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      L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria.

      Zeitschrift für Naturforschung. C, Journal of biosciences
      Amino Acid Sequence, Amino Acids, Basic, metabolism, Anabaena variabilis, Arginine, Binding Sites, Conserved Sequence, Cyanobacteria, classification, genetics, Flavin-Adenine Dinucleotide, Genome, Bacterial, Histidine, Kinetics, L-Amino Acid Oxidase, Lysine, Molecular Sequence Data, Nostoc, Ornithine, Sequence Homology, Amino Acid, Substrate Specificity, Synechococcus

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          Abstract

          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 specificity for basic L-amino acids (L-arginine being the best substrate). In this paper we show that such an enzyme is also present in the fresh water cyanobacterium Synechococcus cedrorum PCC 6908. In addition, an improved evaluation of the nucleotide/amino acid sequence of the L-amino acid oxidase of Synechococcus elongatus PCC 6301 (encoded by the aoxA gene) with respect to the FAD-binding site and a translocation pathway signal sequence will be given. Moreover, the genome sequences of 24 cyanobacteria will be evaluated for the occurrence of an aoxA-similar gene. In the evaluated cyanobacteria 15 genes encoding an L-amino acid oxidase-similar protein will be found.

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