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Literature summary for 1.4.3.25 extracted from

  • Bockholt, R.; Scholten-Beck, G.; Pistorius, E.K.
    Construction and partial characterization of an L-amino acid oxidase-free Synechococcus PCC 7942 mutant and localization of the L-amino acid oxidase in the corresponding wild type (1996), Biochim. Biophys. Acta, 1307, 111-121.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular small part of the protein Synechococcus sp. 5622
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periplasm predominant localization Synechococcus sp.
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 x * 50000, SDS-PAGE Synechococcus sp.

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
-
-
Synechococcus sp. PCC 7942
-
-
-

Subunits

Subunits Comment Organism
? x * 50000, SDS-PAGE Synechococcus sp.

Synonyms

Synonyms Comment Organism
aoxA
-
 Synechococcus sp.

General Information

General Information Comment Organism
physiological function mutant cells lacking L-amino acid oxidase protein cannot grow on L-arginine as sole N-source. Mutant cells can grow on nitrate or ammonium as N-source under photoautotropic conditions with a growth rate of about 75% of the wild-type rate. Under these conditions the photosynthetic O2 evolving activity is reduced by about the same amount, and the pigment content, especially the phycobiliprotein content, is much lower than in wild-type Synechococcus sp.