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The Arabidopsis class II sirtuin is a lysine deacetylase and interacts with mitochondrial energy metabolism

König, Ann-Christine; Hartl, Markus; Pham, Phuong Anh; Laxa, Miriam; Boersema, Paul J.; Orwat, Anne; Kalitventseva, Ievgeniia; Plöchinger, Magdalena; Braun, Hans-Peter; Leister, Dario; Mann, Matthias; Wachter, Andreas; Fernie, Alisdair R.; Finkemeier, Iris (Rockville, Md. : American Society of Plant Physiologists, 2014)

The posttranslational regulation of proteins by lysine (Lys) acetylation has recently emerged to occur not only on histones, but also on organellar proteins in plants and animals. In particular, the catalytic activities ...
L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria

Gau, Achim E.; Heindl, Achim; Nodop, Anke; Kahmann, Uwe; Pistorius, Elfriede K. (Berlin : De Gruyter, 2007)

The two closely related fresh water cyanobacteria Synechococcus elongatus PCC 6301 and Synechococcus elongatus PCC 7942 have previously been shown to constitutively express a FAD-containing L-amino acid oxidase with high ...
Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity

Stehr, Matthias; Smau, Liliana; Singh, Mahavir; Seth, Oliver; Macheroux, Peter; Ghisla, Sandro; Diekmann, Hans (Berlin : De Gruyter, 1999)

The proposed FAD binding site of L-lysine N6-hydroxylase (EC 1.14.13.99) exhibits an unusual proline in a position where a highly conserved glycine is found in other FAD dependent hydroxylases. We have studied the role of ...

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