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  • 1
    Electronic Resource
    Electronic Resource
    Photosynthesis, photorespiration and nitrogen metabolism (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 6 (1983), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. The ATP and reduced ferredoxin generated in photosynthetic reactions in the chloroplast are utilized for a large number of reactions other than CO2-fixation. Quantitatively the most important reaction is the reassimilation of ammonia liberated during photorespiration in C3 plants via the glutamate synthase cycle. Chloroplasts are also able to reduce nitrite to ammonia, sulphate to sulphide, and synthesize a number of amino acids. The amino acids essential for human nutrition are all synthesized in the chloroplast and evidence is presented to suggest that they may be the sole site of such biosynthetic reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/1365-3040.ep11612102
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  • 2
    Electronic Resource
    Electronic Resource
    Aspartate kinase and the synthesis of aspartate-derived amino acids in wheat (1978)
    Springer
    Planta 139 (1978), S. 119-125 
    Details
    ISSN: 1432-2048
    Keywords: Aspartate kinase ; Feedback regulation ; Lysine ; Methionine ; Threonine ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate kinase (EC 2.7.2.4.) has been purified from 7 day etiolated wheat (Triticum aestivum L. var. Maris Freeman) seedlings and from embryos imbibed for 8 h. The enzyme was 50% inhibited by 0.25 mM lysine. In this study wheat aspartate kinase was not inhibited by threonine alone or cooperatively with lysine; these results contrast with those published previously. In vivo regulation of the synthesis of aspartate-derived amino acids was examined by feeding [14C]acetate and [35S]sulphate to 2–3 day germinating wheat embryos in culture in the presence of exogenous amino acids. Lysine (1 mM) inhibited lysine synthesis by 86%. Threonine (1 mM) inhibited threonine synthesis by 79%. Lysine (1 mM) plus threonine (1 mM) inhibited threonine synthesis by 97%. Methionine synthesis was relatively unaffected by these amino acids, suggesting that there are important regulatory sites other than aspartate kinase and homoserine dehydrogenase. [35S]sulphate incorporation into methionine was inhibited 50% by lysine (2 mM) plus threonine (2 mM) correlating with the reported 50% inhibition of growth by these amino acids in this system. The synergistic inhibition of growth, methionine synthesis and threonine synthesis by lysine plus threonine is discussed in terms of lysine inhibition of aspartate kinase and threonine inhibition of homoserine dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387136
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  • 3
    Electronic Resource
    Electronic Resource
    The effect of aspartate-derived amino acids (lysine, threonine, methionine) on the growth of excised embryos of wheat and barley (1978)
    Springer
    Planta 139 (1978), S. 113-117 
    Details
    ISSN: 1432-2048
    Keywords: Hordeum ; Lysine ; Metabolic control ; Methionine ; Threonine ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Excised wheat (Triticum aestivum L. var. Maris Freeman) and barley (Hordeum vulgare L. var. Maris Mink) embryos were grown on medium containing both nitrate and ammonium ions. Addition of lysine (1 mM) plus threonine (1 mM) caused a synergistic inhibition of growth measured by length of first leaf or dry weight. The inhibition was specifically relieved by methionine, homocysteine and homoserine. Threonine at 0.2–0.3 mM caused half-maximal inhibition of growth at all lysine concentrations whereas lysine increased the synergistic inhibition up to 3 mM. The inhibition is explained by a model in which lysine acts as a feedback inhibitor of aspartate kinase and threonine of homoserine dehydrogenase. This is compatible with published studies of the enzymes involved. The implications of these findings for using lysine plus threonine as a selection system for lysine-overproducing cereals are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387135
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  • 4
    Electronic Resource
    Electronic Resource
    The development of NAD(P)H-dependent and ferredoxin-dependent glutamate synthase in greening barley and pea leaves (1982)
    Springer
    Planta 154 (1982), S. 473-476 
    Details
    ISSN: 1432-2048
    Keywords: Ferredoxin ; Glutamate synthase ; Greening (leaves) ; Hordeum ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activity of NAD(P)H-dependent glutamate synthase (E.C. 1.4.1.14) has been demonstrated in extracts from etiolated shoots of pea (Pisum sativum L.) and barley (Hordeum vulgare L.). This activity does not significantly alter upon greening of the etiolated shoots, and is at a similar level in light-grown material. Ferredoxin-dependent glutamate synthase (E.C. 1.4.7.1) has low activity in etiolated shoots but increases rapidly on greening. In light grown leaves ferredoxin-dependent activity is 30–40-fold higher than NAD(P)H-dependent activity. It is not considered that the NAD(P)H-dependent glutamate synthase plays an important role in ammonia assimilation in the photosynthetic tissue of higher plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01267816
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  • 5
    Electronic Resource
    Electronic Resource
    Lysine metabolism in a barley mutant resistant to S(2-aminoethyl)cysteine (1979)
    Springer
    Planta 146 (1979), S. 629-633 
    Details
    ISSN: 1432-2048
    Keywords: Biochemical mutant ; Feedback regulation ; Hordeum ; Lysine ; Mutant ; S(2-aminoethyl)cysteine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lysine and S(2-aminoethyl)cysteine (AEC) metabolism were investigated in normal barley (Hordeum vulgare L. cv. Bomi) and a hemozygous recessive AEC-resistant mutant (R906). Feedback regulation of lysine and threonine synthesis from [14C] acetate was unimpaired in plants of the mutant 3 d after germination. Seeds of Bomi and R906 contained similar total amounts of lysine, threonine, methionine and isoleucine. Concentrations of these amino acids in the soluble fraction of plants grown 6 d without AEC were also similar. The concentration of AEC in R906 plants was less than in the parent variety when both were grown in the presence of 0.25 mM AEC for 6 d. The uptake of [3H]AEC and [3H]lysine by roots of R906 was, respectively, 33% and 32% of that by Bomi roots whereas the uptake of these compounds into the scutellum was the same in both the mutant and its parent. The uptake of [3H]leucine and its incorporation into proteins was also the same in Bomi and R906 plants. These results suggest that a transport system specific for lysine and AEC but not leucine is altered or lost in roots of the mutant R906. AEC is incorporated into protein and this could be the reason for inhibition of growth rather than action as a false-feedback inhibitor of lysine biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388843
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  • 6
    Electronic Resource
    Electronic Resource
    In vitro synthesis of barley storage proteins (1980)
    Springer
    Planta 149 (1980), S. 262-268 
    Details
    ISSN: 1432-2048
    Keywords: Hordeum ; Polyribosomes ; Protein synthesis ; RNA ; Seeds ; Storage proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Membrane-bound polysomes were isolated from developing endosperms of barley (Hordeum vulgare L.) and shown to support the synthesis of trichloroacetic acid-insoluble material by an in vitro wheat germ protein synthesis system. The mRNA associated with the polysomes was separated from the ribosomes by affinity chromatography on oligo-dT cellulose and was also shown to support in vitro protein synthesis. The poly-A+ RNA isolated contained material of between 0.55 and 2.55 kilobases in length with about 6% poly A. The products of in vitro protein synthesis resembled hordeins (the prolamin storage proteins of the barley endosperm) in that they were predominantly soluble in 55% propan-2-ol, contained a low proportion of lysine as compared with leucine and had similar, but not identical, electrophoretic properties. The differences in the electrophoretic behaviour between the products of poly-A+ RNA translation and authentic hordeins is suggested to be due to the presence of an extra (leader?) sequence on the former.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384563
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  • 7
    Electronic Resource
    Electronic Resource
    Two genes for threonine accumulation in barley seeds (1982)
    [s.l.] : Nature Publishing Group
    Nature 299 (1982), S. 278-279 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] From an M2 population of 104 mature embryos (Mi treated with sodium azide) three mutants resistant to lysine plus threonine (2-3 mM) were selected for further study. These were R(Rothamsted) 2501 (ref. 6), R3004 and R3202 which produced sensitive and resistant progeny in the M3 generation. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/299278a0
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  • 8
    Electronic Resource
    Electronic Resource
    S -adenosylmethionine—a novel regulator of aspartate kinase (1980)
    [s.l.] : Nature Publishing Group
    Nature 287 (1980), S. 357-359 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Initial studies suggested that plant aspartate kinases may be inhibited by Lys alone6'7, Thr alone8 or in a concerted manner by Lys plus Thr9. More recent work has shown that certain plants contain two isoenzymes, one sensitive to Thr and one to Lys, the relative proportions of which may vary at ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/287357a0
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  • 9
    Electronic Resource
    Electronic Resource
    The isolation and characterisation of a catalase-deficient mutant of barley (Hordeum vulgare L.) (1983)
    Springer
    Planta 159 (1983), S. 505-511 
    Details
    ISSN: 1432-2048
    Keywords: Catalase deficiency ; Hordeum (mutant) ; Mutant (barley) ; Photorespiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A mutant line of barley, R(othamsted)-Pr 79/4, has been isolated which grows poorly in natural air, but normally in air enriched to 0.2% CO2. Analysis of the products of 14CO2 fixation showed that there was no major block in photosynthetic or photorespiratory carbon metabolism in the mutant and that rates of CO2 fixation were only slightly lower than those measured in the wild type (c.v. Maris Mink). Leaves of the mutant line contained only 10% of the catalase (EC 1.11.1.6) activity found in the wild type; and the two major bands of catalase activity detected after starch-gel electrophoresis of extracts of normal leaves were missing from similar extracts of RPr 79/4. Peroxisomes isolated from mutant leaves contained negligible catalase activity, but normal levels of other enzymes involved in photorespiration. Genetic analysis has shown that the mutation is recessive and that both air-sensitivity and catalase-deficiency segregate together in F2 plants derived from a cross between the mutant and the cultivar Golden Promise. [1-14C]Glycollate was not converted to 14CO2 faster in the mutant leaves than in the normal leaves. Thus there was no evidence that photorespiratory CO2 may be obtained by the chemical action of H2O2 on glyoxylate or hydroxypyruvate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409139
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  • 10
    Electronic Resource
    Electronic Resource
    Feedback-insensitive aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine (1983)
    Springer
    Planta 157 (1983), S. 32-38 
    Details
    ISSN: 1432-2048
    Keywords: Aspartate kinase (isoenzymes) ; Hordeum (mutants) ; Isoenzymes (feedback sensitivity) ; Mutant (barley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulatory properties of aspartate kinase (EC 2.7.2.4) and homoserine dehydrogenase (EC 1.1.1.3) in two barley (Hordeum vulgare L.) mutants resistant to growth inhibition by lysine plus threonine, Rothamsted (R) 3004 and R3202, were compared with those in the normal, sensitive parent line cv. Bomi. Three forms of aspartate kinase (AKI, AKII, AKIII) were chromatographically separated and were considered to represent at least three independently regulated isoenzymes. Aspartate kinase I was inhibited by threonine; AKII and AKIII by lysine or lysine plus S-adenosylmethionine. The characteristics of AKI were unchanged in the mutants. Aspartate kinase II and AKIII from Bomi were both inhibited by lysine and by lysine plus S-adenosylmethionine. Aspartate kinase II from mutant R3202 was altered in its properties such that it was insensitive to lysine or lysine plus S-adenosylmethionine; AKII from mutant R3004 did not differ in its properties from AKII of Bomi. The concentration of lysine required to give half maximal inhibition of AKIII from R3004 was ten times that required for AKIII of Bomi; AKIII from R3202 did not differ from that of Bomi in this regard. There was no change in the properties of homoserine dehydrogenase of the mutants as compared with that of Bomi. We conclude that the lt1 and lt2 loci code for structural genes for lysine- and lysine plus S-adenosylmethionine-sensitive aspartate kinase isoenzymes. The mutant genes Lt1b and Lt2 in R3202 and R3004 respectively code for feedback-desensitized isoenzymes. The presence of one of these is sufficient to allow the synthesis of methionine to overcome the growth inhibition by lysine plus threonine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00394537
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