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

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dc.identifier.uri http://dx.doi.org/10.15488/2440
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/2466
dc.contributor.author Gau, Achim E.
dc.contributor.author Heindl, Achim
dc.contributor.author Nodop, Anke
dc.contributor.author Kahmann, Uwe
dc.contributor.author Pistorius, Elfriede K.
dc.date.accessioned 2017-11-24T10:31:43Z
dc.date.available 2017-11-24T10:31:43Z
dc.date.issued 2007
dc.identifier.citation Gau, A.E.; Heindl, A.; Nodop, A.; Kahmann, U.; Pistorius, E.K.: L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria. In: Zeitschrift für Naturforschung - Section C Journal of Biosciences 62 (2007), Nr. 3-4, S. 273-284. DOI: https://doi.org/10.1515/znc-2007-3-419
dc.description.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. eng
dc.language.iso eng
dc.publisher Berlin : De Gruyter
dc.relation.ispartofseries Zeitschrift für Naturforschung - Section C Journal of Biosciences 62 (2007), Nr. 3-4
dc.rights CC BY-NC-ND 3.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subject Cyanobacteria eng
dc.subject L-amino acid oxidase eng
dc.subject Synechococcus elongatus PCC 6301 and PCC 7942 eng
dc.subject Cyanobacteria eng
dc.subject Cyanobacterium stanieri eng
dc.subject Synechococcus eng
dc.subject Synechococcus elongatus eng
dc.subject Synechococcus elongatus PCC 6301 eng
dc.subject Synechococcus elongatus PCC 7942 eng
dc.subject amino acid eng
dc.subject amino acid oxidase eng
dc.subject arginine eng
dc.subject flavine adenine nucleotide eng
dc.subject histidine eng
dc.subject lysine eng
dc.subject ornithine eng
dc.subject amino acid sequence eng
dc.subject Anabaena variabilis eng
dc.subject article eng
dc.subject bacterial genome eng
dc.subject binding site eng
dc.subject classification eng
dc.subject Cyanobacterium eng
dc.subject enzyme specificity eng
dc.subject genetics eng
dc.subject kinetics eng
dc.subject metabolism eng
dc.subject molecular genetics eng
dc.subject Nostoc eng
dc.subject nucleotide sequence eng
dc.subject sequence homology eng
dc.subject Synechococcus eng
dc.subject Amino Acid Sequence eng
dc.subject Amino Acids, Basic eng
dc.subject Anabaena variabilis eng
dc.subject Arginine eng
dc.subject Binding Sites eng
dc.subject Conserved Sequence eng
dc.subject Cyanobacteria eng
dc.subject Flavin-Adenine Dinucleotide eng
dc.subject Genome, Bacterial eng
dc.subject Histidine eng
dc.subject Kinetics eng
dc.subject L-Amino Acid Oxidase eng
dc.subject Lysine eng
dc.subject Molecular Sequence Data eng
dc.subject Nostoc eng
dc.subject Ornithine eng
dc.subject Sequence Homology, Amino Acid eng
dc.subject Substrate Specificity eng
dc.subject Synechococcus eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title L-amino acid oxidases with specificity for basic L-amino acids in cyanobacteria
dc.type Article
dc.type Text
dc.relation.essn 1865-7125
dc.relation.issn 0939-5075
dc.relation.doi https://doi.org/10.1515/znc-2007-3-419
dc.bibliographicCitation.issue 3-4
dc.bibliographicCitation.volume 62
dc.bibliographicCitation.firstPage 273
dc.bibliographicCitation.lastPage 284
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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