نتایج جستجو برای: syringomycin

تعداد نتایج: 93  

Journal: :Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology 2009

Journal: :Chemistry & biology 2005
Carl J Balibar Frédéric H Vaillancourt Christopher T Walsh

The first 6 residues of the biosurfactant lipopeptidolactone arthrofactin have the D configuration, yet none of the 11 modules of the nonribosomal peptide synthetase assembly line have epimerization domains. We show that the two-module ArfA subunit and the first module of the ArfB subunit, which act in tandem to produce the N-acyl-D-Leu1-D-Asp2-D-Thr3-S-protein intermediate, activate the L amin...

Journal: :Chemistry & biology 2007
Gitanjali M Singh Frédéric H Vaillancourt Jun Yin Christopher T Walsh

Syringomycin, a lipopeptidolactone assembled from nine amino acid monomers by four enzymes, SyrB1, SyrB2, SyrC, and SyrE, is a cyclic nonribosomal peptide made by plant-associated Pseudomonas spp. This assembly is unusual because the terminal residue, 4-chlorothreonine, has been proposed to be added in trans since the ninth module of the megasynthetase SyrE lacks an adenylation domain required ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1988
M Abdel-Ghany D Raden E Racker E Katchalski-Katzir

A synthetic random polymer of threonine and glutamate (1:4.4) is readily phosphorylated by protein kinase P but not by five other protein-serine (threonine) kinases. A synthetic random polymer of serine and arginine (1:3) is readily phosphorylated by protein kinase A and protein kinase C but not by protein kinase P. Although the amino acid sequences surrounding the phosphorylated serine (threon...

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