Zobrazeno 1 - 10
of 165
pro vyhledávání: ''
Autor:
Carl Frieden, Eliza A. Ruben, Prafull S. Gandhi, Zhiwei Chen, Sarah K. Koester, Gregory T. DeKoster, Enrico Di Cera
Publikováno v:
The Journal of Biological Chemistry
The conformational properties of trypsin-like proteases and their zymogen forms remain controversial because of a lack of sufficient information on their free forms. Specifically, it is unclear whether the free protease is zymogen-like and shifts to
Autor:
Alexander Wlodawer, Mi Li, Poorva Dharkar, Alfred L. Goldberg, Olga Kandror, Tatos Akopian, Michael R. Maurizi
Publikováno v:
Journal of Biological Chemistry. 291:7465-7476
The ClpP protease complex and its regulatory ATPases, ClpC1 and ClpX, in Mycobacterium tuberculosis (Mtb) are essential and, therefore, promising drug targets. The Mtb ClpP protease consists of two heptameric rings, one composed of ClpP1 and the othe
Autor:
Pradeep S. Pallan, Chunxue Wang, Martin Egli, Li Lei, Michael R. Waterman, Richard J. Auchus, F. Peter Guengerich, Francis K. Yoshimoto
Publikováno v:
Journal of Biological Chemistry. 290:13128-13143
Cytochrome P450 (P450) 21A2 is the major steroid 21-hydroxylase, and deficiency of this enzyme is involved in ~ 95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. A structure of the bovine enzyme we previousl
Publikováno v:
Journal of Biological Chemistry. 290:9906-9918
Background: ZPI-protein Z complex is a critical anticoagulant regulator of membrane-associated factor Xa. Results: The energetics and multistep kinetics of the ZPI-protein Z interaction were characterized with fluorescently labeled K239C ZPI. Conclus
Autor:
Natalia Stach, Jan Potempa, Benedykt Wladyka, Marcin Drag, Adam Dubin, Paweł Mak, Anna Czarna, Grzegorz M. Popowicz, Michal Zdzalik, Justyna Stec-Niemczyk, Przemyslaw Cichon, Grzegorz Dubin, Guy S. Salvesen, Katarzyna Pustelny
Publikováno v:
J. Biol. Chem. 289, 15544-15553 (2014)
Staphylococcal SplB protease belongs to the chymotrypsin family. Chymotrypsin zymogen is activated by proteolytic processing at the N terminus, resulting in significant structural rearrangement at the active site. Here, we demonstrate that the molecu
Publikováno v:
Journal of Biological Chemistry. 288:32020-32035
Serpin protein protease inhibitors inactivate their target proteases through a unique mechanism in which a major serpin conformational change, resulting in a 70-A translocation of the protease from its initial reactive center loop docking site to the
Autor:
Kyle Cahill, Ann Heroux, Blaine H. M. Mooers, Matthew West, Yunyu I. Chen, Stephanie Wickham, Marie H. Hanigan
Publikováno v:
Journal of Biological Chemistry. 288:31902-31913
The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds. In animals, GGT1 is expressed on the surface of the c
Autor:
Mark Paetzel, Ivy Yeuk Wah Chung
Publikováno v:
Journal of Biological Chemistry. 288:13068-13081
Yellowtail ascites virus (YAV) is an aquabirnavirus that causes ascites in yellowtail, a fish often used in sushi. Segment A of the YAV genome codes for a polyprotein (pVP2-VP4-VP3), where processing by its own VP4 protease yields the capsid protein
Autor:
Lindsay D. Eltis, Israël Casabon, Natalie C. J. Strynadka, Robert J. Gruninger, Jenna K. Capyk
Publikováno v:
Journal of Biological Chemistry. 286:40717-40724
Mycobacterium tuberculosis (Mtb), a significant global pathogen, contains a cholesterol catabolic pathway. Although the precise role of cholesterol catabolism in Mtb remains unclear, the Rieske monooxygenase in this pathway, 3-ketosteroid 9α-hydroxy
Autor:
Mark Paetzel, Ivy Yeuk Wah Chung
Publikováno v:
Journal of Biological Chemistry. 286:12475-12482
Viruses of the Birnaviridae family are characterized by their bisegmented double-stranded RNA genome that resides within a single-shelled non-enveloped icosahedral particle. They infect birds, aquatic organisms, and insects. Tellina virus 1 (TV-1) is