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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Chemical Compound Review: 

AC1LCV1V     [5-(6-aminopurin-9-yl)-3,4- dihydroxy...

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High impact information on lipoyl-AMP

  • Lipoyl-AMP is bound deeply in the bifurcated pocket of LplA and adopts a U-shaped conformation [1].
  • Both lipoyltransferase I and II could not use lipoic acid plus MgATP as a substrate in place of lipoyl-AMP [2].
  • The lipoylation was dependent on lipoyl-AMP, apo-H-protein, and lipoyltransferase [3].
  • A nonhydrolyzable lipoyl-AMP analogue was found to competitively inhibit both ACP-dependent and ATP-dependent reactions of LplA, suggesting that the same active site catalyzes two chemically diverse reactions [4].
 

Anatomical context of lipoyl-AMP

  • The purified recombinant apo-H-protein was lipoylated and consequently activated in vitro with lipoyl-AMP as a lipoyl donor by lipoyltransferase purified 150-fold from bovine liver mitochondria [3].

References

  1. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. Kim, d.o. .J., Kim, K.H., Lee, H.H., Lee, S.J., Ha, J.Y., Yoon, H.J., Suh, S.W. J. Biol. Chem. (2005) [Pubmed]
  2. Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria. Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y. J. Biol. Chem. (1994) [Pubmed]
  3. Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform. Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y. J. Biol. Chem. (1992) [Pubmed]
  4. The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase. Jordan, S.W., Cronan, J.E. J. Bacteriol. (2003) [Pubmed]
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