Results 61 to 70 of about 3,915,254 (313)

Elucidation of interface interactions between a dehydratase domain and an acyl carrier protein in cremimycin polyketide synthase

FEBS Letters, EarlyView.
In modular polyketide synthases, the dehydratase (DH) domain catalyzes the dehydration reaction of the β‐hydroxyacyl unit attached to the cognate acyl carrier protein (ACP) domain. However, it is unclear how DH interacts with ACP during the reaction. In this study, we identified DH–ACP interface residues, providing the first detailed insights into DH ...
Kaede Kotagiri, Haruka Tachibana, Daisuke Kawasaki, Taichi Chisuga, Toma Kashima, Shinya Fushinobu, Fumitaka Kudo, Tadashi Eguchi, Akimasa Miyanaga   +8 more
wiley   +1 more source

Secondary Metabolites of Fomitopsis betulina: Chemical Structures, Biological Activity and Application Prospects

Journal of Fungi
Fomitopsis betulina, as a macrofungus with both medicinal and dietary applications, is renowned for its rich content of bioactive substances. The recent advancements in research have significantly enhanced our understanding of its polysaccharides ...
Jianghao Li, Ziheng Li, Yingce Duan, Chengwei Liu, Meixia Yan   +4 more
doaj   +1 more source

Rapid generation of recombinant Pseudomonas putida secondary metabolite producers using yTREX

Synthetic and Systems Biotechnology, 2017
Microbial secondary metabolites represent a rich source of valuable compounds with a variety of applications in medicine or agriculture. Effective exploitation of this wealth of chemicals requires the functional expression of the respective biosynthetic ...
Andreas Domröse, Robin Weihmann, Stephan Thies, Karl-Erich Jaeger, Thomas Drepper, Anita Loeschcke   +5 more
doaj   +1 more source

The iSplit GFP assay detects intracellular recombinant proteins in Bacillus subtilis

Microbial Cell Factories, 2021
Background Bacillus subtilis is one of the most important microorganisms for recombinant protein production. It possesses the GRAS (generally recognized as safe) status and a potent protein secretion capacity.
Patrick Lenz, Fabienne Hilgers, Alina Burmeister, Leonie Zimmermann, Kristina Volkenborn, Alexander Grünberger, Dietrich Kohlheyer, Thomas Drepper, Karl-Erich Jaeger, Andreas Knapp   +9 more
doaj   +1 more source

The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry [PDF]

, 2011
In protein film electrochemistry a redox protein of interest is studied as an electroactive film adsorbed on an electrode surface. For redox enzymes this configuration allows quantification of the relationship between catalytic activity and ...
Ackrell, Anderson, Anderson, Andrew G. Mayes, Andrew J. Gates, Angove, Armstrong, Armstrong, Armstrong, Armstrong, Armstrong, Arnoux, Bamford, Bekker, Berks, Blumberger, Blumberger, Buc, Butler, Butler, Chun Yip To, Clarke, Costa, David J. Richardson, Davis, de Vries, Dementin, Dias, Dridge, Eddowes, Ellington, Elliott, Field, Flores, Fourmond, Fourmond, Fourmond, Frangioni, Frew, Gates, Gates, Gemma L. Kemp, Georgellis, Gwyer, Hagedoorn, Hanson, Healy, Heering, Hirst, Hofmann, Hunte, Immoos, Ivanov, James Mann, Jepson, Jepson, Jeuken, Julea N. Butt, Kell, Kemp, Lin, Léger, Léger, Léger, Marritt, Marsili, Moore, Murgida, Niki, Otten, Otten, Page, Pershad, Potter, Ramirez, Richardson, Ridnour, Sears, Sears, Simons, Sophie J. Marritt, Sun, Tenderholt, Tenderholt, Thauer, Tipmanee, Wang, Westerhoff, Yeh, Zuman   +89 more
core   +1 more source

Clustering and optimal arrangement of enzymes in reaction-diffusion systems [PDF]

Phys. Rev. Lett. 110, 208104 (2013), 2013
Enzymes within biochemical pathways are often colocalized, yet the consequences of specific spatial enzyme arrangements remain poorly understood. We study the impact of enzyme arrangement on reaction efficiency within a reaction-diffusion model. The optimal arrangement transitions from a cluster to a distributed profile as a single parameter, which ...
arxiv   +1 more source

Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions

FEBS Letters, EarlyView.
This study addresses the inhibition of lytic polysaccharide monooxygenases (LPMOs) by cyanide and explains how and why the magnitude of observed inhibitory effects depends on the way LPMO reactions are setup and on the type of LPMO. Enzymes known as lytic polysaccharide monooxygenases (LPMOs) are mono‐copper polysaccharide‐degrading peroxygenases that ...
Ole Golten, Lorenz Schwaiger, Zarah Forsberg, Kelsi R. Hall, Anton A. Stepnov, Tom Z. Emrich‐Mills, Iván Ayuso‐Fernández, Morten Sørlie, Roland Ludwig, Åsmund Kjendseth Røhr, Vincent G. H. Eijsink   +10 more
wiley   +1 more source

GhWRKY1-like, a WRKY transcription factor, mediates drought tolerance in Arabidopsis via modulating ABA biosynthesis

BMC Plant Biology, 2021
Background Drought stress has great negative effects on the plant growth and development. The tolerance of plants to such abiotic stress is triggered by complicated and multilayered signaling pathways to restore cellular homeostasis and to promote ...
Qin Hu, Chuanwei Ao, Xiaorui Wang, Yanfei Wu, Xuezhu Du   +4 more
doaj   +1 more source

The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: interactions at ferrous heme and cysteine thiols [PDF]

, 2009
It has been previously proposed that nitric oxide (NO) is the only biologically relevant nitrogen oxide capable of activating the enzyme soluble guanylate cyclase (sGC). However, recent reports implicate HNO as another possible activator of sGC.
Adrian J. Hobbs, Anderegg, Andrea J. Lee, Bari, Bartberger, Bermejo, Bonner, Brandwein, Burstyn, Craven, Craven, De Witt, DeMaster, Denninger, Derbyshire, DeRubertis, Dierks, Doyle, Drago, Dutton, Dutton, Ellis, Ellis, Farmer, Favaloro, Feelisch, Fukuto, Fukuto, Haddox, Halliwell, Hobbs, Hoshino, Ignarro, Ignarro, Ignarro, Ignarro, Immoos, Irvine, Irvine, Jon M. Fukuto, Judith N. Burstyn, Kamisaki, Katrina M. Miranda, Kim, Lin, Lopez, Maragos, Melisa M. Cherney, Miranda, Miranda, Miranda, Nestor E. Francoleon, Niederhoffer, Paolocci, Paolocci, Patrick J. Farmer, Pervitsky, Pino, Poulos, Rusche, S. Bruce King, Sayed, Scheidt, Schmidt, Serfass, Sha, Shafirovich, Shahidullah, Shen, Smith, Stasch, Stone, Stone, Sulc, Sulc, Thadani, Thomas W. Miller, Turk, Väänänen, Väänänen, Wanstall, Wayland, Wayland, Wolin, Wong, Yonetani   +85 more
core   +2 more sources

Characteristics of the Kelch domain containing (KLHDC) subfamily and relationships with diseases

FEBS Letters, EarlyView.
The Kelch protein superfamily includes 63 members, with the KLHDC subfamily having 10 proteins. While their functions are not fully understood, recent advances in KLHDC2's structure and role in protein degradation have highlighted its potential for drug development, especially in PROTAC therapies.
Courtney Pilcher, Paula Armina V. Buco, Jia Q. Truong, Paul A. Ramsland, Monique F. Smeets, Carl R. Walkley, Jessica K. Holien   +6 more
wiley   +1 more source