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Autor:
Naomi Kishine, Yoichi Tsumuraya, Naoki Sunagawa, Kiyohiko Igarashi, Masahiro Samejima, Toshihisa Kotake, Satoshi Kaneko, Kaori Matsuyama, Zui Fujimoto
Publikováno v:
Matsuyama, K, Kishine, N, Fujimoto, Z, Sunagawa, N, Kotake, T, Tsumuraya, Y, Samejima, M, Igarashi, K & Kaneko, S 2020, ' Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-β-1,3-galactanase from Phanerochaete chrysosporium. ', Journal of Biological Chemistry, vol. 295, no. 52, pp. 18539-18552 . https://doi.org/10.1074/jbc.RA120.016149
Arabinogalactan proteins (AGPs) are plant proteoglycans with functions in growth and development. However, these functions are largely unexplored, mainly because of the complexity of the sugar moieties. These carbohydrate sequences are generally anal
Publikováno v:
J Biol Chem
A key step in bacteriochlorophyll biosynthesis is the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide), catalyzed by dark-operative protochlorophyllide oxidoreductase (DPOR). DPOR is made of electron donor (BchL) and acceptor (Bc
Publikováno v:
J Biol Chem
Vitamin B(12) and other cobamides are essential cofactors required by many organisms and are synthesized by a subset of prokaryotes via distinct aerobic and anaerobic routes. The anaerobic biosynthesis of 5,6-dimethylbenzimidazole (DMB), the lower li
Publikováno v:
J Biol Chem
The ATP-grasp superfamily of enzymes shares an atypical nucleotide-binding site known as the ATP-grasp fold. These enzymes are involved in many biological pathways in all domains of life. One ATP-grasp enzyme, d-alanine–d-alanine ligase (Ddl), cata
Autor:
Madison R. Sendzik, Amy C. Rosenzweig, Brian M. Hoffman, Thomas J. Lawton, Oriana S. Fisher, Matthew O. Ross
Publikováno v:
Journal of Biological Chemistry. 294:16351-16363
Copper is critically important for methanotrophic bacteria because their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is copper-dependent. In addition to pMMO, many other copper proteins are encoded in the genomes of methanotro
Autor:
Mériem Merrouch, Catherine L. Drennan, Vincent Fourmond, Elizabeth C. Wittenborn, Steven E. Cohen, Sébastien Dementin, Christophe Léger
Publikováno v:
J Biol Chem
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
The nickel-dependent carbon monoxide dehydrogenase (CODH) employs a unique heterometallic nickel–iron–sulfur cluster, termed the C-cluster, to catalyze the interconversion of CO and CO(2). Like other complex metalloenzymes, CODH requires dedicate
Publikováno v:
J Biol Chem
Small-molecule inhibitors of insect chitinases have potential applications for controlling insect pests. Insect group II chitinase (ChtII) is the most important chitinase in insects and functions throughout all developmental stages. However, the poss
Autor:
Mary M. Leeman, Michael R. Oliver, Rachel A. North, Austin J. Bartl, Müge Kasanmascheff, Renwick C. J. Dobson, Hironori Suzuki, Michael D. W. Griffin, Katherine A. Donovan, André O. Hudson, Jennifer M. Crowther, Penelope J. Cross
Publikováno v:
Crowther, J M, Cross, P J, Oliver, M R, Leeman, M M, Bartl, A J, Weatherhead, A W, North, R A, Donovan, K A, Griffin, M D W, Suzuki, H, Hudson, A O, Kasanmascheff, M & Dobson, R C J 2019, ' Structure–function analyses of two plant meso-diaminopimelate decarboxylase isoforms reveal that active-site gating provides stereochemical control ', Journal of Biological Chemistry, vol. 294, no. 21, pp. 8505-8515 . https://doi.org/10.1074/jbc.RA118.006825
J Biol Chem
J Biol Chem
meso-Diaminopimelate decarboxylase catalyzes the decarboxylation of meso-diaminopimelate, the final reaction in the diaminopimelate l-lysine biosynthetic pathway. It is the only known pyridoxal-5-phosphate–dependent decarboxylase that catalyzes the
Autor:
Kirk A. Vander Meulen, Daniel R. Noguera, Wayne S. Kontur, Daniel L. Gall, Kevin A. Walters, Timothy J. Donohue, Charles N. Olmsted, Steven D. Karlen, Emily T. Beebe, Larissa M. Yusko, Alyssa V. Niles
Publikováno v:
Journal of Biological Chemistry. 294:1877-1890
Lignin is a heterogeneous polymer of aromatic subunits that is a major component of lignocellulosic plant biomass. Understanding how microorganisms deconstruct lignin is important for understanding the global carbon cycle and could aid in developing
Autor:
Jeppe Kari, Trine Holst Sørensen, Kenneth Jensen, Kim Borch, Nanna Sandager Røjel, Peter Westh, Corinna Schiano-di-Cola
Publikováno v:
Schiano-de-Cola, C, Røjel, N, Jensen, K, Kari, J, Sørensen, T H, Borch, K & Westh, P 2019, ' Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungus Trichoderma reesei reveal flexible loops critical for CBH activity ', Journal of Biological Chemistry, vol. 294, no. 6, pp. 1807-1815 . https://doi.org/10.1074/jbc.RA118.006699
Glycoside hydrolase family 7 (GH7) cellulases are some of the most efficient degraders of cellulose, making them particularly relevant for industries seeking to produce renewable fuels from lignocellulosic biomass. The secretome of the cellulolytic m