Zusammenfassung
Die in den nachfolgenden Abschnitten dieses Kapitels zu behandelnden Stickstoffverbindungen lassen in ihrer überwiegenden Zahl zwei Besonderheiten erkennen:
-
1.
Der Stickstoff ist als Heteroatom Bestandteil mehr oder weniger kompli-zierter Ringsysteme.
-
2.
Der Stickstoff — in aliphatischer oder cyclischer Bindung — fungiert als Trägeratom für CH3-Gruppen.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
Literatur
Abderhalden, E.: Fütterungsversuche mit vollständig abgebauten Nahrungsstoffen. Z. physiol. Chem. 77, 22–58 (1912).
Abderhalden, E., U. S. Buadze: Über die Wirkung des Cholins auf den tierischen Organismus und seine Beziehungen zum Kreatin. Z. physiol. Chem. 164, 280–305 (1927).
Ackermann, D.: Zur vergleichenden Biochemie des Stickstoffs. Vergleichend biochemische Fragen (6. Mosbacher Kolloquium), S. 100–131. Berlin: Springer 1956.
Ackermann, D., U. S. Skraup: Endgültige Konstitutionsermittlung und Synthese des Spinacins. Z. physiol. Chem. 284, 129–131 (1949).
Ames, B. N.: The biosynthesis of histidine. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 357 bis 372. Baltimore 1955.
Arnstein, H. R. V.: The metabolism of glycine. Adv. Protein Chem. 9, 1–91 (1954).
The function of vitamin B12 and folic acid in the metabolism of one-carbon units. Vitamin B12 und Intrinsic Factor, S. 86–100. Stuttgart: Ferdinand Enke 1957.
Aronoff, S.: Biogenesis of the pyridine ring in higher plants. Federat. Proc. 15, 212 (1956).
Baddiley, J., and G. A. Jamieson: Synthesis of “active methionine”. J. Chem. Soc. (Lond.) 1954, 4280–4284.
Berg, P.: A study of formate utilization in pigeon liver extract. J. of Biol. Chem. 205, 145–162 (1953).
Bergmann: Diskussionsbemerkung zum Vortrag von D. Ackermann. Vergleichend biochemische Fragen (6. Mosbacher Kolloquium), S. 129 bis 131. Berlin: Springer 1956.
Berlin, N. I., A. Neuberger and J. J. Scott: The metabolism of δ-aminolaevulic acid. 1. Normal pathways, studied with the aid of N15. Biochemic. J. 64, 80–90 (1956a).
The metabolism of δ-aminolaevulic acid. 2. Normal pathways, studied with the aid of C14. Biochemic. J. 64, 90–100 (1956b).
Beyerman, H. C, et P. H. Enthoven: Synthesis of ⍺-phenacyl-N-methylpiperidine (“sedamine-ketone”) under pseudo-physiological conditions. Rec. Trav. chim. Pays-Bas 75, 82–84 (1956).
Birkinshaw, J. H., W. P. K. Findlay and R. A. Webb: The production of methyl mercaptan by Schizo-phyllum commune Fr. Biochemic. J. 36, 526–529 (1942).
Bloch, K., and R. Schoenheimer: The biological precursors of creatine. J. of Biol. Chem. 138, 167–194 (1941).
Block, R. J., J. A. Stekol and J. K. Loosli: Synthesis of cystine and methionine from sodium sulfate by the goat and by microorganisms of the rumen of the ewe. Arch. of Biochem. a. Biophysics 33, 353–363 (1951).
Bogorad, L., and S. Granick: The enzymatic synthesis of porphyrins from porphobilinogen. Proc. Nat. Acad. Sci. U.S.A. 39, 1176–1186 (1953).
Bohlmann, F.: Die natürlich vorkommenden Polyacetylen-Verbindungen. Angew. Chem. 67, 389–394 (1955).
Borsook, H., and J. W. Dubnoff: The formation of creatine from glycocyamine in the liver. J. of Biol. Chem. 132, 559 (1940).
Bothner-By, A. A., R. F. Dawson and D. R. Christman: IS lysine the source of the pyridine ring in nicotine ? Experientia (Basel) 12, 151–152 (1956).
Bowden, K.: Biogenesis of nicotine. Nature (Lond.) 172, 768 (1953).
Brockmann, H, U. H. Muxfeldt: Die Konstitution des Despeptidoactinomycins. Angew. Chem. 67, 617–618 (1955).
Brown, S. A., and R. U. Byerrum: The origin of the methyl carbon of nicotine formed by Nicotiana rustica L. J. Amer. Chem. Soc. 74, 1523–1526 (1952).
Burroughs, L. F.: 1-Aminocyclopropane-1-carboxylic acid: a new amino-acid in perry pears and cider apples. Nature (Lond.) 179, 360–361 (1957).
Butenandt, A., E. Biekert U. G. Neubert: Untersuchungen über Ommochrome, eine Klasse natürlicher Phenoxazonfarbstoffe. Angew. Chem. 68, 379 (1956).
Butenandt, A., P. Karlson u. W. Zillig: Über das Vorkommen von Kynurin in Seidenspinnerpuppen. Z. physiol. Chem. 288, 125–129 (1951).
Butenandt, A., U. U. Renner: Über Kynuramin als Intermediärprodukt des Tryptophan-Stoffwechsels. Z. Naturforsch. 8b, 454–462 (1953).
Butenandt, A., U. Schiedt, E. Biekert u. R. J. T. Cromartie: Über Ommochrome. IV. Mitt. Konstitution des Xanthommatins. Ann. Chem. 590, 75–90 (1954).
Butenandt, A., W. Weidel U. H. Schlossberger: 3-Oxy-kynurenin als cn+-Genabhängiges Glied im intermediären Tryptophan-Stoffwechsel. Z. Naturforsch. 4b, 242–244 (1949).
Byerrum, R. U., L. J. Dewey, R. L. Kamill and C. D. Ball: The utilization of glycolic acid for methyl group synthesis in tobacco. J. of Biol. Chem. 219, 345–350 (1956).
Byerrum, R. U., J. H. Flokstra, L.J. Dewey and C. D. Ball: Incorporation of formate and the methyl group of methionine into methoxyl groups of lignin. J. of Biol. Chem. 210, 633–643 (1954).
Byerrum, R. U., R. L. Hamill and C. D. Ball: The incorporation of glycine into nicotine in tobacco plant metabolism. J. of Biol. Chem. 210, 645–650 (1954).
Byerrum, R. U., R. L. Ringler, R. L. Hamill and C. D. Ball: Serine and formaldehyde as metabolic precursors for the nicotine N-methyl group. J. of Biol. Chem. 216, 371–378 (1955).
Byerrum, R. U., C. S. Sato and C. D. Ball: Utilization of betaine as a methyl group donor in tobacco. Plant Physiol. 31, 374–377 (1956).
Byerrum, R. U., and R. E. Wing: The role of choline in some metabolic reactions of Nicotiana rustica. J. of Biol. Chem. 205, 637–642 (1953).
Cantoni, G. L.: Enzymatic mechanisms and biological significance of transmethylation reactions. 3. Congr. Internat. de Biochemie, Bruxelles, 1955, S. 233–237.
Cantoni, G. L., and J. Durell: Activation of methionine for transmethylation. II. The methionine-acti-vating enzyme: studies on the mechanism of the reaction. J. of Biol. Chem. 226, 1033–1048 (1957).
Cantoni, G. L., and E. Scarano: The formation of S-adenosylhomocysteine in enzymatic transmethylation reactions. J. Amer. Chem. Soc. 76, 4744 (1954).
Challenger, F.: Biological methylation. Adv. Enzymol. 12, 429–491 (1951).
Some aspects of mycological methylation and their relation to analogous processes in plants and animals, and to purely chemical reactions. 3. Congr. Internat. de Biochimie, Bruxelles, 1955, S. 238–241.
Challenger, F., and C. Higginbottom: The production of trimethyl-arsine by Penicillium brevicaule (Scopulariopsis brevicaulis). Biochemic. J. 29, 1757–1778 (1935).
Challenger, F., D. B. Lisle and P. B. Dransfield: The study of mycological methylation with radioactive methyl donors or sources. Chem. a. Ind. 1953, 128–129.
Cookson, G. H.: The structure of porphobilinogen. Nature (Lond.) 172, 457–458 (1953).
Cookson, G. H., and C. Rimington: Isolation of porphobilinogen from the urine of a patient with acute porphyria. Nature (Lond.) 170, 614 (1952).
Connell, G. E., and C. S. Hanes: Enzymic formation of pyrrolidone carboxylic acid from γ-glutamyl peptides. Nature (Lond.) 177, 377–378 (1956).
Davis, B.D.: Biosynthetic interrelations of lysine, diaminopimelic acid and threonine in mutants of Escherichia coli. Nature (Lond.) 169, 534–536 (1952).
Biosynthesis of aromatic amino acids. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 779–811. Baltimore 1955a.
Intermediates in amino acid biosynthesis. Adv. Enzymol. 16, 247–312 (1955b).
Dawson, R. F.: Alkaloid biogenesis: nicotine demethylation on excised leaves of Nicotiana glutinosa. Amer. J. Bot. 39, 250–253 (1952).
Della Rosa, R. J., K. I. Altman and K. Salomon: The biosynthesis of chlorophyll as studied with labeled glycine and acetic acid. J. of Biol. Chem. 202, 771–779 (1953).
Dewey, L. J., and R. U. Byerrum: Biosynthese des Pyrrolidin-Ringes von Nicotin. (Vortragsreferat.) Angew. Chem. 67, 351 (1955).
Dewey, L. J., R. U. Byerrum and C. D. Ball: The origin of the methyl group of nicotine through transmethylation. J. Amer. Chem. Soc. 76, 3997–3999 (1954).
Diener, T. O., and C. A. Dekker: Isolation and identification of L-pipecolic acid from westem-X diseased peach leaves. Phytopathology 44, 643–645 (1954).
Dresel, E. I. B., and J. E. Falk: Conversion of δ-aminolaevulinic acid to porphobilinogen in a tissue system. Nature (Lond.) 172, 1185 (1953).
Studies on the biosynthesis of blood pigments. II. Haem and porphyrin formation in intact chicken erythrocytes. Biochemic. J. 63, 72–79 (1956a).
Studies on the biosynthesis of blood pigments. III. Haem and porphyrin formation from δ-aminolaevulic acid and from porphobilinogen in haemolysed chicken erythrocytes. Biochemic. J. 63, 80–87 (1956b).
Studies on the biosynthesis of blood pigments. V. Intermediates in haem biosynthesis. Biochemic. J. 63, 388–395 (1956c).
Dubbck, M., and S.Kirkwood: The origin of the O- and N-methyl groups of the alkaloid ricinine. J. of Biol. Chem. 199, 307–312 (1952).
Dubnoff, J. W.: The role of choline oxidase in labilizing choline methyl. Arch. of Biochem. 24, 251–262 (1949).
Eds, F. de, A. N. Booth and F. T. Jones: Methylation and dehydroxylation of phenolic compounds by rats and rabbits. J. of Biol. Chem. 225, 615–621 (1957).
Ehrensvärd, G.: Metabolism of amino acids and proteins. Annual Rev. Biochem. 24, 275–303 (1955).
Ellfolk, N., and R. L. M. Synge: Detection of pyrrolidone carboxylic acid. Biochemic. J. 59, 523–526 (1955).
Elwyn, D., and D. Sprinson: The extensive synthesis of the methyl group of thymine in the adult rat. J. Amer. Chem. Soc. 72, 3317 (1950).
Elwyn, D., A. Weissbach, S. S. Henry and D. B. Sprinson: The biosynthesis of choline from serine and related compounds. J. of Biol. Chem. 213, 281–(1955).
Euler, U. S. V.: Identification of a urine base with nicotine-like action. Nature (Lond.) 154, 17 (1944).
Falk, J. E., E. I. B. Dresel, A. Benson and B. C. Knight: Studies on the biosynthesis of blood pigments. IV. The nature of porphyrins formed on incubation of chicken erythrocyte preparations with glycine, δ-aminolaevulic acid or porphobilinogen. Biochemic. J. 63, 87–94 (1956).
Falk, J. E., E. I. B. Dresel and C. Rimington: Porphobilinogen as a porphyrin precursor, and interconversion of porphyrins in a tissue system. Nature (Lond.) 172, 292–294 (1953).
Fieser, L. F., u. M. Fieser: Ringbildung. In Lehrbuch der organischen Chemie, S. 313–346. Weinheim: Verlag Chemie 1954.
Fincham, J. R. S.: Ornithine transaminase in Neurospora and its relation to the biosynthesis of proline. Biochemic. J. 53, 313–320 (1953).
Fowden, L.: Azetidine-2-carboxylic acid: A new constituent of plants. Nature (Lond.) 176, 347–348 (1955).
Azetidine-2-carboxylic acid: a new cyclic imino acid occuring in plants. Biochemic. J. 64, 323–332 (1956).
Fowden, L., and F. C. Steward: Nitrogenous compounds and nitrogen metabolism in the Liliaceae. I. The occurence of soluble nitrogenous compounds. Ann. of Bot., N. S. 21, 53–67 (1957).
Gale, E. F.: The bacterial amino acid decarboxylases. Adv. Enzymol. 6, 1–32 (1946).
Gibson, K. D., A. Neuberger and J. J. Scott: The purification and properties of δ-amino-laevulic acid dehydrase. Biochemic. J. 61, 618–629 (1955).
Glass, B.: Summary. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 1025. Baltimore 1955.
Gosio, B.: Zur Frage, wodurch die Giftigkeit arsenhaltiger Tapeten bedingt ist. Ber. dtsch. chem. Ges. 30, 1024–1026 (1897).
Granick, S.: Enzymatic conversion of (δ-amino levulinic acid to porphobilinogen. Science (Lancaster, Pa.) 120, 1105–1106 (1954a).
Metabolism of heme and chlorophyll. In D. M. Greenberg, Chemical pathways of metabolism, Bd. II, S. 287–342. New York: Academic Press 1954b.
Greenberg, D. M.: Synthetic processes involving amino acids. In D. M. Greenberg, Chemical pathways of metabolism, Bd. II, S. 113–147. New York: Academic Press 1954.
Grobbelaar, N., and F. C. Steward: Pipecolic acid in Phaseolus vulgaris: Evidence on its derivation from lysine. J. Amer. Chem. Soc. 75, 4341–4343 (1953).
Grobbelaar, N., J. K. Pollard and F. C. Steward: New soluble nitrogen compounds (amino- and iminoacids) in plants. Nature (Lond.) 175, 703–708 (1955).
Guggenheim, M.: Lysin. Die biogenen Amine, 4. Aufl., S. 297–308. Basel u. New York: S. Karger 1951.
Hamill, R. L., R. U. Byerrum and C. D. Ball: A study of the biosynthesis of the methoxyl groups of lignin in tobacco plants. J. of Biol. Chem. 224, 713–716 (1957).
Harris, G., and J. R. A. Pollock: Pipecolinic acid, a widely occuring amino-acid. Chem. a. Ind. 1952, 931.
Harris, J. O., and F. Binns: α-Aminomethylmuconic acid as a possible precursor of niacin. Nature (Lond.) 179, 475–476 (1957).
Hasse, K., U. H. Maisack: Δ1-Pyrrolin und Δ1-Piperidein aus Putrescin imd Cadaverin durch enzymatische Oxydation. Naturwiss. 42, 627–628 (1955a).
Die Reaktionsprodukte der enzymatischen Oxydation von Putrescin und Cadaverin. Biochem. Z. 327, 296–304 (1955b).
Δ1-Aza-cyclohepten, ein enzymatisches Oxydationsprodukt von Hexamethylendiamin. Biochem. Z. 328, 429–432 (1957).
Hayaishi, O.: Enzymatic studies on the metabolic interrelationship of hydroxy-substituted derivatives of tryptophan and its intermediate metabolites. In W. D. Mc Elroy u. B. Glass, Amino acid metabolism, S. 914–929. Baltimore 1955.
Heath, H., and J. Wildy: The biosynthesis of ergothioneine and histidine by Claviceps purpurea. I. The incorporation of 2-C14-acetate. Biochemic. J. 64, 612–620 (1956).
Biosynthesis of ergothioneine. Nature (Lond.) 179, 196–197 (1957).
Heidelberger, C, E. P. Abraham and S. Lepkovsky: Tryptophan metabolism. II. Concerning the mechanism of the mammalian conversion of tryptophan into nicotinic acid. J. of Biol. Chem. 179, 151–155 (1949).
His, W.: Über das Stoffwechselprodukt des Pyridins. Arch. exper. Path. u. Pharmakol. 22, 253–260 (1887).
Hoffmann-Ostenhof, O.: Transmethylasen und verwandte Enzyme. Enzymologie, S. 357–364. Wien: Springer 1954.
Hofmeister, F.: Über Methylirung im Thierkörper. Arch. exper. Path. u. Pharmakol. 33, 198–215 (1894).
Hoppe-Seyler, F. A.: Über das Homarin, eine bisher unbekannte tierische Base. Z. physiol. Chem. 222, 105 (1933).
Hückel, W.: Spannungstheorie. Anwendung der Spannungstheorie auf hetero-cyclische Verbindungen und Verbindungen mit mehrfacher Bindung. Theoretische Grund-lagen der Organischen Chemie, Bd. I, S. 71–85. Leipzig: Geest u. Portig 1952.
Ring-bildung und Ringöffnung. Theoretische Grundlagen der Organischen Chemie, Bd. II, S. 667–680. Leipzig: Geest u. Portig 1954.
Hughes, G. K., and E. Ritchie: Synthesis of alkaloids under physiological conditions, relation to alkaloid biogenesis. Rev. Pure a. Appl. Chem. 2, 125–138 (1952).
Huisgen, R.: Neuere Beiträge zur Chemie mittlerer Ringe. Angew. Chem. 69, 341–359 (1957).
Hulme, A. C, and W. Arthington: New amino-acids in young apple fruits. Nature (Lond.) 170, 659–660 (1952).
Jaffé, M.: Untersuchungen über die Entstehung des Kreatins im Organismus. Z. physiol. Chem. 48, 430–468 (1906).
James, W. O.: Alkaloids in the plant. In R. H. F. Manske u. H. L. Holmes, The alkaloids, Bd. I, S. 16–90. New York: Academic Press 1950.
Alkaloid formation in plants. J. Pharmacy a. Pharmacol. 5, 809–822 (1953).
Jucker, E.: Anwendung von zellmöglichen Alkaloidsynthesen auf einige Gebiete der Arzneimittelsynthese. Chimia 9, 195–215 (1955).
Karlson, P.: Biochemische Wirkungen der Gene. Erg. Enzymforsch. 13, 85–206 (1954).
Klein, G., U. H. Linser: Zur Bildung der Betaine und der Alkaloide in der Pflanze. L Die Bildung von Stachydrin und Trigonellin. Z. physiol. Chem. 209, 75–96 (1932).
Zur Bildung der Betaine und der Alkaloide in der Pflanze. II. Stachydrin und Trigonellin. Planta (Berl.) 19, 366–388 (1933).
Kisliuk, R. L., and W. Sakami: A study on the mechanism of serine biosynthesis. J. of Biol. Chem. 214, 47–57 (1955).
Krebs, H. A., M. M. Hafez and L. V. Eggleston: Indole formation in Bacterium coli commune. Biochemic. J. 36, 306–309 (1942).
Lang, K., U. G. Schmid: Über Prolinoxydase. Biochem. Z. 322, 1–8 (1951).
Lascelles, J.: The synthesis of porphyrins and bacteriochlorophyll by cell suspensions of Rhodo-Pseudomonas sphaeroides. Biochemic. J. 62, 78–93 (1956).
Leete, E.: The biogenesis of nicotine. Chem. a. Ind. 1955, 537.
Leete, E., L. Marion and I. D. Spenser: The biogenesis of alkaloids. XII. The mode of formation of the tropine base of hyoscyamine. Canad. J. Chem. 32, 1116–1123 (1954).
The biogenesis of alkaloids. XIV. A study of the biosynthesis of damascenine and trigonelline. Canad. J. Chem. 33, 405–410 (1955).
Lerner, A. B.: Metabolism of phenylalanine and tyrosine. Adv. Enzymol. 14, 73–128 (1953).
Levy, L., and M. J. Coon: The role of formate in the biosynthesis of histidine. J. of Biol. Chem. 192, 807–815 (1951).
Biosynthesis of histidine from radioactive acetate and glucose. J. of Biol. Chem. 208, 691–700 (1954).
Long, C. L., H. N. Hill and I. M. Weinstock: Studies on the enzymatic transformation of 3-hydroxy-anthranilate to quinolate. J. of Biol. Chem. 211, 405–417 (1954).
Lowy, P. H.: The conversion of lysine to pipecolic acid by Phaseolus vulgaris. Arch. of Biochem. a. Biophysics 47, 228–229 (1953).
Mackenzie, C. G.: Conversion of N-methyl glycines to active formaldehyde and serine. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 684–726. Baltimore 1955.
Mann, P. J. G., and W. R. Smithies: Plant enzyme reactions leading to the formation of heterocyclic compounds. I. The formation of unsaturated pyrrolidine and piperidine compounds. Biochemic. J. 61, 89–100 (1955a).
Plant enzyme reactions leading to the formation of heterocyclic compounds. II. The formation of indole. Biochemic. J. 61, 101–105 (1955b).
Manske, R. H. F.: The isoquinoline alkaloids. J. Chem. Soc. (Lond.) 1954a, 2987–2990.
Die Isochinolin-Alkaloide. Angew. Chem. 66, 568 (1954b).
Marion, L.: The alkaloids of Sedum acre L. Canad. J. Res., Sect. B 23, 165–166 (1945).
Marion, L., R. Lavigne and L. Lemay: The structure of sedamine. Canad. J. Chem. 29, 347–351 (1951).
Mauzerall, D., and S. Granick: The occurrence and determination of δ5-amino-levulinic acid and porphobilinogen in urine. J. of Biol. Chem. 219, 435–446 (1956).
Mehler, A. H.: Metabolism of tryptophan. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 882–908. Baltimore 1955.
Formation of picolinic and quinolinic acids following enzymatic oxydation of 3-hydroxyanthranilic acid. J. of Biol. Chem. 218, 241–254 (1956).
Meister, A.: The α-keto analogues of arginine, ornithine, and lysine. J. of Biol. Chem. 206, 577–585 (1954).
Melville, D. B., and S. Eich: The occurence of ergothioneine in plant material. J. of Biol. Chem. 218, 647–651 (1956).
Melville, D. B., S. Eich and M. L. Ludwig: Biosynthesis of ergothioneine. Federat. Proc. 15, 314 (1956).
The biosynthesis of ergothioneine. J. of Biol. Chem. 224, 871–878 (1957).
Melville, D. B., D. S. Genghof, E. Inamine and V. Kovalenko: Ergothioneine in microorganisms. J. of Biol. Chem. 223, 9–17 (1956).
Mistry, S. P., and B. C. Johnson: Vitamin B12 in methyl group and purine biosynthesis. Vitamin B12 und Intrinsic Factor, S. 101–108. Stuttgart: Ferdinand Enke 1957.
Mitchell, H. K., and M. B. Houlaean: An intermediate in the biosynthesis of lysine in Neurospora. J. of Biol. Chem. 174, 883–887 (1948).
Miyake, A., A. H. Bokman and B. S. Schweigert: 3-Hydroxyanthramlic acid metabolism. J. of Biol. Chem. 211, 391–404 (1954).
Morrison, R. L: Naturally occuring L-pipecolinic acid. Biochemic. J. 50, XIV–XV (1952).
The isolation of L-pipecolinic acid from Trifolium repens. Biochemic. J. 53, 474–478 (1953).
Mothes, K.: Physiology of alkaloids. Annual Rev. Plant Physiol. 6, 393–432 (1955).
Ammoniak-Entgiftung und Amino gruppen-Vorrat. Die Kulturpflanze, Beiheft 1, Biochemie der Kulturpflanzen, S. 103–115. Berlin: Akademie-Verlag 1956.
Muntz, J. A.: The inability of choline to transfer a methyl group directly to homocysteine for methionine formation. J. of Biol. Chem. 182, 489–499 (1950).
Musso, H.: Neue natürliche Aminosäuren. Angew. Chem. 68, 313–323 (1956).
Neidle, A., and H. Waelsch: Histidine synthesis in E.coli. Federat. Proc. 16, 225 (1957).
Neuberg, C, U. A. Grauer: Biosynthese von Mercaptanen. Z. physiol. Chem. 289, 253–256 (1952).
Neuberger, A.: The metabolism of δ-aminolaevulic acid “in vivo” and properties of the δ-aminolaevulic dehydrase. 3. Congr. Internat. de Biochimie, Bruxelles, 1955, S. 204–207.
Neuberger, A., and J. J. Scott: Aminolaevulinic acid and porphyrin biosynthesis. Nature (Lond.) 172, 1093–1094 (1953).
Nyc, J. F., H. K. Mitchell, E. Leifer and W. H. Langham: The use of isotopic carbon in a study of the metabolism of anthranilic acid in Neurospora. J. of Biol. Chem. 179, 783–787 (1949).
Pailer, M.: Die Biogenese der Alkaloide. Österreich. Chem.-Ztg 51, 23–29 (1950).
Parks, L. W., and H. C. Douglas: N-Fructosyl anthranilic acid as a possible intermediate in the synthesis of indole by Saccharomyces. Biochim. et Biophysica Acta 23, 207–208 (1957).
Partridge, C. W. H., D. M. Bonner and C. Yanofsky: A quantitative study of the relationship between tryptophan and niacin in Neurospora. J. of Biol. Chem. 194, 269–278 (1952).
Perry, J. J., and J. W. Foster: Studies on the biosynthesis of dipicolinic acid in spores of Bacillus cereus var. mycoides. J. Bacter. 69, 337–346 (1955).
Phillips, D. M.: Pipecolic acid (piperidine-2-carboxylic acid). Chem. a. Ind. 1953, 127–128.
Pictet, A.: Über die Bildungsweise der Alkaloide in der Pflanze. Arch. Pharmaz. 244, 389 (1906).
Pictet, A., u. G. Court: Über einige neue Pflanzenalkaloide. Ber. dtsch. chem. Ges. 40, 3771–3783 (1907).
Pontecorvo, G.: New fields in the biochemical genetics of microorganisms. Biochem. Soc. Symp. 4, 40–50 (1950).
Powell, J. F.: Isolation of dipicolinic acid (pyridine-2,6-dicarboxylic acid) from spores of Bacillus megatherium. Biochemic. J. 54, 210–211 (1953).
Prasad, K. S. N., and R. Raper: Chemical structures of porphobilinogen. Nature (Lond.) 175, 629–630 (1955).
Rauen, H. M.: Vergleichende Biochemie der C1-Körper. Vergleichend biochemische Fragen (6. Mosbacher Kolloquium), S. 132–164. Berlin: Springer 1956.
Transformy-lierungen und Transoxymethylierungen. Biochem. Z. 328, 562–575 (1957).
Rege, D. V., and A. Sreenivasan: Conversion of uracil to thymine by strains of Bacillus subtilis. J. of Biol. Chem. 208, 471–476 (1954).
Reichard, P.: Biosynthesis of purines and pyrimidines. In E. Chargaff U. J. N. Davidson, The nucleic acids. Bd. II, S. 277–308. New York: Academic Press 1955.
Riesser, O.: Theoretisches und Experimentelles zur Frage der Kreatinbildung im tierischen Organismus. Z. physiol. Chem. 86, 415–435 (1913).
Weitere Beiträge zur Frage der Kreatinbildung aus Cholin und Betain. Z. physiol. Chem. 90, 221–235 (1914).
Rimngton, C, and H. L. Booij: Porphyrin biosynthesis in human red cells. Biochemic. J. 65, 3P (1957).
Rimington, C, and S. Krol: Chemical synthesis of porphobilinogen. Nature (Lond.) 175, 630–631 (1955).
Robinson, R.: A synthesis of tropinone. J. Chem. Soc. (Lond.) 111, 762–768 (1917a).
A theory of the mechanism of the phyto-chemical synthesis of certain alkaloids. J. Chem. Soc. (Lond.) 1917b, 876–899.
Synthesis in biochemistry. J. Chem. Soc. (Lond.) 1936, 1079–1090.
Rothstein, M., C. G. Bly and L. L. Miller: The metabolism of D-lysine-ε-C14. Arch. of Biochem. a. Biophysics 50, 252–256 (1954).
Rothstein, M., and L. L. Miller: The formation of pipecolic acid from lysine in the rat. Federat. Proc. 13, 286 (1954a).
The conversion of lysine to pipecolic acid in the rat. J. of Biol. Chem. 211, 851–865 (1954b).
Loss of the α-amino group in lysine metabolism to form pipecolic acid. J. Amer. Chem. Soc. 76, 1459 (1954c).
The metabolism of L-lysine-6-C14. J. of Biol. Chem. 206, 243–253 (1954d).
Saito, Y., O. Hayaishi, S. Rothberg and S. Senoh: L-Kynurenine hydroxylase. Federat. Proc. 16, 240 (1957).
Sato, C. S., R. U. Byerrum and C. D. Ball: The biosynthesis of pectinic acid methyl esters through transmethylation from methionine. J. of Biol. Chem. 224, 717–723 (1957).
Schayer, R. W., and L. M. Henderson: The conversion of deutero-N15-tryptophan to quinolinic acid by the rat. J. of Biol. Chem. 195, 657–661 (1952).
Schiffmann, E., and D. Shemin: Further studies on the utilization of δ-amino-laevulic acid for porphyrin synthesis. J. of Biol. Chem. 225, 623–628 (1957).
Schlüssel, H., W. Maurer, A. Hock U. O. Hummel: Biosynthese von S35-markiertem Methionin. Biochem. Z. 322, 226–229 (1951).
Schöpf, C: Die Synthese von Naturstoffen, insbesondere von Alkaloiden, unter physiologischen Bedingungen und ihre Bedeutung für die Frage der Entstehung einiger pflanzlicher Naturstoffe in der Zelle. Angew. Chem. 50, 779–790, 797–805 (1937).
Neue Synthesen unter physiologischen Bedingungen. Angew. Chem. 59, 174–175 (1947).
Neuere Synthesen unter physiologischen Bedingungen. Angew. Chem. 61, 31–32 (1949).
Synthesen unter physiologischen Bedingungen. In Naturforschung und Medizin in Deutschland (Fiat-Review). Bd. 37: Präparative Organische Chemie, Teil 2, S. 117–123. 1953.
Schöpf, C, U. G. Lehmann: Die Synthese des Tropinons, Pseudopelletierins, Lobelanins und verwandter Alkaloide unter physiologischen Bedingungen. Liebigs Ann. 518, 1–37 (1935).
Schöpf, C, u. R. Unger: Über physiologische, durch einen Gehalt an verschiedenen Alkaloiden charakterisierte Rassen von Sedum acre L. Experientia (Basel) 12, 19–20 (1956).
Schröter, H.-B.: Biologische Methylierungen. Pharmazie 10, 141–157 (1955).
Zur Frage der Umwandlung von Nicotin in Anabasin im Sproß von Nicotiana glauca. Z.Naturforsch. 12b, 334–336 (1957).
Schröter, H.-B., u. L. Engelbrecht: Nachweis der Nornicotin-Bildung in isolierten Tabakwurzeln. Arch. Pharmaz. Ber. dtsch. pharmaz. Ges. 290, 204–206 (1957).
Schulman, M. P.: Purines and pyrimidines. In D. M. Greenberg, Chemical pathways of metabolism, Bd. II, S. 223–262. New York: Academic Press 1954.
Schweet, R. S.: The quantitative determination of proline and pipecolic acid with ninhydrin. J. of Biol. Chem. 208, 603–612 (1954).
Schweet, R. S., J. T. Holden and P. H. Lowy: The metabolism of lysine in Neurospora. J. of Biol. Chem. 211, 517–529 (1954a).
Lysine metabolism in Neurospora. Federat. Proc. 13, 293 (1954b).
The isolation and metabolism of the α-keto acid of lysine. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 496–506. Baltimore 1955.
Shemin, D.: The succinate-glycine cycle. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 727–740. Baltimore 1955a.
The biosynthesis of porphyrins. 3. Congr. Internat. de Biochimie, Bruxelles, 1955b, S. 197–204.
Shemin, D., J. W. Corcoran, C. Rosenblum and I. M. Miller: On the biosynthesis of the porphyrin-like moiety of vitamin B12. Science (Lancaster, Pa.) 124, 272 (1956).
Shemin, D., and C. S. Russell: δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines. J. Amer. Chem. Soc. 75, 4873–4874 (1953).
Shemin, D., C. S. Russell and T. Abramsky: The succinate-glycine cycle. I. The mechanism of pyrrole synthesis. J. of Biol. Chem. 215, 613–626 (1955).
Shimizu, T.: Verhalten des Pyrrols im Tierkörper. Biochem. Z. 117, 266–268 (1921).
Sourkes, T. L.: Transmethylases. In Sumner-Myrbäck, The enzymes, Bd. I, Teil 2, S. 1068–1078. New York: Academic Press 1951.
Sprinson, D. B.: On the formation of C1-fragments from serine. In W. D.Mc Elroy u. B. Glass, Amino acid metabolism, S. 608–615. Baltimore 1955.
Sribney, M., and S. Kirkwood: Origin of the methylendioxy groups of the alkaloid protopine. Nature (Lond.) 171, 931 (1953).
Stekol, J. A.: Synthetic pathways of methionine, cysteine and threonine. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 509–557. Baltimore 1955.
Stetten, M. R.: Metabolic relationship between glutamic acid, proline, hydroxyproline and ornithine. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 277–290. Baltimore 1955.
Tabor, H.: Diamine oxidase. J. of Biol. Chem. 188, 125–136 (1951).
Treibs, A.: Chemische Grundlagen zur Biosynthese der Porphyrine. 3. Congr. Internat. de Biochimie, Bruxelles, 1955, S. 207–210.
Trier, G.: Über einfache Pflanzenbasen und ihre Beziehungen zum Aufbau der Eiweisse und Lecithine. Berlin: Gebrüder Borntraeger 1912.
Tyler jr. V. E., and A. E. Schwarting: The culture of Claviceps purpurea. III. Tryptophan metabolism. J. Amer. Pharmaceut. Assoc., Sci. Ed. 43, 207 (1954).
Vähätalo, M.-L., and A. I. Virtanen: A new cyclic α-aminocarboxylic acid in berries of cowberry. Acta chem. scand. (Copenh.) 11, 741–743 (1957).
Verly, W. G.: Contribution à l’étude du métabolisme du groupe méthyle labile. Thèse. Université de Liège 1956.
Vigneaud, V. du: A trail of research in sulfur chemistry and metabolism and related fields. Ithaca, N.Y.: Cornell University Press 1952.
Virtanen, A. I.: A new imino-acid in some Liliaceae. Nature (Lond.) 176, 984 (1955).
Virtanen, A. I., u. P. Linko: A new type of nitrogen compound in green plants. A cyclic homoserine derivative in some Liliaceae plants. Acta chem. scand. (Copenh.) 9, 551–553 (1955).
Vogel, H. J.: On the glutamate-proline-ornithine interrelation in various microorganisms. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 335–346. Baltimore 1955.
Waldenström, J., u. B. Vahlquist: Studien über die Entstehung der roten Harn-pigmente (Uroporphyrin und Porphobilin) bei der akuten Porphyrie aus der farblosen Vorstufe (Porphobilinogen). Z. physiol. Chem. 260, 189–209 (1939).
Welch, A. D., and C. A. Nichol: Water-soluble vitamins concerned with one- and two-carbon intermediates. Annual Rev. Biochem. 21, 633–686 (1952).
Westall, R. G.: Isolation of porphobilinogen from the urine of a patient with acute porphyria. Nature (Lond.) 170, 614–616 (1952).
Westley, J., and J. Ceithaml: Synthesis of histidine in E. coli. I. Biochemical mutant studies. Arch. of Biochem. a. Biophysics 60, 215–225 (1956a).
Synthesis of histidine in E. coli. II. Radioisotopic tracer studies. J. of Biol. Chem. 219, 139–149 (1956b).
Wildy, J., and H. Heath: Biosynthesis of ergothioneine by Claviceps purpurea. II Incorporation of S35-methionine and the non-utilization of 2(ring)-C14-histamine. Biochemic. J. 65, 220–222 (1957).
Winterstein, E., U. G. Trier: Die Alkaloide, 1. Aufl. Berlin 1910.
Wiss, O.: Die oxydative Spaltung der 3-Oxyanthranilsäure. Z. Naturforsch. 9b, 740–741 (1954).
Über die Wirkungsweise der Hydroxy-anthranilsäure-Oxydase. Z. Natur-forsch. 11b, 54 (1956).
Wiss, O., u. G. Bettendorf: Über die Umwandlung der 3-Hydroxy-anthranilsäure in Chinolinsäure und Nicotinsäure im tierischen Organismus. II. Die Iso-lierung und vorläufige Charakterisierung des primären Oxydationsproduktes der 3-Hydroxy-anthranilsäure. Z. physiol. Chem. 306, 145–153 (1957).
Wiss, O., H. Simmer U. H. Peters: Über die Umwandlung der 3-Hydroxy-anthranilsäure in Chinolinsäure und Nicotin-säure im tierischen Organismus. I. Die enzymatische Oxydation der 3-Hydroxy-anthranil-säure. Z. physiol. Chem. 304, 221–231 (1956).
Woodward, R. B.: Neuere Entwicklungen in der Chemie der Naturstoffe. Angew. Chem. 68, 13–20 (1956).
Work, E.: The isolation of α,ε-diaminopimelic acid from Corynebacterium diphtheriae and Mycobacterium tuberculosis. Biochemie. J. 49, 17–23 (1951).
Some comparative aspects of lysine metabolism. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 462–492. Baltimore 1955.
Work, E., and R. F. Denman: The use of a bacterial culture field as a source of α,ε-diaminopimelic acid. Biochim. et Biophysica Acta 10, 183 (1953 a).
Work, E., and D. L. Dewey: The distribution of α,ε-diaminopimelic acid among various microorganisms. J. Gen. Microbiol. 9, 394–409 (1953b).
Yanofsky, C.: The absence of a tryptophan-niacin relationship in E. coli and B. subtilis. J. Bacter. 68, 577–584 (1954).
Tryptophan and niacin synthesis in various organisms. In W. D. Mc Elroy U. B. Glass, Amino acid metabolism, S. 930–939. Baltimore 1955a.
On the conversion of anthranilic acid to indole. Science (Lancaster, Pa.) 121, 138–139 (1955b).
The enzymatic conversion of anthranilic acid to indole. J. of Biol. Chem. 223, 171–184 (1956a).
Indole-3-glycerol phosphate, an intermediate in the biosynthesis of indole. Biochim. et Biophysica Acta 20, 438–439 (1956b).
Enzymatic studies with a series of tryptophan auxothrophs of Escherichia coli. J. of Biol. Chem. 224, 783–791 (1957).
Yura, T., and H. J. Vogel: On the biosynthesis of proline in Neurospora crassa: enzymic reduction of Δ1-pyrroline-5-carboxylate. Biochim. et Biophysica Acta 17, 582 (1955).
Zacharius, R. M., J. F. Thompson and F. C. Steward: The detection, isolation and identification of (—)-pipecolic acid as a constituent of plants. J. Amer. Chem. Soc. 74, 2949 (1952).
The detection, isolation and identification of L(—)-pipecolic acid in the nonprotein fraction of beans (Phaseolus vulgaris). J. Amer. Chem. Soc. 76, 2908–2912 (1954).
Zeijlemaker, F. C. J.: The metabolism of nicotinic acid in the green pea and its connection with trigonelline. Acta bot. neerl. 2, 123–143 (1953).
Zeile, K.: Die Biosynthese des Hämins. Angew. Chem. 66, 729–735 (1954).
Neuere Entwicklungen in der Chemie der Porphin-Farbstoffe. Angew. Chem. 68, 193–201 (1956).
Ziegler, K.: Methoden zur Herstellung und Umwandlung großer Ringsysteme. In Houben-Weyl, Methoden der organischen Chemie, 4. Aufl., Bd. IV/2, S. 730–822. 1955.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1958 Springer-Verlag oHG. Berlin · Göttingen · Heidelberg
About this chapter
Cite this chapter
Schröter, HB. (1958). Ringschluß mit N und Methylierung am N. In: Allen, E.K., et al. Der Stickstoffumsatz / Nitrogen Metabolism. Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology, vol 8. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-94733-9_37
Download citation
DOI: https://doi.org/10.1007/978-3-642-94733-9_37
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-94734-6
Online ISBN: 978-3-642-94733-9
eBook Packages: Springer Book Archive