Analysis of the active sites of copper/topa quinone-containing amine oxidases fromLathyrus odoratus andL. sativus seedlings

Šebela, Marek; Luhová, Lenka; Frébort, Ivo; Faulhammer, Heinz G.; Hirota, Shun; Zajoncová, Ludmila; Stužka, V.; Peč, Pavel

doi:10.1002/(sici)1099-1565(199809/10)9:5<211::aid-pca407>3.0.co;2-x

Cited by 29 publications

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“…The following Michaelis-Menten constant (K m ) values for DADO of GPAO, LSAO and ELAO were determined: 0.15, 0.36 and 1.05 mM, respectively. Such values correspond well with those for the best natural diamine substrates of plant CAOs -putrescine, cadaverine and spermidine 10 .…”

Section: Resultssupporting

confidence: 79%

Interaction of plant amine oxidases with diaminoethers

Šebela¹,

Jarkovská²,

Lenobel³

et al. 2006

Arkivoc

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Polyamines are ubiquitous compounds, which are involved in crucial physiological events including cell growth and differentiation. The catabolic oxidative degradation of polyamines is catalyzed by quinoprotein copper-containing amine oxidases (CAOs) and flavoprotein polyamine oxidases (PAOs). Various synthetic polyamine analogs and polyamine derivatives have been reported, which represent important tools (substrates or inhibitors) in the study of catalytic properties of the enzymes. In this work, two related compounds were studied in the reactions with plant amine oxidases: 1,8-diamino-3,6-dioxaoctane (DADO) and 1,10-bis(2-pyridinylmethyl)-4,7-dioxa-1,10-diazadecane (BPDD). Based on activity and stoichiometry assays together with spectrophotometric measurements, DADO can be considered a good substrate for grass pea, lentil and E. characias CAOs with K m values in the range 10 -4 -10 -3 M.Its oxidative degradation produces the corresponding aminoaldehyde 8-amino-3,6-dioxaoctanal, which does not undergo spontaneous cyclization (as it is known for the oxidation products of natural substrates putrescine, cadaverine and spermidine) or polymerization in the reaction mixture. Conversely, oat PAO does not oxidize DADO and is only weakly inhibited by the compound (K i = 1.6 mM towards putrescine). BPDD was found to be a competitive inhibitor of both CAOs and PAOs with K i values of 10 -4 M. DADO could be suggested as a potential affinity ligand for CAOs.

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Section: Resultssupporting

confidence: 79%

Interaction of plant amine oxidases with diaminoethers

Šebela¹,

Jarkovská²,

Lenobel³

et al. 2006

Arkivoc

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“…A high degree of identity was reported for the bovine serum amine oxidase (BSAO) and VAP-1 pair (83%) [12] and the pea and lentil seedling amine oxidases (PSAO and LSAO, respectively) pair (91%) [16]. Other plant amine oxidases probably share this property since the N-terminal 30 amino acid sequences of Lathyrus odoratus and Lathyrus sativus amine oxidase show 100% identity with PSAO [17].…”

Section: Introductionmentioning

confidence: 97%

Substrate specificity of copper-containing plant amine oxidases

Pietrangeli

Federico

Mondovı̀

et al. 2007

Journal of Inorganic Biochemistry

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“…A commercial biosensor analyser (M. Jilek Company, Postřelmov, Czech Republic) connected to a PC was used as a potentiostat (Zajoncová et al 2004). Pea amine oxidase and maize polyamine oxidase were purified as described previously (Šebela et al 1998;Federico et al 1989) and the enzymes were immobilised on a cellophane membrane. Six µl of a solution containing 36 µg of amine oxidase (total activity 11 nkat) and 15 µg of polyamine oxidase (total activity 13.2 nkat), 0.1 mg BSA, 0.03 mg gelatin and 0.8 µl of 2% (v/v) glutaraldehyde in a working buffer (10mM K-phosphate, pH 7.0) were pipetted on the cellophane and left to dry in a refrigerator overnight.…”

Section: Methodsmentioning

confidence: 99%

Modulation of polyamine catabolism in pea seedlings by calcium during salinity stress

Piterková¹,

Luhová²,

Zajoncová³

et al. 2012

Plant Prot. Sci.

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Piterková J., Luhová L., Zajoncová L., Šebela M., Petřivalský M. (2012): Modulation of polyamine catabolism in pea seedlings by calcium during salinity stress. Plant Protect. Sci., 48: 53-64.The relation of polyamine catabolism in the response of Pisum sativum to salinity stress was investigated. Pea seedlings were grown in increasing concentrations of Na + or K + or at different concentration ratios of these ions.We studied the effect of Ca 2+ supplementation on plants exposed to salinity stress. The parameters measured in the roots and shoots of pea seedlings included biomass production, levels of Na + , K + , Ca 2+ and polyamines and activity of enzymes of polyamine catabolism: diamine oxidase, aminoaldehyde dehydrogenase and peroxidases. Salinity induced increased polyamine levels and higher activity of enzymes participating in polyamine degradation. Supplementation of Ca 2+ had a positive effect on biomass production and in most cases it stabilised both the polyamine level and the activity of the studied enzymes. Our results confirm the role of aminoaldehyde dehydrogenase and polyamine catabolism in defence mechanisms of pea plants under salinity stress.

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Analysis of the active sites of copper/topa quinone-containing amine oxidases fromLathyrus odoratus andL. sativus seedlings

Cited by 29 publications

References 0 publications

Interaction of plant amine oxidases with diaminoethers

Interaction of plant amine oxidases with diaminoethers

Substrate specificity of copper-containing plant amine oxidases

Modulation of polyamine catabolism in pea seedlings by calcium during salinity stress

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