Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803

Schriek S, Kahmann U, Staiger D, Pistorius EK, Michel K-P (2009)
Journal of Experimental Botany 60(3): 1035-1046.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The protein Slr0782 from Synechocystis sp. PCC 6803, which has similarity to L-amino acid oxidase from Synechococcus elongatus PCC 6301 and PCC 7942, has been characterized in part. Immunoblot blot analysis showed that Slr0782 is mainly thylakoid membrane-associated. Moreover, expression of slr0782 mRNA and Slr0782 protein were analyzed and an activity assay was developed. Utilizing toluene-permeabilized cells, an L-arginine-stimulated O2 uptake became detectable in Synechocystis sp. PCC 6803. Besides oxidizing the basic L-amino acids L-arginine, L-lysine, L-ornithine, and L-histidine, a number of other L-amino acids were also substrates, while D-amino acids were not. The best substrate was L-cysteine, and the second best was L-arginine. The L-arginine-stimulated O2 uptake was inhibited by cations. The inhibition by o-phenanthroline and salicylhydroxamic acid suggested the presence of a transition metal besides FAD in the enzyme. Moreover, it is shown that inhibitors of the respiratory electron transport chain, such as KCN and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, also inhibited the L-arginine-stimulated O2 uptake, suggesting that Slr0782 functions as an L-arginine dehydrogenase, mediating electron transfer from L-arginine into the respiratory electron transport chain utilizing O2 as electron acceptor via cytochrome oxidase. The results imply that Slr0782 is an additional substrate dehydrogenase being able to interact with the electron transport chain of the thylakoid membrane.
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Zeitschriftentitel
Journal of Experimental Botany
Band
60
Zeitschriftennummer
3
Seite
1035-1046
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Schriek S, Kahmann U, Staiger D, Pistorius EK, Michel K-P. Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. Journal of Experimental Botany. 2009;60(3):1035-1046.
Schriek, S., Kahmann, U., Staiger, D., Pistorius, E. K., & Michel, K. - P. (2009). Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. Journal of Experimental Botany, 60(3), 1035-1046. doi:10.1093/jxb/ern352
Schriek, S., Kahmann, U., Staiger, D., Pistorius, E. K., and Michel, K. - P. (2009). Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. Journal of Experimental Botany 60, 1035-1046.
Schriek, S., et al., 2009. Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. Journal of Experimental Botany, 60(3), p 1035-1046.
S. Schriek, et al., “Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803”, Journal of Experimental Botany, vol. 60, 2009, pp. 1035-1046.
Schriek, S., Kahmann, U., Staiger, D., Pistorius, E.K., Michel, K.-P.: Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. Journal of Experimental Botany. 60, 1035-1046 (2009).
Schriek, Sarah, Kahmann, Uwe, Staiger, Dorothee, Pistorius, Elfriede K., and Michel, Klaus-Peter. “Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803”. Journal of Experimental Botany 60.3 (2009): 1035-1046.
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2 Zitationen in Europe PMC

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New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942.
Pietsch D, Bernát G, Kahmann U, Staiger D, Pistorius EK, Michel KP., Photosynth Res 108(2-3), 2011
PMID: 21607697

84 References

Daten bereitgestellt von Europe PubMed Central.

Extensive accumulation of an extracellular L-amino-acid oxidase during gametogenesis of Chlamydomonas reinhardtii.
Vallon O, Bulte L, Kuras R, Olive J, Wollman FA., Eur. J. Biochem. 215(2), 1993
PMID: 8344302
Photosynthesis and respiration in cyanobacteria
Vermaas WFJ., 2001
Arginine catabolism in Aphanocapsa 6308.
Weathers PJ, Chee HL, Allen MM., Arch. Microbiol. 118(1), 1978
PMID: 100070
L-cysteine oxidase activity in the membrane of Neisseria meningitidis.
Yu EK, DeVoe IW., J. Bacteriol. 145(1), 1981
PMID: 6780513
Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel -amino-acid oxidase with cell apoptosis-inducing activity from pallas venom
Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P., 2004

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