1973
DOI: 10.1042/bj1340001
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Biosynthesis of ergotamine by Claviceps purpurea (Fr.) Tul

Abstract: High-yielding strains of Claviceps purpurea (Fr.) Tul, grown on a defined medium, have been used for a study of the biosynthesis of the peptide ergot alkaloid, ergotamine.

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Cited by 24 publications
(9 citation statements)
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References 20 publications
(39 reference statements)
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“…Furthermore, the rate of synthesis and the spectrum of products is controlled by the nature and concentration of the amino acids present in the cell-free incubations, which is consistent with earlier in vivo data concerning the role of amino acids in the cellular pool of C. purpurea (31,46). From the data presented here it follows that LPS has a broad amino acid substrate specificity giving it the capacity to synthesize naturally many different ergopeptine structures, probably according to fluctuations in the free amino acid pool.…”
Section: Discussionsupporting
confidence: 78%
“…Furthermore, the rate of synthesis and the spectrum of products is controlled by the nature and concentration of the amino acids present in the cell-free incubations, which is consistent with earlier in vivo data concerning the role of amino acids in the cellular pool of C. purpurea (31,46). From the data presented here it follows that LPS has a broad amino acid substrate specificity giving it the capacity to synthesize naturally many different ergopeptine structures, probably according to fluctuations in the free amino acid pool.…”
Section: Discussionsupporting
confidence: 78%
“…Tryptophan and methionine serve as precursors of D-lysergic acid via the elymoclavine pathway in C. purpurea (Bassett et al, 1973;Floss, 1976). We therefore investigated the influence of these two amino acids on ergot peptide synthesis in the protoplasts and the mycelium.…”
Section: Ejkect Of Externally Added Tryptophan and Methioninementioning
confidence: 99%
“…Uber die sich daran anschliel3ende Biosynthese der Ergopepti- [37], ist die Sequenz Chanoelavin-I-*Agroelavin--*Elymoelavin gut bewiesen [30,38]. Bei diesem Ubergang muB eine zweite Isomerisierung der Doppelbindung eingetreten sein, denn die markierte, mit einem Sternehen bezeichnete und cis-ständige Me- [44,45], als Precursor für die a-Hydroxy-ci-arnino-carbonsaure (es kOnnte für andere Ergopeptine auch L-ot-Aminobuttersäurc oder L-Alanin sein), L-Proiin, 77, [46,47], als gemeinsamer Baustein alier Peptidaikaloide und L-Phenyiaianin, 78, [47,48]. (Die ietztgenannte Aminosãure ist in andern Ergopeptinen durch L-Vaun, L-Leucin oder L-Isoleucin ersetzt).…”
Section: Zur Biosynthese Der Ergotalkaloideunclassified