| | 22 | Author
| Z. Schweiz, Naturforsch | Requires 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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| default:Reihe_C/44/ZNC-1989-44c-0019.pdf | | | | Identifier
| ZNC-1989-44c-0019 | | | | Volume
| 44 | |
| 23 | Author
| Jürgen Reichling, RainerM. Artin | Requires 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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| default:Reihe_C/45/ZNC-1990-45c-0942.pdf | | | | Identifier
| ZNC-1990-45c-0942 | | | | Volume
| 45 | |
| 24 | Author
| Gregor Benning, Wolfgang Barz | Requires 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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| default:Reihe_C/50/ZNC-1995-50c-0181.pdf | | | | Identifier
| ZNC-1995-50c-0181 | | | | Volume
| 50 | |
| 25 | Author
| Koshi Saito, Atsushi Komamine, Siro Senoh | Requires 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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| default:Reihe_C/31/ZNC-1976-31c-0015.pdf | | | | Identifier
| ZNC-1976-31c-0015 | | | | Volume
| 31 | |
| 26 | Author
| G. Forkm, W. Heller, H. Grisebach | Requires 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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| default:Reihe_C/35/ZNC-1980-35c-0691.pdf | | | | Identifier
| ZNC-1980-35c-0691 | | | | Volume
| 35 | |
| 27 | Author
| G. Stotz, G. Forkm | Requires 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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| default:Reihe_C/37/ZNC-1982-37c-0019.pdf | | | | Identifier
| ZNC-1982-37c-0019 | | | | Volume
| 37 | |
| 29 | Author
| A. Römer, R. B. Herbert | Requires 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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| default:Reihe_C/37/ZNC-1982-37c-1070.pdf | | | | Identifier
| ZNC-1982-37c-1070 | | | | Volume
| 37 | |
| 30 | Author
| M. Argarete, N. Eu-, M. Üller, H. Ainfried, E. A. Schenk | Requires 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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| default:Reihe_C/38/ZNC-1983-38c-0990.pdf | | | | Identifier
| ZNC-1983-38c-0990 | | | | Volume
| 38 | |
| 31 | Author
| Elisabeth Häusler, Maike Petersen, AugustW. Alfermann | Requires 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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| default:Reihe_C/46/ZNC-1991-46c-0371.pdf | | | | Identifier
| ZNC-1991-46c-0371 | | | | Volume
| 46 | |
| 32 | Author
| H.-R Schulten | Requires cookie* | | | Title
| | | | | 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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| default:Reihe_B/36/ZNB-1981-36b-1289.pdf | | | | Identifier
| ZNB-1981-36b-1289 | | | | Volume
| 36 | |
| 33 | Author
| H. Wesch, R. Jonak, H. Nemetschek-Gansler, H. Riedl, Th Nemetschek | Requires 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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| default:Reihe_C/33/ZNC-1978-33c-0346.pdf | | | | Identifier
| ZNC-1978-33c-0346 | | | | Volume
| 33 | |
| 34 | Author
| U. Margna, L. Laanest, E. Margna, T. Vainjärv | Requires 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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| default:Reihe_C/40/ZNC-1985-40c-0154.pdf | | | | Identifier
| ZNC-1985-40c-0154 | | | | Volume
| 40 | |
| 36 | Author
| Hamako Obata-Sasamoto, Atsushi Komamine, Koshi Saito | Requires 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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| default:Reihe_C/36/ZNC-1981-36c-0921.pdf | | | | Identifier
| ZNC-1981-36c-0921 | | | | Volume
| 36 | |
|
