Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Kleinkauf, Horst

doi:10.1055/s-0028-1097178

Cited by 30 publications

(8 citation statements)

References 21 publications

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“…i> Lysergic acid seems to be a free intermediate in the process of lysergyl-peptide formation, so an enzyme must be present in the cells of C. purpurea catalysing the activation of D-lysergic acid before peptide-bond formation. Such an activation is likely to proceed via adenylate formation, as has been described for numerous non-ribosomally formed peptides (Kleinkauf, 1979). In the present paper we describe the purification and characterization of a D-lysergic acid-activating enzyme from Claviceps purpureoa strain 1029.…”

mentioning

confidence: 58%

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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mentioning

confidence: 58%

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

Keller¹,

Zocher²,

Krengel³

et al. 1984

Biochemical Journal

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“…(, ) in Fusarium proliferatum . BEA and ENs share the same biosynthetic pathway (Kleinkauf ; Peeters et al . ) and vary in amino acid moiety and their aliphatic chain lengths.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional regulation of enniatins production by Fusarium avenaceum

et al. 2013

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Aims: The aim of this study was to analyse the transcriptional regulation of enniatins (ENs) production in Fusarium avenaceum. Methods and Results: We develop a new method to quantify ENs in FDM agar medium. We performed an LC/MS/MS analysis to evaluate enniatin A, A1, B, B1 and B4 production by seven F. avenaceum strains and, in a timecourse experiment, by ITEM 3404 to analyse the transcriptional regulation of the esyn1 gene. The expression profile, achieved by Real time reverse transcriptase assay, showed an activation of gene transcription at the seventh day of incubation, corresponding to the higher increase of total ENs production. Enniatin B was the most abundant ENs analogues, representing the 90% of total ENs. The relative percentage of ENs remained unaltered during the experiment. Conclusions: We reported a transcriptional regulation of esyn1 responsible for the modulation of ENs biosynthesis. Significance and Impact of the Study: Enniatins are cyclic depsipeptides metabolites with a wide range of biological activities. They are also widespread contaminants in grains and cereals due to infection by enniatin-producing Fusarium species. This is the first article describing the transcriptional regulation of esyn1 gene that modulates ENs production in Fusarium avenaceum and provides new knowledge about the molecular mechanism underlying the biosynthesis of these important fungal metabolites in this toxigenic fungal species.

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“…In gramicidin Sand tyrocidine synthesis, the constituent amino acids are first activated as aminoacyl adenylates by the respective subunit of the multienzyme synthetases followed by the transfer of the aminoacyl groups to thiols of the same subunit proteins to form thioesters. In recent years a number of reviews of the biogenesis of small peptides or antibiotic peptides have appeared (ASSELINEAU and ZALTA, 1973;FR0YSHOV etaI., 1978;JOHNE and GROGER, 1977;KATZ and DEMAIN, 1977;KLEINKAUF, 1979;KLEINKAUF and KOISCHWITZ, 1978;KURAHASHI, 1974;MAIER and GROGER, 1972;PERLMAN and BODANSZKY, 1971). The specificity and sequence of the amino acids in the peptide antibiotics are determined by the substrate specificity and the spatial arrangement of the thiols on the subunits of the synthetases.…”

Section: Biosynthesis Of Peptide Antibioticsmentioning

confidence: 99%

Biosynthesis

1981

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Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Cited by 30 publications

References 21 publications

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

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

Transcriptional regulation of enniatins production by Fusarium avenaceum

Biosynthesis

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