Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Siegfried Fittkau"'
Publikováno v:
International Journal of Peptide and Protein Research. 42:560-564
Comparative studies of the hydrolysis of succinyl-Ala2-Phe-methylcoumarylamide with mesentericopeptidase, a mesophilic extracellular serine proteinase from Bacillus mesentericus, and proteinases produced by organisms representing different levels of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25fc173b6b5b02927cf2827055b07634
https://doi.org/10.1111/j.1399-3011.1993.tb00364.x
https://doi.org/10.1111/j.1399-3011.1993.tb00364.x
Publikováno v:
International Journal of Peptide and Protein Research. 23:134-141
The influence of chloromethyl ketones and methyl ketones of N-acylated peptides on the thermal denaturation of thermitase was investigated in the presence and the absence of calcium ions. The chloromethyl ketone derivatives are known to react irrever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8402354a199f1199735bb878e7c7978
https://doi.org/10.1111/j.1399-3011.1984.tb02703.x
https://doi.org/10.1111/j.1399-3011.1984.tb02703.x
Autor:
Christian Betzel, Klaus Peters, Susanne Eschenburg, Michael Degenhardt, Karen M. Moore, Lawrence J. DeLucas, Siegfried Fittkau, Wolfgang Weber
Publikováno v:
Journal of Crystal Growth
Crystals of proteinase K in complex with synthetic substrate analogues have been grown under microgravity on the US space shuttle missions STS-91 and STS-95 using the vapor diffusion apparatus (c-VDA) supplied by the Center for Macromolecular Crystal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::914c55b3a6d17a888a99934c5f9296ea
https://doi.org/10.1016/s0022-0248(99)00392-9
https://doi.org/10.1016/s0022-0248(99)00392-9
Publikováno v:
Protein Science. 5:2453-2458
The crystal structure of a complex formed by the interaction between proteinase K and a designed octapeptide amide, N-Ac-Pro-Ala-Pro-Phe-DAla-Ala-Ala-Ala-NH2, has been determined at 2.5 A resolution and refined to an R-factor of 16.7% for 7,430 refle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2efa5ee780ca960d68f03c4e5d55e8d4
https://doi.org/10.1002/pro.5560051207
https://doi.org/10.1002/pro.5560051207
Autor:
Christian Betzel, Keith S. Wilson, Siegfried Fittkau, Tej P. Singh, Marcia Visanji, Klaus Peters, Ajay K. Saxena
Publikováno v:
Proteins: Structure, Function, and Genetics. 25:195-201
The crystal structure of a ternary complex of proteinase K, Hg(II) and a hexapeptide N-Ac-Pro-Ala-Pro-Phe-Pro-Ala-NH2 has been determined at 2.2 A resolution and refined to an R factor of 0.172 for 12,910 reflections. The mercury atom occupies two al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46c95bdab000eb67f00568b598d69fe9
https://doi.org/10.1002/(sici)1097-0134(199606)25:2<195::aid-prot5>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199606)25:2<195::aid-prot5>3.0.co
Autor:
A. Stöckel, Heidrun Kirschke, Dieter Brömme, Angelika Schierhorn, Siegfried Fittkau, Hans-Ulrich Demuth
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1202:265-270
10 N-aminoacyl-O-4-nitrobenzoyl hydroxamates were investigated as potential inhibitors of aminopeptidases. While the metal-depending enzymes aminopeptidase M. aminopeptidase P and leucine aminopeptidase were inhibited reversibly by the compounds, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23d772dcc444d95381f35381609d51c5
https://doi.org/10.1016/0167-4838(93)90014-i
https://doi.org/10.1016/0167-4838(93)90014-i
Autor:
Wolfram Saenger, Tej Singh, Klaus Peters, Keith S. Wilson, Marcia Visanji, Ch. Betzel, Siegfried Fittkau
Publikováno v:
Journal of Biological Chemistry. 268:15854-15858
The crystal structure of a transition state/product complex formed by the interaction between proteinase K and the substrate analogue N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution of 2.2 A and refined to an R-factor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::939ed5781c85f73a84a5c43c1ea26a32
https://doi.org/10.1016/s0021-9258(18)82332-8
https://doi.org/10.1016/s0021-9258(18)82332-8
Publikováno v:
Journal of Enzyme Inhibition. 4:35-42
Peptide diazomethyl ketones, well known as specific cysteine protease inhibitors are also potent inhibitors of the microbial serine proteases thermitase (EC 3.4.21.14) and subtilisin Carlsberg (EC 3.4.21.14). The affinity of the enzymes towards the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e7a6ab7859af6785955911dc646a12
https://doi.org/10.3109/14756369009030386
https://doi.org/10.3109/14756369009030386
Autor:
Susanne Eschenburg, Keith S. Wilson, Christian Betzel, Nicolay Genov, Klaus Peters, Stanka Stoeva, Siegfried Fittkau
Publikováno v:
European journal of biochemistry. 257(2)
The crystal structure of subtilisin DY inhibited by N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R facto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3fb47818e2c37b025dc6ca7b0b974cf
https://pubmed.ncbi.nlm.nih.gov/9826175
https://pubmed.ncbi.nlm.nih.gov/9826175
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9780306451089
In the last 12 years more than 80 peptidyl substrates and substrate analogous inhibitors were synthesized in our group and used to characterize thermitase, a serine proteinase of the subtilisin family produced by Thermoactinomyces vulgaris. The kinet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e51ab17fb3974c5f7bbc369d6104106
https://doi.org/10.1007/978-1-4613-0319-0_14
https://doi.org/10.1007/978-1-4613-0319-0_14
