Literature DB >> 7961164

Structural elucidation of aibellin, a new peptide antibiotic with efficiency enhancing activity on rumen fermentation.

S Kumazawa1, M Kanda, H Aoyama, M Utagawa, J Kondo, S Sakamoto, H Ohtani, T Mikawa, I Chiga, T Hayase.   

Abstract

A new peptide antibiotic, aibellin, that had the efficiency enhancing activity on rumen fermentation, was isolated from the culture broth of the fungus, Verticimonosporium ellipticum D1528, and its primary structure was elucidated from spectrometric analysis and chemical degradation. Aibellin is a 20-residue peptaibol, and it has a unique structural feature in the novel C-terminal amino alcohol. Moreover, aibellin is the first peptaibol that possesses two acidic amino acids in the C-terminal region and a Phe residue in the middle of the sequence.

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Year:  1994        PMID: 7961164     DOI: 10.7164/antibiotics.47.1136

Source DB:  PubMed          Journal:  J Antibiot (Tokyo)        ISSN: 0021-8820            Impact factor:   2.649


  2 in total

1.  Diversity of monomers in nonribosomal peptides: towards the prediction of origin and biological activity.

Authors:  Ségolène Caboche; Valérie Leclère; Maude Pupin; Gregory Kucherov; Philippe Jacques
Journal:  J Bacteriol       Date:  2010-08-06       Impact factor: 3.490

2.  Total synthesis of Septocylindrin B and C-terminus modified analogues.

Authors:  Jo Nelissen; Koen Nuyts; Marta De Zotti; Rob Lavigne; Chris Lamberigts; Wim M De Borggraeve
Journal:  PLoS One       Date:  2012-12-20       Impact factor: 3.240

  2 in total

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