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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
Publikováno v:
J Biol Chem
The Journal of biological chemistry, vol 295, iss 19
The Journal of biological chemistry, vol 295, iss 19
The atypical trichromatic cyanobacterial phytochrome NpTP1 from Nostoc punctiforme ATCC 29133 is a linear tetrapyrrole (bilin)-binding photoreceptor protein that possesses tandem-cysteine residues responsible for shifting its light-sensing maximum to
Autor:
Taeho Kim, Kayla Nemr, Alexander F. Yakunin, Peter J. Stogios, Radhakrishnan Mahadevan, Tatiana Skarina, Anna N. Khusnutdinova, Jeong Chan Joo, Robert Flick, Alexei Savchenko
Publikováno v:
Journal of Biological Chemistry. 295:597-609
Carbon–carbon bond formation is one of the most important reactions in biocatalysis and organic chemistry. In nature, aldolases catalyze the reversible stereoselective aldol addition between two carbonyl compounds, making them attractive catalysts
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