidentical subunits (I and II) of the pigeon liver fatty acid synthetase complex has been achieved on a large (20 mg) scale by affinity chromatography on Sepharose epsilon-aminocaproyl pantetheine [2].
  • Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase [3].
  • The low level of endogenous fatty acid synthesis in Acholeplasma laidlawii A strain EF22 was found to be caused by a deficiency of pantetheine in the lipid-depleted growth medium [4].

High impact information on pantetheine


Biological context of pantetheine


Anatomical context of pantetheine


Associations of pantetheine with other chemical compounds


Gene context of pantetheine

  • Pantetheine also serves as an amino acid acceptor in reactions catalyzed by AspRS, IleRS, and MetRS, forming corresponding aminoacyl-S-pantetheine thioesters [10].

Analytical, diagnostic and therapeutic context of pantetheine

  • Finally bioorthogonal pantetheine analogues were shown to target carrier proteins with high specificity in vivo and undergo chemoselective ligation to reporters in crude cell lysate [18].
  • This reagent now represents a simple and convenient tool both for quantification of the pantetheine thiol and for labelling this site for peptide mapping and isolation [19].


  1. Purification and characterization of recombinant spinach acyl carrier protein I expressed in Escherichia coli. Guerra, D.J., Dziewanowska, K., Ohlrogge, J.B., Beremand, P.D. J. Biol. Chem. (1988) [Pubmed]
  2. Subunits of fatty acid synthetase complexes. Enzymatic activities and properties of the half-molecular weight nonidentical subunits of pigeon liver fatty acid synthetase. Lornitzo, F.A., Qureshi, A.A., Porter, J.W. J. Biol. Chem. (1975) [Pubmed]
  3. Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase. Martin, D.P., Drueckhammer, D.G. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  4. Control of membrane polar lipid composition in Acholeplasma laidlawii a by the extent of saturated fatty acid synthesis. Christiansson, A., Wieslander, A. Biochim. Biophys. Acta (1980) [Pubmed]
  5. Small-angle neutron-scattering and electron microscope studies of the chicken liver fatty acid synthase. Stoops, J.K., Wakil, S.J., Uberbacher, E.C., Bunick, G.J. J. Biol. Chem. (1987) [Pubmed]
  6. Biosynthetic thiolase from Zoogloea ramigera. II. Inactivation with haloacetyl CoA analogs. Davis, J.T., Chen, H.H., Moore, R., Nishitani, Y., Masamune, S., Sinskey, A.J., Walsh, C.T. J. Biol. Chem. (1987) [Pubmed]
  7. Two functional domains of coenzyme A activate catalysis by coenzyme A transferase. Pantetheine and adenosine 3'-phosphate 5'-diphosphate. Fierke, C.A., Jencks, W.P. J. Biol. Chem. (1986) [Pubmed]
  8. Measurement of distance between the active serine of the thioesterase domain and the pantetheine thiol of fatty acid synthase by fluorescence resonance energy transfer. Foster, R.J., Poulose, A.J., Bonsall, R.F., Kolattukudy, P.E. J. Biol. Chem. (1985) [Pubmed]
  9. Purification and properties of a pantetheine-hydrolyzing enzyme from pig kidney. Wittwer, C.T., Burkhard, D., Ririe, K., Rasmussen, R., Brown, J., Wyse, B.W., Hansen, R.G. J. Biol. Chem. (1983) [Pubmed]
  10. Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: possible link between noncoded and coded peptide synthesis. Jakubowski, H. Biochemistry (1998) [Pubmed]
  11. Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes. Schuster, H., Rautenstrauss, B., Mittag, M., Stratmann, D., Schweizer, E. Eur. J. Biochem. (1995) [Pubmed]
  12. Effects of pantetheine on cholesteryl ester synthesis in the arterial wall of rats on high cholesterol diet. Shirai, K., Matsuoka, N., Saito, Y., Kumagai, A., Okuda, H. Tohoku J. Exp. Med. (1979) [Pubmed]
  13. Modulation of HMG-CoA reductase activity by pantetheine/pantethine. Cighetti, G., Del Puppo, M., Paroni, R., Galli Kienle, M. Biochim. Biophys. Acta (1988) [Pubmed]
  14. Regulation of fatty acid synthetase activity. The 4'-phosphopantetheine hydrolase of rat liver. Sobhy, C. J. Biol. Chem. (1979) [Pubmed]
  15. Mechanism of action of glutaryl-CoA and butyryl-CoA dehydrogenases. Purification of glutaryl-CoA dehydrogenase. Gomes, B., Fendrich, G., Abeles, R.H. Biochemistry (1981) [Pubmed]
  16. Specific modification of the condensation domain of fatty acid synthase and the determination of the primary structure of the modified active site peptides. Poulose, A.J., Bonsall, R.F., Kolattukudy, P.E. Arch. Biochem. Biophys. (1984) [Pubmed]
  17. Investigating the role of the geminal dimethyl groups of coenzyme A: synthesis and studies of a didemethyl analogue. Vogel, K.W., Stark, L.M., Mishra, P.K., Yang, W., Drueckhammer, D.G. Bioorg. Med. Chem. (2000) [Pubmed]
  18. Synthesis and evaluation of bioorthogonal pantetheine analogues for in vivo protein modification. Meier, J.L., Mercer, A.C., Rivera, H., Burkart, M.D. J. Am. Chem. Soc. (2006) [Pubmed]
  19. Reaction of chloroacetyl-CoA with rabbit fatty acid synthase. A new method to label specifically and quantify pantetheine prosthetic groups. McCarthy, A.D., Hardie, D.G. FEBS Lett. (1982) [Pubmed]
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