Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Renata A.G. Reis"'
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 1108-1118 (2021)
Effective use of plant biomass as an abundant and renewable feedstock for biofuel production and biorefinery requires efficient enzymatic mobilization of cell wall polymers. Knowledge of plant cell wall composition and architecture has been exploited
Externí odkaz:
https://doaj.org/article/9c9d4e72b57e45d198302fa77628d693
Publikováno v:
Archives of biochemistry and biophysics. 715
d-Arginine dehydrogenase from Pseudomonas aeruginosa (PaDADH) catalyzes the flavin-dependent oxidation of d-arginine and other d-amino acids. Here, we report the crystal structure at 1.29 Å resolution for PaDADH-Y249F expressed and co-crystallized w
Publikováno v:
Biochemistry. 58:2594-2607
PA0660 from Pseudomonas aeruginosa PAO1 is currently classified as a hypothetical nitronate monooxygenase (NMO), but no evidence at the transcript or protein level has been presented. In this study, PA0660 was purified and its biochemical and kinetic
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1108-1118 (2021)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
Graphical abstract
Highlights • A left-handed triangular prism beta-solenoid scaffold (BeSS) was designed, built and validated. • Vertex inserts in BeSS-CBM3-GH11 xylanase chimeras varies interdomain distance and orientation. • A library o
Highlights • A left-handed triangular prism beta-solenoid scaffold (BeSS) was designed, built and validated. • Vertex inserts in BeSS-CBM3-GH11 xylanase chimeras varies interdomain distance and orientation. • A library o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b08ecf17dd95f7957858d966687992
Autor:
Donald Hamelberg, Irene T. Weber, Giovanni Gadda, Siming Wang, Mohamed Momin, Samer Gozem, Markus W. Germann, Swathi Gannavaram, Johnson Agniswamy, Alexander M. Spring-Connell, Yoelvis Orozco-Gonzalez, Archana Iyer, Renata A.G. Reis
Publikováno v:
Biochemistry. 60(9)
Proteins are inherently dynamic, and proper enzyme function relies on conformational flexibility. In this study, we demonstrated how an active site residue changes an enzyme's reactivity by modulating fluctuations between conformational states. Repla
Autor:
Crystal Smitherman, Dan Su, Renata A.G. Reis, Giovanni Gadda, Johnson Agniswamy, Irene T. Weber, Yuan-Fang Wang
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 86:599-605
Nitronate monooxygenase (NMO) is an FMN-dependent enzyme that oxidizes the neurotoxin propionate 3-nitronate (P3N) and represents the best-known system for P3N detoxification in different organisms. The crystal structure of the first eukaryotic Class
Autor:
Felipe A. Calil, Giovani P. Tomaleri, Renata A.G. Reis, Juliana S. David, Humberto D'Muniz Pereira, Ricardo A.P. de Pádua, M. Cristina Nonato
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
Trematode worms of the genus Schistosoma are the causing agents of schistosomiasis, a parasitic disease responsible for a considerable economic and healthy burden worldwide. In the present work, the characterization of the enzyme dihydroorotate dehyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c49620f0f660157f21bef20ee2e7a89e
Publikováno v:
Archives of Biochemistry and Biophysics. 699:108765
Flavin-dependent monooxygenases catalyze a wide variety of redox reactions in important biological processes and are responsible for the synthesis of highly complex natural products. Although much has been learned about FMO chemistry in the last ~80
Publikováno v:
Biochemical Journal. 473:651-660
Leishmania major dihydro-orotate dehydrogenase (DHODHLm) has been considered as a potential therapeutic target against leishmaniasis. DHODHLm, a member of class 1A DHODH, oxidizes dihydro-orotate (DHO) to orotate (ORO) during pyrimidine biosynthesis
The crystal structure of the NADH:quinone oxidoreductase PA1024 has been solved in complex with NAD(+) to 2.2 Å resolution. The nicotinamide C4 is 3.6 Å from the FMN N5 atom, with a suitable orientation for facile hydride transfer. NAD(+) binds in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf0e4d690284713f68b5bd835786a9ef
https://europepmc.org/articles/PMC6295900/
https://europepmc.org/articles/PMC6295900/