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  • 1
    Electronic Resource
    Electronic Resource
    Sulfite-mediated destruction of .beta.-carotene (1979)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 27 (1979), S. 446-449 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60222a060
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  • 2
    Electronic Resource
    Electronic Resource
    Sulfoxide formation from methionine or its sulfide analogs during aerobic oxidation of sulfite (1970)
    s.l. : American Chemical Society
    Biochemistry 9 (1970), S. 5008-5014 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00827a027
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  • 3
    Electronic Resource
    Electronic Resource
    The methionine salvage pathway in relation to ethylene and polyamine biosynthesis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 69 (1987), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1987.tb04302.x
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  • 4
    Electronic Resource
    Electronic Resource
    Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls (1994)
    Springer
    Planta 194 (1994), S. 223-229 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylate oxidase ; Ethylene ; Gene expression ; Hypocotyl excision ; Vigna ; Wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By screening a mung bean (Vigna radiata L.) hypocotyl cDNA library using a combination of apple (pAE12) and tomato (pTOM13) 1-aminocyclopropane1-carboxylate (ACC)-oxidase cDNAs as probes, putative ACC-oxidase clones were isolated. Based on restriction-enzyme map and DNA-sequencing analyses, they can be divided into two homology classes, represented by pVR-ACO1 and pVR-ACO2. While pVR-ACO1 and pVR-ACO2 exhibit close homology in their coding regions, their 3′-noncoding regions are divergent. pVR-ACO1 is a 1312-bp full-length clone and contains a single open reading frame encoding 317 amino acids (MW = 35.8 kDa), while pVR-ACO2 is 1172 bp long and is a partial cDNA clone encoding 308 amino acids. These two deduced amino-acid sequences share 83% identity, and display considerable sequence conservation (73–86%) to other ACC oxidases from various plant species. Northern blot analyses of RNAs isolated from hypocotyl, leaf, and stem tissues using gene-specific probes indicate that the pVR-ACO1 transcript is present in all parts of the seedling and that the expression in hypocotyls is further increased following excision. The maximum induction of ACC-oxidase transcripts occurred at about 6 h after excision, while the maximum enzyme activity was observed at 24 h. When excised hypocotyls were treated with ethylene a further enhanced level of transcripts was observed. Aminooxyacetic acid, an inhibitor of ACC-synthase activity, and 2,5-norbornadiene, an inhibitor of ethylene action, suppressed the wound-induced accumulation of ACC-oxidase mRNA, while an addition of ethylene in these tissues restored the accumulation of ACC-oxidase mRNA. These results indicate that the wound-induced expression of ACC-oxidase transcripts is mediated through wound-induced ethylene. Furthermore, when intact mung-bean seedlings were treated with exogenous ethylene, a marked increase in the level of ACC-oxidase mRNA was observed. Together, these results indicate that ethylene plays a key role in activating the expression of the ACC-oxidase gene in both intact and excised mung-bean hypocotyls.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01101681
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and expression of its mRNA in ripening apple fruit (1991)
    Springer
    Planta 185 (1991), S. 38-45 
    Details
    ISSN: 1432-2048
    Keywords: 1-Amninocyclopropane-1-carboxylate synthase ; cDNA ; Ethylene synthesis ; Fruit ripening ; Gene expression ; Malus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1-Aminocyclopropane-1-carboxylate (ACC) synthase (EC 4.4.1.14) purified from apple (Malus sylvestris Mill.) fruit was subjected to trypsin digestion. Following separation by reversed-phase high-pressure liquid chromatography, ten tryptic peptides were sequenced. Based on the sequences of three tryptic peptides, three sets of mixed oligonucleotide probes were synthesized and used to screen a plasmid cDNA library prepared from poly(A)+ RNA of ripe apple fruit. A 1.5-kb (kilobase) cDNA clone which hybridized to all three probes were isolated. The clone contained an open reading frame of 1214 base pairs (bp) encoding a sequence of 404 amino acids. While the polyadenine tail at the 3′-end was intact, it lacked a portion of sequence at the 5′-end. Using the RNA-based polymerase chain reaction, an additional sequence of 148 bp was obtained at the 5′-end. Thus, 1362 bp were sequenced and they encode 454 amino acids. The deduced amino-acid sequence contained peptide sequences corresponding to all ten tryptic fragments, confirming the identity of the cDNA clone. Comparison of the deduced amino-acid sequence between ACC synthase from apple fruit and those from tomato (Lycopersicon esculentum Mill.) and winter squash (Cucurbita maxima Duch.) fruits demonstrated the presence of seven highly conserved regions, including the previously identified region for the active site. The size of the translation product of ACC-synthase mRNA was similar to that of the mature protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), indicating that apple ACC-synthase undergoes only minor, if any, post-translational proteolytic processing. Analysis of ACC-synthase mRNA by in-vitro translation-immunoprecipitation, and by Northern blotting indicates that the ACC-synthase mRNA was undetectable in unripe fruit, but was accumulated massively during the ripening proccess. These data demonstrate that the expression of the ACC-synthase gene is developmentally regulated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194512
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  • 6
    Electronic Resource
    Electronic Resource
    Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls (1994)
    Springer
    Planta 194 (1994), S. 223-229 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylate oxidase ; Ethylene ; Gene expression ; Hypocotyl excision ; Vigna ; Wounding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By screening a mung bean (Vigna radiata L.) hypocotyl cDNA library using a combination of apple (pAE12) and tomato (pTOM13) 1-aminocyclopropane1-carboxylate (ACC)-oxidase cDNAs as probes, putative ACC-oxidase clones were isolated. Based on restriction-enzyme map and DNA-sequencing analyses, they can be divided into two homology classes, represented by pVR-ACO1 and pVR-ACO2. While pVR-ACO1 and pVR-ACO2 exhibit close homology in their coding regions, their 3′-noncoding regions are divergent. pVR-ACO1 is a 1312-bp full-length clone and contains a single open reading frame encoding 317 amino acids (MW = 35.8 kDa), while pVR-ACO2 is 1172 bp long and is a partial cDNA clone encoding 308 amino acids. These two deduced amino-acid sequences share 83% identity, and display considerable sequence conservation (73–86%) to other ACC oxidases from various plant species. Northern blot analyses of RNAs isolated from hypocotyl, leaf, and stem tissues using gene-specific probes indicate that the pVR-ACO1 transcript is present in all parts of the seedling and that the expression in hypocotyls is further increased following excision. The maximum induction of ACC-oxidase transcripts occurred at about 6 h after excision, while the maximum enzyme activity was observed at 24 h. When excised hypocotyls were treated with ethylene a further enhanced level of transcripts was observed. Aminooxyacetic acid, an inhibitor of ACC-synthase activity, and 2,5-norbornadiene, an inhibitor of ethylene action, suppressed the wound-induced accumulation of ACC-oxidase mRNA, while an addition of ethylene in these tissues restored the accumulation of ACC-oxidase mRNA. These results indicate that the wound-induced expression of ACC-oxidase transcripts is mediated through wound-induced ethylene. Furthermore, when intact mung-bean seedlings were treated with exogenous ethylene, a marked increase in the level of ACC-oxidase mRNA was observed. Together, these results indicate that ethylene plays a key role in activating the expression of the ACC-oxidase gene in both intact and excised mung-bean hypocotyls.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196391
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  • 7
    Electronic Resource
    Electronic Resource
    The physiological role of lipoxygenase in ethylene formation from 1-aminocyclopropane-1-carboxylic acid in oat leaves (1987)
    Springer
    Planta 170 (1987), S. 190-196 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylic acid ; Avena (ethylene synthesis) ; Lipoxygenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to understand the physiological significance of the in-vitro lipoxygenase (EC 1.13.11.12)-mediated ethylene-forming system (J.F. Bousquet and K.V. Thimann 1984, Proc. Natl. Acad. Sci. USA 81, 1724–1727), its characteristics were compared to those of an in-vivo ethylene-forming system. While oat (Avena sativa L.) leaves, as other plant tissues, preferentially converted only one of the 1-amino-2-ethylcyclopropane-1-carboxylic acid (AEC) isomers to 1-butene, the lipoxygenase system converted all four AEC isomers to 1-butene with nearly equal efficiencies. While the in-vivo ethylene-forming system of oat leaves was saturable with ACC with a Km of 16 μM, the lipoxygenase system was not saturated with ACC even at 10 mM. In contrast to the in-vivo results, only 10% of the ACC consumed in the lipoxygenase system was converted to ethylene, indicating that the reaction is not specific for ethylene formation. Increased ACC-dependent ethylene production in oat leaves following pretreatment with linoleic acid has been inferred as evidence of the involvement of lipoxygenase in ethylene production. We found that pretreating oat leaves with linoleic acid resulted in increased ACC uptake and thereby increased ethylene production. A similar effect was observed with oleic acid, which is not a substrate of lipoxygenase. Since linoleic acid hydroperoxide can substitute for lipoxygenase and linoleic acid in this system, it is assumed that the alkoxy radicals generated during the decomposion of linoleic acid hydroperoxide are responsible for the degradation of ACC to ethylene. Our results collectively indicate that the reported lipoxygenase system is not the in-vivo ethylene-forming enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397887
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  • 8
    Electronic Resource
    Electronic Resource
    Metabolism of α-aminoisobutyric acid in mungbean hypocotyls in relation to metabolism of 1-aminocyclopropane-1-carboxylic acid (1984)
    Springer
    Planta 161 (1984), S. 439-443 
    Details
    ISSN: 1432-2048
    Keywords: d-Amino acid ; 1-Aminocyclopropane-1-carboxylic acid ; α-Aminoisobutyric acid ; Ethylene synthesis ; 1-(Malonylamino)cyclopropane-1-carboxylic acid ; α-(Malonylamino)isobutyric ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1-Aminocyclopropane-1-carboxylic acid (ACC) is known to be converted to ethylene and conjugated into N-malonyl-ACC in plant tissues. When α-amino[1-14C]isobutyric acid (AIB), a structural analog of ACC, was administered to mungbean (Vigna radiata L.) hypocotyl segments, it was metabolized to 14CO2 and conjugated to N-malonyl-AIB (MAIB). α-Aminoisobutyric acid inhibited the conversion of ACC to ethylene and also inhibited, to a lesser extent, N-malonylation of ACC and d-amino acids. Although the malonylation of AIB was strongly inhibited by ACC as well as by d-amino acids, the metabolism of AIB to CO2 was inhibited only by ACC but not by d-amino acids. Inhibitors of ACC conversion to ethylene such as anaerobiosis, 2,4-dinitrophenol and Co2+, similarly inhibited the conversion of AIB to CO2. These results indicate that the malonyalation of AIB to MAIB is intimately related to the malonylation of ACC and d-amino acids, whereas oxidative decarboxylation of AIB is related to the oxidative degradation of ACC to ethylene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394575
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  • 9
    Electronic Resource
    Electronic Resource
    Relationship between the malonylation of 1-aminocyclopropane-1-carboxylic acid and D-amino acids in mung-bean hypocotyls (1983)
    Springer
    Planta 158 (1983), S. 437-441 
    Details
    ISSN: 1432-2048
    Keywords: D-amino acid ; 1-Aminocyclopropane-1-carboxylic acid ; Ethylene and amino acids ; 1-(Malonylamino)cyclopropane-1-carboxylic acid ; N-Malonyl-D-methionine ; Methionine ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In sections from hypocotyls of dark-grown mung-bean (Vigna radiata L.) seedlings, D-phenylalanine and D-methionine (D-met) inhibited the formation of 1-(malonylamino)cyclopropane-1-carboxylic acid from exogenously administered 1-aminocyclopropane-1-carboxylic acid (ACC), resulting in an increase in free ACC content and stimulation of ethylene production, whereas their L-enantiomers had little or no such effect. When the hypocotyls were administered D-Met, it was mainly metabolized to N-malonylmethionine and N-malonylmethionine sulfoxide, and this malonylation process was inhibited to a greater extent by ACC and D-amino acids (phenylalanine and serine) than by L-amino acids. These results indicate that malonylation of D-amino acids and of ACC are intimately interrelated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397737
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  • 10
    Electronic Resource
    Electronic Resource
    Changes in 1-(malonylamino)cyclopropane-1-carboxylic acid content in wilted wheat leaves in relation to their ethylene production rates and 1-aminocyclopropane-1-carboxylic acid content (1983)
    Springer
    Planta 157 (1983), S. 518-523 
    Details
    ISSN: 1432-2048
    Keywords: 1-Aminocyclopropane-1-carboxylic acid ; Cytokinin and ethylene production ; Ethylene in wilted leaves ; Leaf, wilted, ethylene production ; 1-(Malonylamino)cyclopropane-1-carboxylic acid ; Triticum (ethylene production) ; Water stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In excised wheat (Triticum aestivum L.) leaves, water-deficit stress resulted in a rapid increase, followed by a decrease, in ethylene production rates and in the levels of 1-aminocyclopropane-1-carboxylic acid (ACC), the immediate precursor of ethylene. However, the level of N-malonyl-ACC (MACC), the major metabolite of ACC, increased gradually, then leveled off. This increase in MACC was much greater than the decrease in ACC level. The MACC levels were positively correlated with severity of water stress. Once established, the MACC levels did not decrease even after the stressed tissues were rehydrated. Administration of labeled ACC and MACC showed that the conjugation of ACC to MACC was essentially irreversible. Repeated wilting treatments following the first wilting and rehydration cycle resulted in no further increase in ethylene production and in the levels of ACC and MACC. However, when benzyladenine was supplied during the preceding rehydration process, subsequent wilting treatment resulted in a rise in MACC level and a rapid rise followed by a decline in ethylene production rates and in the level of ACC. The magnitude of these increases was, however, smaller in these rewilted tissues than that observed in the first wilting treatment. Since MACC accumulates with water stress and is not appreciably metabolized, the MACC level is a good indicator of the stress history in the detached leaves used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00396882
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