Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Henk Van Liempt"'
Publikováno v:
Biotechnology: Products of Secondary Metabolism, Volume 7, Second Edition
Autor:
Hans-Jochen Schaefer, Maja Pavela-Vrančić, Horst Kleinkauf, Eva Pfeifer, Hans von Doehren, Henk van Liempt
Publikováno v:
Biochemistry. 33:6276-6283
Characterization of the nucleotide binding domain in peptide synthetases was approached by photoaffinity labeling of tyrocidine synthetase 1 (TY1) with 2-azidoadenosine triphosphate (2-azido-ATP). Exposure of TY1 in the presence of photolabel to irra
Autor:
Henk van Liempt, Horst Kleinkauf, H. Palissa, Torsten Schwecke, Hans von Döhren, Yair Aharonowitz
Publikováno v:
European Journal of Biochemistry. 205:687-694
delta-(L-alpha-Aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase, the multienzyme catalyzing the formation of ACV from the constituent amino acids and ATP in the presence of Mg2+ and dithioerythritol, was purified about 2700-fold from Streptomyces c
Publikováno v:
FEBS letters. 357(2)
Peptide synthetases and acyl-CoA-synthetases form acyl adenylates which are transferred to CoA or enzyme-bound pantetheine. To verify the existence of an adenylate domain in peptide synthetases, a 60.8 kDa fragment of tyrocidine 1-synthetase was cons
Publikováno v:
European journal of biochemistry. 220(2)
Peptide synthetases consist of linearly arranged catalytic units, which by sequence alignment show equally spaced amino-acid-activating segments/modules of 600–700 amino acid residues. The consensus sequence comprises a new class of sequence motifs
Autor:
Yair Aharonowitz, Jürgen Bergmeyer, Jesus M. Cantoral, Gerald Cohen, Arnold L. Demain, Uwe Fink, Jim Kinghorn, Horst Kleinkauf, Andrew MacCabe, Harriet Palissa, Eva Pfeifer, Torsten Schwecke, Henk van Liempt, Hans von Döhren, Saul Wolfe, Jinyou Zhang
Publikováno v:
Bio/technology (Nature Publishing Company). 11(7)
ACV synthetase forms the tripeptide precursor of penicillins and cephalosporins from alpha-aminoadipate, cysteine, and valine. Catalytic sites for substrate carboxyl activation as adenylates, peptide bond formations, epimerization and release of the