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Browsing by Subject "Sequence Homology, Amino Acid"

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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 ...
New insights into the co-evolution of cytochrome c reductase and the mitochondrial processing peptidase

Brumme, Stefanie; Kruft, Volker; Schmitz, Udo K.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 1998)

The mitochondrial processing peptidase (MPP) is a heterodimeric enzyme that forms part of the cytochrome c reductase complex from higher plants. Mitochondria from mammals and yeast contain two homologous enzymes: (i) an ...
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 ...
Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants

Jänsch, Lothar; Kruft, Volker; Schmitz, Udo K.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 1998)

Transport of most nuclear encoded mitochondrial proteins into mitochondria is mediated by heteropolymeric translocases in the membranes of the organelles. The translocase of the outer mitochondrial membrane (TOM) was ...

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Browsing by Subject "Sequence Homology, Amino Acid"

Browsing by Subject "Sequence Homology, Amino Acid"

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