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Hatano K,
Nishii T,
Kasai H,
( 2003 ) Taxonomic re-evaluation of whorl-forming Streptomyces (formerly Streptoverticillium) species by using phenotypes, DNA-DNA hybridization and sequences of gyrB, and proposal of Streptomyces luteireticuli (ex Katoh and Arai 1957) corrig., sp. nov., nom. rev. PMID : 13130042 : DOI : 10.1099/ijs.0.02238-0 DOI : 10.1099/ijs.0.02238-0 Abstract >>
The taxonomic status of 64 strains of whorl-forming Streptomyces (formerly Streptoverticillium) species was re-evaluated and strains were reclassified on the basis of their phenotypes, DNA-DNA hybridization data and partial sequences of gyrB, the structural gene of the B subunit of DNA gyrase. These strains, which consisted of 46 species and eight subspecies with validly published names and 13 species whose names have not been validly published [including 10 strains examined by the International Streptomyces Project (ISP)], were divided into two groups, namely typical and atypical whorl-forming Streptomyces species, based on their phenotypes and gyrB gene sequences. The typical whorl-forming species (59 strains) were divided into six major clusters of three or more species, seven minor clusters of two species and five single-member clusters, based on the threshold value of 97 % gyrB sequence similarity. Major clusters were typified by Streptomyces abikoensis, Streptomyces cinnamoneus, Streptomyces distallicus, Streptomyces griseocarneus, Streptomyces hiroshimensis and Streptomyces netropsis. Phenotypically, members of each cluster resembled each other closely except for the S. distallicus cluster, which was divided phenotypically into the S. distallicus and Streptomyces stramineus subclusters, and the S. netropsis cluster, which was divided into the S. netropsis and Streptomyces eurocidicus subclusters. Strains in each minor cluster closely resembled each other phenotypically. DNA-DNA relatedness between the representative species and others in each major cluster and/or subcluster, and between strains in the minor clusters, was >70 %, indicating that the major clusters and/or subclusters and the minor clusters each comprise a single species. It was concluded that 59 strains of typical whorl-forming Streptomyces species consisted of the following 18 species, including subjective synonym(s): S. abikoensis, Streptomyces ardus, Streptomyces blastmyceticus, S. cinnamoneus, S. eurocidicus, S. griseocarneus, S. hiroshimensis, Streptomyces lilacinus, 'Streptomyces luteoreticuli', Streptomyces luteosporeus, Streptomyces mashuensis, Streptomyces mobaraensis, Streptomyces morookaense, S. netropsis, Streptomyces orinoci, S. stramineus, Streptomyces thioluteus and Streptomyces viridiflavus.
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Fredenhagen A,
Fendrich G,
Märki F,
Märki W,
Gruner J,
Raschdorf F,
Peter HH,
( 1990 ) Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin. PMID : 2125590 : DOI : 10.7164/antibiotics.43.1403 Abstract >>
Duramycins B and C, two new lanthionine containing antibiotics, have been isolated from Streptoverticillium strain R2075 and Streptomyces griseoluteus (R2107). The known antibiotics duramycin and cinnamycin were reisolated from Streptoverticillium hachijoense (DSM 40114) and Streptomyces longisporoflavus (DSM 40165). The structures of these latter two compounds should be revised by changing amino acid residue 3 to glutamine and 17 to asparagine, respectively. Cinnamycin therefore seems to be identical to Ro 09-0198. Leucopeptin has been shown to be identical to duramycin. Physico-chemical data of these compounds provide evidence for a similar structure for all duramycin antibiotics. All compounds of this group inhibit human phospholipase A2 at a concentration of 10(-6) molar.
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Kaletta C,
Entian KD,
Jung G,
( 1991 ) Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic. PMID : 2070795 : DOI : 10.1111/j.1432-1033.1991.tb16138.x Abstract >>
The tetracyclic polypeptide antibiotic cinnamycin (Ro 90-0198) belongs to the duramycin-type lantibiotics and contains the unusual amino acids threo-3-methyl-lanthionine, meso-lanthionine, lysinoalanine and 3-hydroxyaspartic acid. Its structural gene, referred to as cinA, has been identified on isolated chromosomal DNA of the Ro 09-0198-producing strain Streptoverticillium griseoverticillatum via a 39-residue oligonucleotide probe derived from fragment 7-19 of the hypothetical prolantibiotic sequence CRQSCSFGPFTFVCDGNTK. This propeptide part was then found within an open reading frame of 77 amino acids. In contrast to the nisin-type prelantibiotics, this first duramycin-type prelantibiotic has an unusually long leader sequence of 58 amino acids. it also differs in the processing site and the direction of the formation of the threo-3-methyl-lanthionine bridges is from N-terminal cysteine to C-terminal dehydrated threonine residues, whereas the meso-lanthionine and lysinoalanine bridges are formed by addition reactions from C-terminal cysteine or lysine to N-terminal dehyrated serine residues.
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Naruse N,
Tenmyo O,
Tomita K,
Konishi M,
Miyaki T,
Kawaguchi H,
Fukase K,
Wakamiya T,
Shiba T,
( 1989 ) Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin. PMID : 2544544 : DOI : 10.7164/antibiotics.42.837 Abstract >>
A strain of Streptoverticillium cinnamoneum produced a peptide antibiotic named lanthiopeptin, which contained four unusual amino acids, erythro-beta-hydroxyaspartic acid, mesolanthionine, threo-beta-methyllanthionine and lysinoalanine. Lanthiopeptin showed antiviral activity against herpes simplex virus type 1 KOS strain infection in Vero cells by cytopathic effect reduction assay. The structure of lanthiopeptin is similar to that of ancovenin.
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Itazaki H,
Kawamura Y,
Matsumoto K,
Nagashima K,
( 1990 ) The structure of PA48009: the revised structure of duramycin. PMID : 2272918 : DOI : 10.7164/antibiotics.43.1421 Abstract >>
PA48009, a lanthionine-containing peptide antibiotic was isolated from the culture broth of Streptoverticillium griseoverticillatum PA-48009, and identified as duramycin. Determination of the structure using both Edman degradations and 2D NMR spectroscopy showed the need to revise the structure of duramycin given in literature. Duramycin (PA48009) was different from lanthiopeptin (Ro 09-0198, cinnamycin) only by a Lys/Arg exchange at position 2.
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