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  • ZIB Catalog
  • Articles: DFG German National Licenses  (10)
  • 2000-2004
  • 1990-1994  (7)
  • 1960-1964  (3)
  • 1890-1899
  • 1880-1889
  • 1990  (7)
  • 1963  (3)
  • 1888
  • Biosynthesis
Source
  • ZIB Catalog
  • Articles: DFG German National Licenses  (10)
Material
Years
  • 2000-2004
  • 1990-1994  (7)
  • 1960-1964  (3)
  • 1890-1899
  • 1880-1889
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Regulation of biosynthesis of bacilysin byBacillus subtilis (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 91-100 
    Details
    ISSN: 1476-5535
    Keywords: Bacilysin ; Bacillus subtilis ; Antibiotic ; Biosynthesis ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Production of the dipeptide antibiotic bacilysin byBacillus subtilis 168 was growth associated and showed no evidence of repression by glucose or sucrose. Carbohydrates other than glucose and sucrose yielded lower specific titers of bacilysin. Bacilysin production in three such carbon sources (maltose, xylose, ribose) was delayed until growth slowed down. Ammonium salts were poor for bacilysin production when used as the sole nitrogen source. When added to the standard medium containing glutamate, they suppressed antibiotic production. Aspartate was slightly better than glutamate for antibiotic production as sole nitrogen source. No other nitrogen source tested, including inorganic, organic or complex, approached the activity of glutamate or aspartate. When added to glutamate, casamino acids, phenylalanine and alanine (a substrate of bacilysin synthetase) suppressed bacilysin production while stimulating growth. Phosphate provided for optimum growth and production at 7.5 mM and both processes were inhibited at higher concentrations. Ferric citrate stimulated growth and inhibited bacilysin production, the effects being due to both the iron and the citrate components. Elimination of ferric citrate stimulated production as did increasing the concentration of Mn to its optimum concentration of 6.6×10−4M.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01576428
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of indolepyruvic acid as an intermediate of rebeccamycin biosynthesis (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 291-294 
    Details
    ISSN: 1476-5535
    Keywords: Rebeccamycin ; Indolepyruvic acid ; Biosynthesis ; Antitumor antibiotic ; Saccharothrix aerocolongigenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Experimental evidence is presented to demonstrate that indolepyruvic acid is an intermediate in the rebeccamycin biosynthetic pathway. [3-14C]Indolepyruvic acid was prepared and efficiently incorporated (8%) into rebeccamycin bySaccharothrix aerocolonigenes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575876
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Biosynthesis of coenzyme F420 and methanopterin in Methanobacterium thermoautotrophicum (1990)
    Springer
    Archives of microbiology 153 (1990), S. 259-263 
    Details
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Coenzymes ; Biosynthesis ; Methanopterin ; Factor F420 ; Deazaflavin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Growing cultures of Methanobacterium thermoautotrophicum were supplemented with [U-14C]adenosine or [1′-14C]adenosine. 7,8-Didemethyl-8-hydroxy-5-deazariboflavin (factor F0) and 7-methylpterin were isolated from the culture medium. Hydrolysis of cellular RNA yielded purine and pyrimidine nucleotides. The ribose side chain of proffered adenosine is efficiently incorporated into cellular adenosine and guanosine nucleotide pools but not into pyrimidine nucleotides. Thus, M. thermoautotrophicum can utilize exogenous adenosine by direct phosphorylation without hydrolysis of the glycosidic bond, and AMP can be efficiently converted to GMP. Factor F0 and 7-methylpterin had approximately the same specific activities as the purine nucleotides. It follows that the ribityl side chain of factor F0 is derived from the ribose side chain of a nucleotide precursor by reduction. The pyrazine ring of methanopterin is formed by ring expansion involving the ribose side chain of the precursor, GTP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249078
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of lipid activated pseudomurein precursors from Methanobacterium thermoautotrophicum (1990)
    Springer
    Archives of microbiology 153 (1990), S. 444-447 
    Details
    ISSN: 1432-072X
    Keywords: Methanogens ; Archaebacteria ; Methanobacterium thermoautotrophicum ; Cell walls ; Murein ; Pseudomurein ; Biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From cell extracts of the pseudomurein possessing methanogen Methanobacterium thermoautotrophicum two putative pseudomurein precursors were isolated and characterized: (1) an undecaprenyl pyrophosphate activated disaccharide pentapeptide composed of N-acetylglucosamine, N-acetyltalosaminuronic acid, alanine, glutamic acid and lysine in a molar ratio of 1:1:2:2:1 and (2) the corresponding undecaprenyl pyrophosphate activated tetrapeptide lacking one alanine residue. The isolation of these precursors show that the biosynthesis of the eubacterial murein and the methano-bacterial pseudomurein differs not only in the cytoplasmic step, as recently described, but also in the lipid stage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248425
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  • 5
    Electronic Resource
    Electronic Resource
    Biosynthesis, cDNA and amino acid sequences of a precursor of conglutin δ, a sulphur-rich protein from Lupinus angustifolius (1990)
    Springer
    Plant molecular biology 15 (1990), S. 879-893 
    Details
    ISSN: 1573-5028
    Keywords: Biosynthesis ; DNA sequence ; Lupinus angustifolius ; protein sequence ; plant cDNA ; 2S storage protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The biosynthesis of conglutin δ has been studied in developing cotyledons of Lupinus angustifolius L. Precursors of conglutin δ formed the major sink for [35S]-cysteine incorporated by developing lupin cotyledons, and these precursors were rapidly sequestered into the endoplasmic reticulum. The sequence of a cDNA clone coding for one such precursor of conglutin δ was determined. The structure of the precursor polypeptide for conglutin δ predicted from the cDNA sequence contained an N-terminal leader peptide of 22 amino acids directly preceding a subunit polypeptide of M r 4520, together with a linking region of 13 amino acids and a subunit polypeptide of M r 9558 at the C-terminus. The amino acid sequence predicted from the cDNA sequence showed minor variations from that established by sequencing of the protein purified from mature dried seeds (Lilley and Inglis, 1986). These were consistent with the existence of a multi-gene family coding for conglutin δ. Comparison of the sequences of conglutin δ with those of other 2S storage proteins showed that the cysteines involved in internal disulphide bridges between the mature subunits of conglutin δ, were maintained throughout this family of proteins but that little else was conserved either at the protein or DNA level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039427
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  • 6
    Electronic Resource
    Electronic Resource
    Artemisia annua L.: a source of novel antimalarial drugs (1990)
    Springer
    Pharmacy world & science 12 (1990), S. 169-181 
    Details
    ISSN: 1573-739X
    Keywords: Artemisia annua L. ; Artemisinin ; Biosynthesis ; Chemistry, analytical ; Clinical trials ; Pharmacology ; Sesquiterpene lactones ; Structure—activity relationship
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Artemisia annua L. contains artemisinin, an endoperoxide sesquiterpene lactone, mainly in its leaves and inflorescences. This compound and a series of derivatives have attracted attention because of their potential value as antimalarial drugs. In this review a survey of the currently available literature data is given. It includes phytochemical aspects, such as constituents ofA. annua, the artemisinin content during the development of the plant and its biosynthesis, isolation, analysis and stability. Total chemical synthesis of artemisinin is referred to, as well as structure—activity relationships of derivatives and simplified analogues. Pharmacological studies are summarized, including the mechanism of action, interaction of the antimalarial activity with other drugs, possible occurrence of resistance to artemisinin, clinical results, toxicological aspects, metabolism and pharmacokinetics. Finally, plant cell biotechnologyy is mentioned as a possible means to obtain plants and cell cultures with higher artemisinin contents, allowing an industrial production of pharmaceuticals containing this novel drug.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01980041
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation of a crustaceann-acetyl-d-glucosamine-1-phosphate transferase and its activation by phospholipids (1990)
    Springer
    Journal of comparative physiology 159 (1990), S. 777-788 
    Details
    ISSN: 1432-136X
    Keywords: Chitin ; GlcNAc-1-P transferase ; Phospholipid ; Biosynthesis ; Artemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Then-acetyl-d-glucosamine-1-phosphate: dolichol phosphate transferase fromArtemia has been partially purified and characterized. The enzyme is solubilized from crude microsomes using Triton X-100, and after detergent removal appears to be associated with phospholipids. Using dolichol phosphate and UDP-n-acetyl-d-glucosamine as substrates, the enzyme catalyzes the formation of dolichol-pyrophosphate-n-acetyl-d-glucosamine. the product identity has been verified by TLC and paper chromatography following mild acid hydrolysis. Under the incubation conditions used only one product is made, i.e., Dol-p-p-GlcNAc. The formation of product is linear with increasing amounts of added protein and with time of incubation. The enzyme requires magnesium ions for activity. Activity of the enzyme is stimulated 6-fold by exogenous dolichol phosphate and is also stimulated by added phospholipids, with optimal activity being obtained in the presence of mixtures of phosphatidylcholine and phosphatidylglycerol. Enzymatic activity is not increased upon addition of GDP-mannose or dolichol phosphate mannose. The enzyme is rapidly inactivated by exposure to several detergents, including Triton X-100 and deoxycholate. The activity is inhibited by tunicamycin and by the purified B2 homologue of this antibiotic. Other antibiotic inhibitors such as diumycin and polyoxin D have little effect on the enzyme. Both the microsomal and solubilized enzyme preparations are inactivated by 70% upon treatment with phospholipase A2; activity may be restored by addition of phospholipids. Following hydrophobic interaction chromatography on Phenyl Sepharose, gel filtration chromatography on Sepharose CL-4B indicated that the enzyme, purified 81-fold, contained phophatidylcholine and phosphatidyl-ethanolamine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691724
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    The Biosynthesis of Alkaloids IIPart I of this review appeared in Angew. Chem. Internet. Edit. 2, 341 (1963). (1963)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 2 (1963), S. 441-458 
    Details
    ISSN: 0570-0833
    Keywords: Biosynthesis ; Alkaloids ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.196304411
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  • 9
    Electronic Resource
    Electronic Resource
    The Biogenesis of Ergot AlkaloidsDedicated to Professor Hans von Euler on the occasion of his 90th birthday (1963)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 2 (1963), S. 243-247 
    Details
    ISSN: 0570-0833
    Keywords: Ergot alkaloids ; Alkaloids ; Biosynthesis ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In this article the biogenesis of the ergoline ring in lysergic acid derivatives and the clavines is discussed. T·yptophan and mevalonic acid are the precursors. The N-methyl group is supplied by formate or methionine. Concepts and results dealing with the manner in which the compounds are formed are discussed. Finally, the known biogenetic relationships among the ergot alkaloids are discussed in connection with their biogenesis.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.196302431
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  • 10
    Electronic Resource
    Electronic Resource
    The Biosynthesis of Alkaloids IPart II of this review will appear in a subsequent issue of this journal.Dedicated to Professor Dr. Adolf Butenandt on the occasion of his 60th birthday (1963)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 2 (1963), S. 341-357 
    Details
    ISSN: 0570-0833
    Keywords: Biosynthesis ; Alkaloids ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.196303411
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    Paper (German National Licenses)
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