Zobrazeno 1 - 5
of 5
pro vyhledávání: '"W S Willett"'
Publikováno v:
Biochemistry. 35:5999-6009
The three-dimensional structures of complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d79e0c374e1e231e32a41c201ffc842
https://doi.org/10.1021/bi9530200
https://doi.org/10.1021/bi9530200
Publikováno v:
Biochemistry. 35(19)
Recognition for proteolysis by trypsin depends almost exclusively on tight binding of arginine or lysine side chains by the primary substrate specificity pocket. Although extended subsite interactions are important for catalysis, the majority of bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eac0dfa57905018ce70a5dab140f2c0
https://pubmed.ncbi.nlm.nih.gov/8634240
https://pubmed.ncbi.nlm.nih.gov/8634240
Autor:
D Reilly, Michael A. Baldwin, D Yansura, Darlene Groth, Fred E. Cohen, Robert J. Fletterick, W S Willett, R Vandlen, Ingrid Mehlhorn, D Henner, B Moffat, Johannes Stöckel, Stanley B. Prusiner
Publikováno v:
Biochemistry. 35(17)
The major, and possible only, component of the infectious prion is the scrapie prion protein (PrPSc); the protease resistant core of PrPSc is PrP 27-30, a protein of approximately 142 amino acids. PrPSc is derived from the cellular PrP isoform (PrPC)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7fa67d91b2bb1e8b41718c02fffba61
https://pubmed.ncbi.nlm.nih.gov/8611544
https://pubmed.ncbi.nlm.nih.gov/8611544
Publikováno v:
Biochemistry. 34(36)
Histidine 57 of the catalytic triad of trypsin was replaced with alanine to determine whether the resulting variant would be capable of substrate-assisted catalysis [Carter, P., & Wells, J. A. (1987) Science 237, 394-9]. A 2.5-fold increase in kcat/K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d245416ef80cef2d1c160ba4d9cc4c1
https://pubmed.ncbi.nlm.nih.gov/7547882
https://pubmed.ncbi.nlm.nih.gov/7547882
Publikováno v:
Biochemistry. 34(7)
Histidine substrate specificity has been engineered into trypsin by creating metal binding sites for Ni2+ and Zn2+ ions. The sites bridge the substrate and enzyme on the leaving-group side of the scissile bond. Application of simple steric and geomet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31df28688cfaab734e4c8c1c6000b49e
https://pubmed.ncbi.nlm.nih.gov/7857928
https://pubmed.ncbi.nlm.nih.gov/7857928