Über Aktivierungsreaktionen bei Claviceps

Maier, W.; Erge, D.; Gröger, D.

doi:10.1016/s0015-3796(17)31268-4

Cited by 21 publications

(12 citation statements)

References 12 publications

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“…activation) (see Lipmann, 1971), no evidence was obtained that the enzyme is able to catalyse the formation of a D-lysergyl-peptide or even a D-lysergyl-CoA thioester. This latter compound has been claimed to be a precursor of peptide-bound D-lysergic acid (Maier et al, 1972). Thus it must be supposed that another compound serves as an acceptor for the activated D-lysergic acid residue.…”

Section: Discussionmentioning

confidence: 99%

d-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea

Keller¹,

Zocher²,

Krengel³

et al. 1984

Biochemical Journal

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A D-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea was purified about 145-fold. The enzyme was able to catalyse both the D-lysergic acid-dependent ATP-pyrophosphate exchange and the formation of ATP from D-lysergic acid adenylate and pyrophosphate. Both reactions were also catalysed to a decreased but significant extent with respect to dihydrolysergic acid. The molecular mass of the enzyme was estimated to lie between 135 and 140 kDa. The involvement of the enzyme in the biosynthesis of ergot peptide alkaloids is discussed.

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Section: Discussionmentioning

confidence: 99%

d-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea

Keller¹,

Zocher²,

Krengel³

et al. 1984

Biochemical Journal

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“…On the other hand, previously published data on the cell-free synthesis of ergopeptines indicate that biosynthetic precursors of D-lysergic acid such as elymoclavine or agroclavine rather than free D-lysergic acid serve as the precursors of peptidebound D-lysergic acid (Maier et al, 1981). Instead of free D-lysergic acid a D-lysergyl coenzyme A thioester is proposed to play a role in the biosynthetic process (Maier et al, 1972).…”

mentioning

confidence: 99%

D-Lysergic acid activation and cell-free synthesis of D-lysergyl peptides in an enzyme fraction from the ergot fungus Claviceps purpurea

Keller¹,

Han²,

Stöffler‐Meilicke³

1988

Biochemistry

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The D-lysergic acid activating enzyme from the ergot fungus Claviceps purpurea was purified to near homogeneity. It has a native Mr of about 245,000 and in its denatured form is a single polypeptide chain of Mr 62,000. The enzyme catalyzes the ATP-pyrophosphate exchange reaction dependent on D-lysergic acid and, though much less, that dependent on dihydrolysergic acid. Western blot analysis of SDS electropherograms of crude protein extracts from C. purpurea using monospecific antibodies directed against the D-lysergic acid activating enzyme revealed the immunostaining of one particular band which was identical with that of the D-lysergic acid activating enzyme. No significant immunoreactive band with higher molecular weight was seen, which precludes the possibility that the enzyme had arisen from the proteolysis of a high molecular weight ergot peptide synthetase. An ammonium sulfate fractionated enzyme fraction was prepared from C. purpurea strain C1 that catalyzed the incorporation of D-lysergic acid into two peptides which besides D-lysergic acid contained alanine, phenylalanine, and proline. Dihydrolysergic acid was efficiently incorporated into the corresponding dihydrolysergic acid containing analogues of the two compounds. Radiochemical analysis and degradation studies suggest that the two D-lysergic acid containing peptides most probably are N-[N-(D-lysergyl)-L-alanlyl]-L-phenylalanyl-L-proline lactam and N-[N-(D-lysergyl)-L-analyl]-L-phenylalanyl-D-proline lactam, respectively. N-[N-(D-Lysergyl)-L-alanyl]-L-phenylalanyl-L-proline lactam is considered to be the immediate precursor of ergotamine.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Wir bevorzugen die Hypothese, daB es sich bei der Peptidteilbildung der Cyclolalkaloide um einen RNS-unabhangigen nichtribosomalen ProzeR handelt. Darauf deuten Hemmversuche mit Cycloheximid hin (ERGE et al, 1972). Offenbar Iaufl die Bildung an einem Multienzymkomplex ab, etwa vergleichbar mit der Biosynthese bestimmter Peptidantibiotica (Gramicidin, Tyrocidin).…”

Section: In Diesem Zusammenhang War Auch Das Vorkommen Und Der Stoffunclassified

“…Die einzelnen Verbindungen sollten daher im Pilz intermediar in ,,aktivierterU Form vorliegen. Aktivierungsreaktionen bei Claviceps sind von uns untersucht worden (MAIER et al, 1972). Interessant sind die Befunde iiber die Prolin-Aktivierung in jungen Kulturen eines Ergotoxinbildners.…”

Section: In Diesem Zusammenhang War Auch Das Vorkommen Und Der Stoffunclassified

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Biosynthese Des Peptidteils Der Mutterkornalkaloide Vom Cyclol–typ

Gröger¹

1975

Planta Med

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A review is given on the biosynthesis o f the peptide moiety in ergot alkaloids.Feeding experiments with labeled amino acids have revealed that phenylalanine, proline, valine and leucine are specifically incorporated into the appropriate constituents of the peptides of ergotamine, ergocornine and ergokryptine, respectively. The a-hydroxy-&-amino acid residue of the ergotoxine alkaloids is derived from valine. In the case of ergotamine alanine or a close relative is the immediate precursor of the hydroxyamino acid fragment.The exact mechanism of cyclol formation in ergot alkaloid biosynthesis is not yet clarified. Abe's group in Japan has found the intact incorporation of lysergylalanine and lysergylvaline in peptide alkaloids of various ergot strains. Furthermore they demonstrated the incorporation of L-lezrcyl-L-proline lactam and Lphenylalanyl-l-proline-lactam in ergokryptine and ergotamine, respectively. Other authors (Floss, Groger) did not confirm these results. They have tested the possible involvement o f free simple lysergic acid derivatives, various di-and tripeptides as well as the corresponding diketopiperazines. In these experiments the added precursors were split by the fulzgus into the correspo~zding compounds (lysergic acid and amino acids) prior to incorporation into the peptide moitety o f ergot alkaloids. Based on these results and on inhibitor experiments one may speculate that the synthesis o f the peptide portion is a nonribosomal process. Apparently like in the biosynthesis of peptide antibiotics the peptide chain formation takes place on a multienzyme complex. EinfiihrungBislang sind etwa 50 Mutterkornalkaloide bekannt. Die iiberwiegende Zahl dieser Indolalkaloide wurde aus verschiedenen Claviceps-Arten isoliert. Lange Zeit war man der Ansicht, dat3 nur Vertreter dieser Ascomyceten-Gattung in der Heruntergeladen von: University of Illinois. Urheberrechtlich geschützt.

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Über Aktivierungsreaktionen bei Claviceps

Cited by 21 publications

References 12 publications

d-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea

d-lysergic acid-activating enzyme from the ergot fungus Claviceps purpurea

D-Lysergic acid activation and cell-free synthesis of D-lysergyl peptides in an enzyme fraction from the ergot fungus Claviceps purpurea

Biosynthese Des Peptidteils Der Mutterkornalkaloide Vom Cyclol–typ

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