نتایج جستجو برای: lipopeptides

تعداد نتایج: 737  

2013
Wen Li Hassan Rokni-Zadeh Matthias De Vleeschouwer Maarten G. K. Ghequire Davy Sinnaeve Guan-Lin Xie Jef Rozenski Annemieke Madder José C. Martins René De Mot

The rhizosphere isolate Pseudomonas putida BW11M1 produces a mixture of cyclic lipopeptide congeners, designated xantholysins. Properties of the major compound xantholysin A, shared with several other Pseudomonas lipopeptides, include antifungal activity and toxicity to Gram-positive bacteria, a supportive role in biofilm formation, and facilitation of surface colonization through swarming. Aty...

2002
Manabu Morita Ken-Ichiro Shibata Takeshi Into Mari Fujita Tsugumi Okusawa Akira Hasebe

Journal: :Chemical communications 2007
Amanda Powell Majid Al Nakeeb Barrie Wilkinson Jason Micklefield

Precursor-directed biosynthesis of calcium dependent antibiotics (CDAs) with modified 3-trifluoromethyl and 3-ethyl glutamate residues was achieved by feeding synthetic glutamate analogues to a mutant strain of Streptomyces coelicolor impaired in the biosynthesis of the natural precursor (2S,3R)-3-methyl glutamic acid.

2013
Huijun Wu Junqing Qiao Jochen Blom Christian Rueckert Oleg Reva Xuewen Gao Rainer Borriss

The genome of rhizobacterium Bacillus amyloliquefaciens subsp. plantarum strain NAU-B3 is 4,196,170 bp in size and harbors 4,001 genes. Nine giant gene clusters are dedicated to the nonribosomal synthesis of antimicrobial lipopeptides and polyketides. Remarkably, NAU_B3 contains a large inversion within the central portion of the genome.

Journal: :Journal of bacteriology 2012
Kun Hao Pengfei He Jochen Blom Christian Rueckert Zichao Mao Yixin Wu Yueqiu He Rainer Borriss

The genome of rhizobacterium Bacillus amyloliquefaciens subsp. plantarum YAU B9601-Y2 was 4.24 Mb in size and harbored 3,991 coding sequences (CDS). Giant gene clusters were dedicated to nonribosomal synthesis of antimicrobial lipopeptides and polyketides. Remarkably, CAU B946 possessed a gene cluster involved in synthesis of mersacidin.

Journal: :The Journal of Cell Biology 1996
H Schroeder R Leventis S Shahinian P A Walton J R Silvius

A variety of cysteine-containing, lipid-modified peptides are found to be S-acylated by cultured mammalian cells. The acylation reaction is highly specific for cysteinyl over serinyl residues and for lipid-modified peptides over hydrophilic peptides. The S-acylation process appears by various criteria to be enzymatic and resembles the S-acylation of plasma membrane-associated proteins in variou...

Journal: :International Journal of Organic Chemistry 2012

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