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21Author    Rainer Martin, Gerhard Schilling, Jürgen ReichlingRequires cookie*
 Title    Studies on the Biosynthesis of Pseudoisoeugenols in Tissue Cultures of Pimpinella anisum  
 Abstract    A leaf-differentiating tissue culture which produced substantial amounts of pseudoisoeugenol-(2-methylbutyrate) has been used to examine the origin of the pseudoisoeugenol skeleton. I4 C-and l3 C-labelling revealed L-phenylalanine, frarts-cinnamic acid and p-coumaric acid as precur-sors. 1? C-labelled precursors proved to be especially useful. 
  Reference    Z. Naturforsch. 43c, 328—336 (1988); received January 20 1988 
  Published    1988 
  Keywords    Pimpinella anisum, Umbelliferae, Pseudoisoeugenols, Tissue Culture, Biosynthesis 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0328.pdf 
 Identifier    ZNC-1988-43c-0328 
 Volume    43 
22Author    Z. Schweiz, NaturforschRequires cookie*
 Title    Biosynthesis of Cytochalasans. XI. New Results on the Incorporation of Phenylalanine into Cytochalasin D by Zygosporium masonii [1]  
 Abstract    Incorporation of L-[2-:H]phenyl-[2-:H]alanine and L-phenyl-[2-l3C, l:,N]alanine into cytochala­ sin D by Zygosporium masonii involved the complete loss of both the a -;H-and the a-'^N-atom. Incorporation of a mixture of L-phenyl-[l;>N]alanine and L-[U-l4C]phenylalanine into cytochalasin D and protein amino acids (phenylalanine, leucine, isoleucine) was accompanied by a substantial loss of 15N with respect to 14C. These effects are attributed to rapid exchange reactions taking place while L-phenylalanine is part of the intracellular pool of amino acids. In addition, the medium-and concentration-dependent incorporation of the carbon skeleton of exogeneous D-phenylalanine into cytochalasin D is reported. In a peptone-based complex medium, D-phenyl-alanine is poorly incorporated. Throughout the whole concentration range (0 —250 mg/1), the incorporation rates are less than 10% of those of L-phenylalanine. In a minimal medium contain­ ing NH 4 NO3 as nitrogen source however, D-phenylalanine is preferred over the natural enantiomer by a factor of 1.28 up to 6.78, depending on the concentrations of exogeneous d -and L-phenylalanine. These effects are attributed to the medium-dependent activities of different amino acid transport systems responsible for the uptake of d -and L-phenylalanine in Z. masonii. 
  Reference    Z. Naturforsch. 44c, 19 (1989); received September 7 1988 
  Published    1989 
  Keywords    Cytochalasans, Cytochalasin D, Biosynthesis, Phenylalanine, Zygosporium masonii 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0019.pdf 
 Identifier    ZNC-1989-44c-0019 
 Volume    44 
23Author    Jürgen Reichling, RainerM. ArtinRequires cookie*
 Title    Further Studies on the Biosynthesis of Pseudoisoeugenols in Tissue Cultures of Pimpinella anisum  
 Abstract    Tissue cultures o f Pimpinella anisum and P. major were used to study the biosynthesis o f pseudoisoeugenols. The putative precursors were labelled with 13C with one exception that was labelled with i4C. The incorporation o f the label was controlled by 13C N M R and liquid scintil­ lation, respectively. The biosynthetic sequence found was L-phenylalanine, /-cinnamic acid, /?-coumaric acid, / 7-hydroxycoum aric alcohol, /»-methoxycoumaric alcohol and anethol. The incorporation rates ranged from 0.5% to 25%. 
  Reference    Z. Naturforsch. 45c, 942 (1990); received April 26/July 2 1990 
  Published    1990 
  Keywords    Pseudoisoeugenols, Phenylpropanoids, Biosynthesis, 13C -Labelling Pimpinella Species 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0942.pdf 
 Identifier    ZNC-1990-45c-0942 
 Volume    45 
24Author    Gregor Benning, Wolfgang BarzRequires cookie*
 Title    Accumulation and Biosynthesis of Solanapyrone Phytotoxins by Ascochyta rabiei  
 Abstract    The biosynthesis of the phytotoxins solanapyrone A , B and C produced by the phytopatho-genic fungus Ascochyta rabiei has been investigated. To optimize feeding conditons for the tracer experiments the growth of the fungus and the accumulation of the toxins in submers culture were determined. The accumulation kinetics revealed that formation of the toxins occurs in the stationary phase of the growth indicating that synthesis of solanapyrones follows a typical pattern of secondary metabolism. Incorporation experiments with sodium [1-14C]-and [2-13C]acetate were performed and the NM R-spectroscopically determined labelling pattern of the 13C-enriched solanapyrone A compound confirmed that the carbon skeleton of this compound is formed via the polyketide pathway. The biosynthetic route to solana­ pyrone B is discussed. 
  Reference    Z. Naturforsch. 50c, 181 (1995); received January 9 1995 
  Published    1995 
  Keywords    Biosynthesis, Solanapyrones, Polyketide Phytotoxin, Ascochyta rabiei 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0181.pdf 
 Identifier    ZNC-1995-50c-0181 
 Volume    50 
25Author    Koshi Saito, Atsushi Komamine, Siro SenohRequires cookie*
 Title    Further Studies on the Biosynthesis of Stizolobinic Acid and Stizolobic Acid in the Etiolated Seedlings of Stizolobium hassjoo  
 Abstract    Incorporation of doubly labelled tyrosine into stizolobinic acid and stizolobic acid by the etio­ lated seedlings of Stizolobium hassjoo was studied. The retention of tritium activity in stizolobinic acid was 55%, while that in stizolobic acid was only 4.4% in average. The results strongly suggest that the heterocyclic rings of these two amino acids may be derived from 3,4-dihydroxyphenyl-alanine (DOPA) by extradiol cleavage of the aromatic ring. 
  Reference    (Z. Naturforsch. 31c, 15 [1976]; received September 1 1975) 
  Published    1976 
  Keywords    Stizolobium hassjoo, Biosynthesis, Stizolobinic Acid, Stizolobic Acid, 3, 4-Dihydroxyphenylalanine 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0015.pdf 
 Identifier    ZNC-1976-31c-0015 
 Volume    31 
26Author    G. Forkm, W. Heller, H. GrisebachRequires cookie*
 Title    Anthocyanin Biosynthesis in Flowers of Matthiola incana Flavanone 3-and Flavonoid 3'-Hydroxylases  
 Abstract    Enzyme preparations from flowers o f defined genotypes o f Matthiola incana contain two dif­ ferent hydroxylases for hydroxylation of naringenin in the 3-and 3'-position, respectively. The 3-hydroxylase is a soluble enzyme and requires as cofactors 2-oxoglutarate, Fe2+ and ascorbate. Besides naringenin eriodictyol is a substrate for the 3-hydroxylase. The 3'-hydroxylase is localized in the microsomal fraction and requires NADPH as cofactor. Naringenin and dihydro-kaempferol but not 4-coumarate or 4-coumaroyl-CoA are substrates for this enzyme. 3'-Hy-droxylase activity is present only in genetic lines of M. incana with the wild-type allele b +. 
  Reference    Z. Naturforsch. 35c, 691—6 (1980); received June 25 1980 
  Published    1980 
  Keywords    Anthocyanins, Flavonoids, Biosynthesis, Flavanon 3-Hydroxylase, Flavonoid 3'-Hydroxylase, Matthiola incana 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0691.pdf 
 Identifier    ZNC-1980-35c-0691 
 Volume    35 
27Author    G. Stotz, G. ForkmRequires cookie*
 Title    Hydroxylation of the B-Ring of Flavonoids in the 3'-and 5'-Position with Enzyme Extracts from Flowers of Verbena hybrida  
 Abstract    Enzyme preparations from flowers of Verbena hybrida do not only catalyse hydroxylation of the B-ring of flavanones and dihydroflavonols in the 3'-position but also in the 5'-position. Enzyme activity for 3',5'-hydroxylation was found to be localized in the microsomal fraction and required NADPH as cofactor. Evidence is provided that the formation o f the 3',4\5'-hydroxylated flavanone (5,7,3',4',5'-pentahydroxyflavanone) and dihydroflavonol (dihydromy-ricetin), respectively, proceeds via the corresponding 3',4'-hydroxylated compounds eriodictyol and dihydroquercetin, respectively, which are most probably formed by action o f the same enzyme. Enzyme activity for 3',5'-hydroxylation was found to be strictly correlated with the prescence of 3',4',5'-hydroxylated flavonoid compounds in the flowers. 
  Reference    Z. Naturforsch. 37c, 19—23 (1982); received October 141981 
  Published    1982 
  Keywords    Anthocyanins, Flavonoids, Biosynthesis, Flavonoid 3', 5'-Hydroxylation, Verbena hybrida 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0019.pdf 
 Identifier    ZNC-1982-37c-0019 
 Volume    37 
28Author    Lutz Heide, Eckhard LeistnerRequires cookie*
 Title    Versuche zur Synthese natürlich vorkommender prenylierter Naphthalinderivate. Nachweis eines neuen Prenylnaphthochinon- derivates in Galium mollugo Synthesis o f Naturally Occurring Prenylated N aphthalene Derivates. Isolation of a New Prenylnaphthoquinone from Galium mollugo  
 Abstract    prenylated naphthalene derivatives were synthesized and characterized by spectro­ scopic methods. One of these compounds, 2-methoxycarbonyl-3-prenyl-1,4-naphthoquinone, was detected as a new natural product in the root system of Galium mollugo L. This new natural product is likely to be related to the biosynthesis of mollugin and anthraquinones. 
  Reference    Z. Naturforsch. 37c, 354 (1982); received January 21 1982 
  Published    1982 
  Keywords    Galium mollugo L, Biosynthesis, Anthraquinones, Naphthalene Derivatives, Prenylation Several 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0354.pdf 
 Identifier    ZNC-1982-37c-0354 
 Volume    37 
29Author    A. Römer, R. B. HerbertRequires cookie*
 Title    Further Observations on the Source of Nitrogen in Phenazine Biosynthesis  
 Abstract    It is concluded from experiments with (S)-[C015NH2]glutamine and [15N]ammonium sulphate that the biosynthesis of iodinin (1), in Brevibacterium iodinum, and of phenazine-1-carboxylic acid (7), in Pseudomonas aureofaciens, is primarily from a single nitrogen source (glutamine) and that 
  Reference    Z. Naturforsch. 37c, 1070—1074 (1982); received July 26 1982 
  Published    1982 
  Keywords    Phenazines, Biosynthesis, Nitrogen Incorporation, Brevibacterium iodinum, Pseudomonas aureofa-ciens 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-1070.pdf 
 Identifier    ZNC-1982-37c-1070 
 Volume    37 
30Author    M. Argarete, N. Eu-, M. Üller, H. Ainfried, E. A. SchenkRequires cookie*
 Title    Der Einfluß von Cycloheximid und Chloramphenicol auf die Biosynthese der Photosynthese-Pigmente in Cyanophora paradoxa Korsch. HI. Chlorophyll a und Phycochromoproteide Chlorophyll a and Phycochrom oproteids  
 Abstract    The Influence o f Cyclohexim ide and C hloram phenicol on the B iosynthesis o f the P hotosynthetic P igm ents in Cyanophora paradoxa. III. The inhibition effects o f CHI and CA on the biosynthesis o f the tetrapyrrolpigments were measured with two methods (in vivo VIS-spectroscopy, for chlorophyll (Chi) and the phyco­ chromoproteids, 14C incorporation only for Chi). In the case o f the Chl-biosynthesis both methods show the sam e results: a) In vivo VIS-spectroscopy demonstrates that the inhibition effect o f CA manifests faster than that o f CHI, b) during the 14C incorporation into Chi chloramphenicol (CA) inhibits more than cyclohexim ide (CHI) in contrary to the behaviour o f chloroplasts. It seems that the CHI caused decrease o f l4C incorporation into Chi can be ascribed to the decreased photosynthesis. The influence o f the antibiotics o f the phycochrom o­ proteids is similar to that observed for chlorophyll. It is remarkable that under the influence o f CHI the phycochromoproteid biosynthesis is significantly better than under CA influence, although CHI damages the consortium more than CA. That can be interpreted, as for chlorophyll, with a more endocytobiont coded phycochrom oproteid synthesis. 
  Reference    Z. Naturforsch. 38c, 990—9 (1983); received July 19 1983 
  Published    1983 
  Keywords    Cyanophora paradoxa, Biosynthesis, Chlorophyll, Phycocyanin, Allophycocyanin, C yclohexim ide, Chloramphenicol 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0990.pdf 
 Identifier    ZNC-1983-38c-0990 
 Volume    38 
31Author    Elisabeth Häusler, Maike Petersen, AugustW. AlfermannRequires cookie*
 Title    Hydroxyphenylpyruvate Reductase from Cell Suspension Cultures of Coleus blumei Benth  
 Abstract    Cell suspension cultures o f Coleus blumei Benth. producing high amounts o f rosmarinic acid were used to study the biosynthetic pathway o f this caffeic acid ester. One o f the involved en­ zymes, the hydroxyphenylpyruvate reductase (H PPR), is characterized in this paper. HPPR catalyzes the N A D (P)H dependent reduction o f /^-hydroxyphenylpyruvate to /»-hydroxyphen-yllactate. The enzyme developed maximal activity at an incubation temperature o f 37 °C and at a pH o f 6.5 to 7.0. The reaction proceeded linearly for an incubation time o f 60 min and up to a protein concentration o f 0.2 mg per assay. As electron donor HPPR accepted N A D H and N A D P H with A^m-values o f 190 jim and 95 |im respectively. The enzyme reduced differently substituted hydroxyphenylpyruvates but not ß-phenylpyruvate. The apparent A^m-values for the various substrates were at 10 for /^-hydroxyphenylpyruvate, at 130^xm for 3,4-dihy-droxyphenylpyruvate and at 250 |iM for 3-methoxy-4-hydroxyphenylpyruvate. HPPR was com petitively inhibited by rosmarinic acid and pyruvate with /^-values o f 210 |iM and 200 |IM respectively. Caffeic acid,/>-coumaric acid and cinnamic acid did not affect the enzyme activity but/>-coumaroyl-CoA inhibited HPPR. 
  Reference    Z. Naturforsch. 46c, 371—3 (1991); received January 21 /February 26 1991 
  Published    1991 
  Keywords    Coleus blumei, Lamiaceae, Cell Suspension Culture, Biosynthesis, Rosmarinic Acid 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0371.pdf 
 Identifier    ZNC-1991-46c-0371 
 Volume    46 
32Author    H.-R SchultenRequires cookie*
 Abstract    A combined 13 C nuclear magnetic resonance and field desorption mass spectrometric investigation of algae grown on 13 C02 has shown that the isotopic enrichment of amino acids extracted therefrom is neither uniform nor statistical. The use of these two indepen-dent techniques allows a new, detailed and accurate insight into the label distribution resulting from biosynthesis. The observed deviations from the statistical abundances are systematic. A system for classifying each member of the complex ensemble of isotopic species has been devised, so that the isotopomers may be ordered according to their relative probability of occurrence. 
  Reference    Z. Naturforsch. 36b, 1289—1296 (1981); received May 20 1981 
  Published    1981 
  Keywords    13 C Enriched Amino Acids, Biosynthesis, Label Distribution, NMR Spectra, Field Desorption Mass Spectrometry 
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 TEI-XML for    default:Reihe_B/36/ZNB-1981-36b-1289.pdf 
 Identifier    ZNB-1981-36b-1289 
 Volume    36 
33Author    H. Wesch, R. Jonak, H. Nemetschek-Gansler, H. Riedl, Th NemetschekRequires cookie*
 Title    Der Einfluß von D-Penicillamin auf den Gehalt einiger Organe an Spurenelementen sowie auf die mechanischen Eigenschaften von Kollagen Trace Elements in Several Organs and Mechanical Properties of Collagen under the Influence of D-Penicillamin  
 Abstract    The content of trace elements in several organs of rats under the influence of D-penicillamine (D-PA) was investigated by the neutronactivation-analysis. It could be shown an diminution of Cu, and Co under D-PA-treatment, the content of Fe, Mn, Rb and Zn was not influenced. The investigat­ ed organs didn't show any submicroscopic alterations under D-PA. On isolated collagen fibrils of tail tendon was seen a significantly diminuition of E-moduls. In accordance with Siegel the principal effect of D-PA is thought to block the synthesis of functional groups from Schiff-base crosslink precursors but not to inhibit lysyloxidase by loss of Cu-ions of connective tissue. The thermostability of D-PA influenced fibrils is changed in stretched state only and will be due to the lack of crosslink Schiff-bases; where as the shrinking point of not stretched fibrils shows only aging dependent changes. 
  Reference    Z. Naturforsch. 33c, 346 (1978); eingegangen am 17. März 1978 
  Published    1978 
  Keywords    D-Penicillamin, Trace Elements, Electron Microscopy, Biosynthesis, Cross-Links, Mechanical Properties of Collagen 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0346.pdf 
 Identifier    ZNC-1978-33c-0346 
 Volume    33 
34Author    U. Margna, L. Laanest, E. Margna, T. VainjärvRequires cookie*
 Title    L-Tyrosine as a Precursor of Flavonoids in Buckwheat Cotyledons  
 Abstract    Exogenous L-tyrosine was incorporated 1 3 -1 4 tim es less effectively than exogenous L-phenyl-alanine into flavonoids in excised cotyledons o f 3 days old buckw heat seedlings but proved to be an only 5 times poorer precursor when the experim ents were carried out with 5 days old material. Simultaneous administration o f L-phenylalanine m arkedly reduced incorporation o f L-tyrosine into flavonoids. A similar decrease in the utilization o f exogenous L-tyrosine for flavonoid b io­ synthesis occurred in kinetin-treated cotyledons. H owever, in cotyledons treated with high doses o f glyphosate, an inhibitor o f the shikim ic acid pathway, an increase in the formation o f flavonoids from exogenously supplied L-tyrosine was observed. Under all conditions the relative incorporation rate o f exogenous L-tyrosine was highest for anthocyanins and lowest for C-glyco-sylflavones while within the latter class o f com pounds the luteolinic derivatives orientin and iso-orientin incorporated more label than their apigeninic analogues vitexin and isovitexin. PAL and TAL activities were found to be present in the cotyledons in a ratio o f 50:1. The possible role o f L-tyrosine as an alternative natural precursor for the biosynthesis o f flavonoids and other related polyphenols is discussed. 
  Reference    Z. Naturforsch. 40c, 154 (1985); received April 24/O ctober 29 1984 
  Published    1985 
  Keywords    Anthocyanins, Flavonoids, Biosynthesis, [14C-L]Tyrosine, [14C-L]Phenylalanine, Kinetin, Glyphosate, Fagopyrum esculentum 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0154.pdf 
 Identifier    ZNC-1985-40c-0154 
 Volume    40 
35Author    Hans-Jürgen Sieweke, Eckhard LeistnerRequires cookie*
 Title    tf-Succinylbenzoate: Coenzyme A Ligase, an Enzyme Involved in Menaquinone (Vitamin K2) Biosynthesis, Displays Broad Specificity  
  Reference    Z. Naturforsch. 46c, 585 (1991); received January 18/April 12 1991 
  Published    1991 
  Keywords    M ycobacterium phlei, Biosynthesis, M enaquinones, o-Succinylbenzoate: Coenzyme A Ligase, Substrate Specificity o f o-Succinylbenzoate: Coenzyme A Ligase 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0585.pdf 
 Identifier    ZNC-1991-46c-0585 
 Volume    46 
36Author    Hamako Obata-Sasamoto, Atsushi Komamine, Koshi SaitoRequires cookie*
 Title    Biosynthesis of 3-Carboxy-6,7-dihydroxy-l, 2,3,4-tetra- hydroisoquinoline and l-Methyl-3-carboxy-6,7-dihydroxy-l, 2,3,4- tetrahydroisoquinoline in a Callus Culture of Stizolobium hassjoo  
 Abstract    dl-[/?-14C] 3,4-Dihydroxyphenylalanine (DOPA), [2-14C]pyruvate and [2-14C]acetate were ad­ ministered to a callus culture o f S. hassjoo and incorporation of the radioactivity into 3-carboxy-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (I) and l-methyl-3-carboxy-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline (II) was examined. Incorporation of radioactivity from labelled DOPA into I and II, and from acetate into I were observed, while that from pyruvate into I and II and from acetate into II were hardly detected. The biosynthetic pathways o f I and D were discussed. 
  Reference    Z. Naturforsch. 36c, 921 (1981); received August 21 1981 
  Published    1981 
  Keywords    Stizolobium hassjoo, Biosynthesis, 3-Carboxy-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline, 1 -Methyl-3-carboxy-6, 7-dihydroxy-1, 2, 3, 4-tetrahydroisoquinoline, Callus Culture 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0921.pdf 
 Identifier    ZNC-1981-36c-0921 
 Volume    36