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'L Amino Acid Oxidase' in keywords
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1Author    ElfriedeK. PistoriusRequires cookie*
 Title    Further Evidence for a Functional Relationship between L-Amino Acid Oxidase Activity and Photosynthetic Oxygen Evolution in Anacystis nidulans. Effect of Chloride on the Two Reactions  
 Abstract    The L-amino acid oxidase from Anacystis nidulans is inhibited by cations as well as anions. The inhibition by cations has been previously described (E. K. Pistorius, Eur. J. Biochem. 135, 217—222 [1983]). We have shown that the order of effectiveness was > M2+ > M +, when e.g. La3+, Ca2+ and K+ were compared. However, in the concentration range where the monovalent cations inhibited, the inhibition was not entirely due to the cation, but an influence of the anion could also be observed. When monovalent anions were compared as the corresponding sodium salts, the order of effectiveness was SCN~ > N 0 3_ > CL, Br > I~ > F ' > H CO O " > CH,COO . The inhibition of the L-amino acid oxidase activity by the various salts was strongly influenced by the pH of the reaction mixture. It could be shown that the inhibition by cations increased in the alkaline pH region, while the inhibition by anions increased in the acidic pH region. Our previous results have also shown that a functional relationship might exist between L-amino acid oxidase activity and photosynthetic 0 2 evolution (E. K. Pistorius and H. Voss, Eur. J. Biochem. 126, 203—209 [1982]). Since the water-splitting complex of photosystem II is affected by a number of anions, although only Cl-and Br" lead to activation of 0 2 evolution, we investigated whether a correlation could be obtained between the anion effect on the L-amino acid oxidase and on photosynthetic 0 2 evolution. The results show that those anions which have a higher affinity for the enzyme than CL or Br", are especially effective in causing inactivation of the 0 2 evolu­ tion. Moreover, we show that L-arginine which is a substrate of the L-amino acid oxidase, and Cl-have antagonistic effects on the L-amino acid oxidase reaction and on photosynthetic 0 2 evolu­ tion. We suggest that this flavoprotein with L-amino acid oxidase activity is modified by Ca:+ and CL in such a way that it can now interact with Mn2* and catalyze the water-splitting reaction of photosystem II. 
  Reference    Z. Naturforsch. 40c, 806—813 (1985); received June 7 1985 
  Published    1985 
  Keywords    Anacystis nidulans, 0 2 Evolution, L-Amino Acid Oxidase, Chloride 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0806.pdf 
 Identifier    ZNC-1985-40c-0806 
 Volume    40 
2Author    Gudrun Wälzlein, AchimE. Gau, ElfriedeK. PistoriusRequires cookie*
 Title    Further Investigations about the Flavin in the L-Amino Acid Oxidase and a Possible Flavin in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    The absorption spectrum of the previously purified L-amino acid oxidase from the cyanobac-terium Anacystis nidulans has shown considerable variation with each preparation and the spec-trum in several preparations was quite different from the absorption spectrum of other simple flavoproteins (E. K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986). Here we show that the spectral complexity and variability of the L-amino acid oxidase can be largely explained by the presence of a modified flavin derivative of yet unknown structure besides oxidized FAD and FAD semiquinone. After removal from the enzyme this modified chromophore has absorption maxima at 260, 396 and in the 600 nm region. This derivative of FAD seems to be formed in variable amounts during the purification of the enzyme. On the other hand, extraction of Anacystis photosystem II complexes which contain the flavoprotein, almost exclusively yields modified flavin derivatives and practically no authentic oxidized FAD. The spectrum of the chromophores which have been extracted from photosystem II complexes at different purification stages, is either similar (although not identical) to the spectrum of the chromophore extracted from the isolated L-amino acid oxidase or similar to the spectrum of reduced flavin. All extracted chromophores show a fluorescence emission in the 420 to 560 nm region when excited with light of 390 nm. These results indicate that the flavin present in the L-amino acid oxidase protein as well as in photosystem II complexes from A. nidulans rapidly undergoes modification reactions of yet unknown nature to yield several closely related FAD derivatives. This might possibly be the reason why so far no flavin has been detected in photosys-tem II. The presence of such modified flavin derivatives in photosystem II complexes of A. nidulans as shown here is an additional support of our hypothesis that an unusual flavin is functional on the donor side of photosystem II. 
  Reference    Z. Naturforsch. 43c, 545—553 (1988); received January 25 1988 
  Published    1988 
  Keywords    L-Amino Acid Oxidase, Flavoprotein, Photosystem II, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0545.pdf 
 Identifier    ZNC-1988-43c-0545 
 Volume    43 
3Author    AchimE. Gau, Gudrun Wälzlein, Susanne Gärtner, Matthias Kuhlmann, Susanne Specht, ElfriedeK. PistoriusRequires cookie*
 Title    Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    Photosystem II complexes from the cyanobacterium Anacystis nidulans have been investigated by Western blots with antisera raised against four photosystem II peptides from plants and with an antiserum raised against the soluble L-amino acid oxidase protein from/1. nidulans to achieve an iden­ tification of the polypeptides — especially of the L-amino acid oxidase related protein — in isolated photosystem II complexes. Anacystis photosystem II complexes which were solubilized with lauryldimethylamine N-oxide and purified by sucrose cushion and sucrose gradient centrifugation, contained as major Coomassie brilliant blue stained polypeptides a 71 kDa band of unknown identity, a 62 kDa band, which partly contained D-l, a 55 and 49 kDa band which were immuno-reactive with an antiserum to the 47 kDa peptide of tobacco PS II complexes, and three distinct bands in the 30 kDa region. These latter bands could be identified as the extrinsic Mn stabilizing peptide (27—30 kDa), D-l (30—33 kDa) and a 36 kDa peptide (35 — 38 kDa) which crossreacted with the antiserum raised against the soluble L-amino acid oxidase protein of 50 kDa. These results suggest that the 36 kDa peptide present in purified photosystem II complexes from A. nidulans might be a processed form of the soluble 50 kDa L-amino acid oxidase protein. 
  Reference    Z. Naturforsch. 44c, 971—975 (1989); received June 22 1989 
  Published    1989 
  Keywords    Photosystem II, L-Amino Acid Oxidase, Antibody, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0971.pdf 
 Identifier    ZNC-1989-44c-0971 
 Volume    44 
4Author    W. LöffelhardtRequires cookie*
 Title    The Biosynthesis of Phenylacetic Acids in the Blue-Green Alga Anacystis nidulans: Evidence for the Involvement of a Thylakoid-Bound L-Amino Acid Oxidase  
 Abstract    Phenylacetic acid and p-hydroxyphenylacetic acid are formed upon incubation of photosynthetic membranes from the prokaryotic alga Anacystis nidulans with L-phenylalanine and L-tyrosine, respectively. The corresponding phenylpyruvic acids act as intermediates as shown by trapping them as the stable oximino acids. The first step in this reaction sequence appears to be catalyzed by a thylakoid-bound L-amino acid oxidase. Already existing evidence concerning phenylacetic acid formation at thylakoid membranes of higher plants via an L-amino acid oxidase and the results obtained with A. nidulans give another example of aromatic amino acids between chloroplasts and 
  Reference    (Z. Naturforsch. 32c, 345—350 [1977]; received February 14 1977) 
  Published    1977 
  Keywords    Membrane-Bound Enzymes, Anacystis nidulans, Thylakoids, Phenylacetic Acids, L-Amino Acid Oxidase 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0345.pdf 
 Identifier    ZNC-1977-32c-0345 
 Volume    32 
5Author    DirkH. Engels, Anke Engels, ElfriedeK. PistoriusRequires cookie*
 Title    Isolation and Partial Characterization of an l -Amino Acid Oxidase and of Photosystem II Complexes from the Cyanobacterium Synechococcus PCC 7942  
 Abstract    An L-amino acid oxidase with high specifity for basic L-amino acids was isolated from the cyanobacterium Synechococcus PCC 7942, and the enzyme was partially characterized. This enzyme was compared to the previously described L-amino acid oxidase from Synechococcus 
  Reference    Z. Naturforsch. 47c, 859 (1992); received October 4 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 7942, Photosystem II, L-Amino Acid Oxidase, Water Oxi­ dizing Enzyme 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0859.pdf 
 Identifier    ZNC-1992-47c-0859 
 Volume    47 
6Author    Klaus-Peter Michel, ElfriedeK. Pistorius, E. Gau, G. Wälzlein, S. Gärtner, M. Kuhlmann, E. K. PistoriusRequires cookie*
 Title    Isolation of a Photosystem II Associated 36 kDa Polypeptide and an Iron-Stress 34 kDa Polypeptide from Thylakoid Membranes of the Cyanobacterium Synechococcus PCC 6301 Grown under Mild Iron Deficiency  
 Abstract    A 36 kDa polypeptide which previously was shown to be present in purified photosystem II complexes from Synechococcus PCC 6301 and which crossreacts with the antiserum raised against the soluble L-amino acid oxidase o f 50 kD a from Synechococcus PCC 6301 (A. was isolated from thylakoid membranes o f the same cyanobacterium grown under mild iron deficiency. This peptide is present in about equal am ounts in thylakoid membranes o f Syne­ chococcus PCC 6301 grown under regular or iron deficient conditions. The antiserum raised against this thylakoid membrane bound 36 kD a peptide crossreacts with the soluble L-amino acid oxidase o f 50 kDa. These results further support our conclusion that the thylakoid mem­ brane bound 36 kD a polypeptide is a modified form o f the soluble 50 kD a L-amino acid oxi­ dase. In addition, a 34 kD a polypeptide was isolated from iron stressed thylakoid membranes, and an antiserum was also raised against this protein. Im m unoblot experiments with this an­ tiserum show that the 34 kD a peptide is present in elevated amounts in thylakoid membranes from Synechococcus cells grown under iron deficiency and that it is alm ost absent in thylakoid membranes from cells grown under regular conditions. 
  Reference    Z. Naturforsch. 47c, 867—8 (1992); received August 4/O ctober 8 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 6301, Photosystem II, L-Amino Acid Oxidase, Iron Stress 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0867.pdf 
 Identifier    ZNC-1992-47c-0867 
 Volume    47