The Structure of Etamycin

Sheehan, John C.; Zachau, Hans G.; Lawson, William B.

doi:10.1021/ja01571a095

Cited by 54 publications

(10 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…b) and peptidolactone compounds, such as the 4‐MHB‐pentapeptidolactone derivative of actinomycin (Fig. e) as well as the heptapeptide lactone etamycin (Fig. f), are distinguished by such a normal pattern.…”

Section: Resultsmentioning

confidence: 96%

MALDI‐TOF mass spectrometry, an efficient technique for in situ detection and characterization of actinomycins

et al. 2014

View full text Add to dashboard Cite

An extensive study of actinomycins was performed using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS). Actinomycins represent a well-known family of peptidolactone chromopeptides with potent cytostatic and antibiotic properties. Using five well-characterized streptomycete strains, we introduced MALDI-TOF MS as an efficient technique for rapid in situ detection of actinomycins in surface extracts of cells picked from agar plates. By this procedure, actinomycin complexes can be investigated with high sensitivity and accuracy in a minimum of time. These studies were complemented by mass spectrometric investigation of actinomycins obtained from culture filtrate extracts and purified by high-performance liquid chromatography to detect yet unknown actinomycin species. By feeding experiments, C-demethyl-actinomycins from Streptomyces chrysomallus and Streptomyces parvulus as well as hemi-actinomycins from Streptomyces antibioticus lacking one of the two pentapeptide lactone rings were isolated and characterized as novel variants for structure-activity relationship studies. Structural characterization of the investigated actinomycins was performed by post source decay MALDI-TOF MS. The specific features of the fragmentation patterns of the protonated and cationized forms of selected actinomycins were investigated in detail.

show abstract

Section: Resultsmentioning

confidence: 96%

MALDI‐TOF mass spectrometry, an efficient technique for in situ detection and characterization of actinomycins

et al. 2014

View full text Add to dashboard Cite

show abstract

“…Hydroxyproline has been found in prokaryotic cells primarily in peptide antibiotics, such as actinomycin (12), etamycin (29), and telomycin (11); the only exception to this is a hydroxyproline-rich protein that has been found in Staphylococcus aureus (30). Proline 4-hydroxylase activity was found only during biosynthesis of etamycin in S. griseoviridus P-8648 (1,15,24).…”

Section: Discussionmentioning

confidence: 99%

Microbial Proline 4-Hydroxylase Screening and Gene Cloning

Shibasaki

Mori

Chiba

et al. 1999

Appl Environ Microbiol

108

View full text Add to dashboard Cite

Microbial proline 4-hydroxylases, which hydroxylate freel-proline totrans-4-hydroxy-l-proline, were screened in order to establish an industrial system for biotransformation of l-proline totrans-4-hydroxy-l-proline. Enzyme activities were detected in eight strains, including strains ofDactylosporangium spp. and Amycolatopsis spp. The Dactylosporangium sp. strain RH1 enzyme was partially purified 3,300-fold and was estimated to be a monomer polypeptide with an apparent molecular mass of 31 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Degenerate primers based on the N-terminal amino acid sequence of the 31-kDa polypeptide were synthesized in order to amplify the corresponding 71-bp DNA fragment. A 5.5-kbp DNA fragment was isolated by using the 71-bp fragment labeled with digoxigenin as a probe for a genomic library ofDactylosporangium sp. strain RH1 constructed inEscherichia coli. One of the open reading frames found in the cloned DNA, which encoded a 272-amino-acid polypeptide (molecular mass, 29,715 daltons), was thought to be a proline 4-hydroxylase gene. The gene was expressed in E. coli as a fused protein with the N-terminal 34 amino acids of the β-galactosidase α-fragment. The E. coli recombinant exhibited proline 4-hydroxylase activity that was 13.6-fold higher than the activity in the original strain, Dactylosporangium sp. strain RH1. No homology was detected with other 2-oxoglutarate-dependent dioxygenases when databases were searched; however, the histidine motif conserved in 2-oxoglutarate-dependent dioxygenases was found in the gene.

show abstract

“…As a free amino acid, sarcosine has been demonstrated in the radial caeca of the starfish Astropecten aurantiacus (Kossel & Edlbacher, 1915), in the muscles of Elasmobranchii (Tarr, 1958) and in the reindeer moss, Cladonia itlvatica (Linko, Alfthan, Miettinen & Virtanen, 1953). Sarcosine has been found bound in peptides in the antibiotics of the actinomycin (Dalgliesh, Johnson, Todd & Vining, 1950) and etamycin (Sheehan, Zachau & Lawson, 1957) groups. The reported presence of sarcosine in the hydrolysate of groundnut protein (Haworth, MaeGillivray & Peacock, 1951) has recently been questioned (Greenstein & Winitz, 1961).…”

mentioning

confidence: 99%