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Autor:
Elena B. Tikhonova, Lan Guan, Aaron C. Scarpa, Parameswaran Hariharan, Kelsey J. Markham, Satoshi Katsube
Publikováno v:
The Journal of Biological Chemistry
The melibiose permease of Salmonella typhimurium (MelBSt) catalyzes the stoichiometric symport of galactopyranoside with a cation (H+, Li+, or Na+) and is a prototype for Na+-coupled major facilitator superfamily (MFS) transporters presenting from ba
Autor:
Brianne E. Lewis, Timothy L. Stemmler, José M. Argüello, Christopher M. Sassetti, Subhalaxmi Nambi, Sarju J. Patel, Jarukit E. Long
Publikováno v:
Journal of Biological Chemistry. 291:11529-11539
Little is known about iron efflux transporters within bacterial systems. Recently, the participation of Bacillus subtilis PfeT, a P1B4-ATPase, in cytoplasmic Fe(2+) efflux has been proposed. We report here the distinct roles of mycobacterial P1B4-ATP
Autor:
Akimasa Miyanaga, Yohei Katsuyama, Nobutaka Funa, Yasuo Ohnishi, Ken-ichi Miyazono, Sueharu Horinouchi, Masaru Tanokura, Ryutaro Satou, Hiroki Ozawa
Publikováno v:
Journal of Biological Chemistry. 288:34146-34157
Type III polyketide synthases (PKSs) show diverse cyclization specificity. We previously characterized two Azotobacter type III PKSs (ArsB and ArsC) with different cyclization specificity. ArsB and ArsC, which share a high sequence identity (71%), pr
Autor:
Rebecca J. Harrison, Daniel Bur, David Wyatt, Timothy John Winterburn, Lowri H. Phylip, Colin Berry, John Kay
Publikováno v:
Journal of Biological Chemistry. 282:6508-6516
The 68-residue IA(3) polypeptide from Saccharomyces cerevisiae is essentially unstructured. It inhibits its target aspartic proteinase through an unprecedented mechanism whereby residues 2-32 of the polypeptide adopt an amphipathic alpha-helical conf
Autor:
Shigeyuki Yokoyama, Ryuya Fukunaga
Publikováno v:
Journal of Biological Chemistry. 280:29937-29945
The editing domain of valyl-tRNA synthetase (ValRS) is known to deacylate, or edit, misformed Thr-tRNA(Val) (post-transfer editing). Here, we determined the 1.7-Angstroms resolution crystal structure of the Thermus thermophilus ValRS editing domain.
Autor:
Jozef Van Beeumen, Carine Bebrone, Bart Devreese, Christine Anne, Moreno Galleni, Jean-Marie Frère, Gian Maria Rossolini, Kris De Vriendt
Publikováno v:
Journal of Biological Chemistry. 280:28195-28202
Among class B beta-lactamases, the subclass B2 CphA enzyme is characterized by a unique specificity profile. CphA efficiently hydrolyzes only carbapenems. In this work, we generated site-directed mutants that possess a strongly broadened activity spe
Autor:
Frank Bosmans, Yu Mei Xiong, Yan Mei Sun, Jan Tytgat, Da-Cheng Wang, Rong Huan Zhu, Cyril Goudet
Publikováno v:
Journal of Biological Chemistry. 278:24125-24131
About one-third of the amino acid residues conserved in all scorpion long chain Na+ channel toxins are aromatic residues, some of which constitute the so-called "conserved hydrophobic surface." At present, in-depth structure-function studies of these
Publikováno v:
Journal of Biological Chemistry. 277:46110-46115
Chloride-dependent alpha-amylases constitute a well conserved family of enzymes thereby allowing investigation of the characteristics of each member to understand, for example, relevant properties required for environmental adaptation. In this contex
Autor:
David O. Wood, D. Eric Walters, Ronald S. Kaplan, David A. Gremse, David Kakhniashvili, June A. Mayor, Yan Xu
Publikováno v:
Journal of Biological Chemistry. 275:7117-7124
Utilizing site-directed mutagenesis in combination with chemical modification of mutated residues, we have studied the roles of cysteine and arginine residues in the mitochondrial citrate transport protein (CTP) from Saccharomyces cerevisiae. Our str
Publikováno v:
Journal of Biological Chemistry. 273:22311-22316
In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelat