A5046358236- Enzyme Structure and Function
- Biochemical and Molecular Research
- Amino Acid Enzymes and Metabolism
- Trypanosoma species research and implications
- Metal-Catalyzed Oxygenation Mechanisms
- Polyamine Metabolism and Applications
- Microbial bioremediation and biosurfactants
- Folate and B Vitamins Research
- HIV/AIDS drug development and treatment
- S100 Proteins and Annexins
- Research on Leishmaniasis Studies
- Machine Learning in Bioinformatics
- Microbial Metabolic Engineering and Bioproduction
- Biofuel production and bioconversion
- ATP Synthase and ATPases Research
- RNA and protein synthesis mechanisms
- Porphyrin Metabolism and Disorders
- Chemical Reactions and Isotopes
- Photosynthetic Processes and Mechanisms
- Diet, Metabolism, and Disease
- Polysaccharides and Plant Cell Walls
- Glycosylation and Glycoproteins Research
- Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Kidney Stones and Urolithiasis Treatments
- Chemistry and Chemical Engineering
Georgia State University
2017-2021
Universidade de São Paulo
2014-2021
Johnson & Johnson (United States)
2018
SUPERA Park of Innovation and Technology of Ribeirão Preto
2015
A técnica de Termofluor constitui uma importante ferramenta na identificação moléculas protótipos a fármacos.No presente trabalho, foi desenvolvido um método alternativo para Termofluor, chamado ThermoFMN, que explora o grupo prostético flavina mononucleotídeo (FMN) como sonda fluorescente.A validação do feita através monitoramento da fluorescência FMN diferentes alvos macromoleculares presença biblioteca aleatória ligantes.Além disso, fármacos com eficácia comprovada tiveram seus perfis...
Leishmania major dihydro-orotate dehydrogenase (DHODHLm) has been considered as a potential therapeutic target against leishmaniasis. DHODHLm, member of class 1A DHODH, oxidizes (DHO) to orotate (ORO) during pyrimidine biosynthesis using fumarate (FUM) the oxidizing substrate. In present study, chemistry reduction and reoxidation flavin mononucleotide (FMN) cofactor in DHODHLm was examined by steady- pre-steady state kinetics under both aerobic anaerobic environments. Our results provide for...
Proteins are inherently dynamic, and proper enzyme function relies on conformational flexibility. In this study, we demonstrated how an active site residue changes enzyme's reactivity by modulating fluctuations between states. Replacement of tyrosine 249 (Y249) with phenylalanine in the flavin-dependent d-arginine dehydrogenase yielded both yellow FAD (Y249F-y) inactive chemically modified green FAD, identified as 6-OH-FAD (Y249F-g) through various spectroscopic techniques. Structural...
Nitronate monooxygenase (NMO) is an FMN-dependent enzyme that oxidizes the neurotoxin propionate 3-nitronate (P3N) and represents best-known system for P3N detoxification in different organisms. The crystal structure of first eukaryotic Class I NMO from Cyberlindnera saturnus (CsNMO) has been solved at 1.65 Å resolution refined to R-factor 14.0%. three-dimensional structures yeast CsNMO bacterial PaNMO are highly conserved with exception three additional loops on surface differences four...
The crystal structure of the NADH:quinone oxidoreductase PA1024 has been solved in complex with NAD+ to 2.2 Å resolution. nicotinamide C4 is 3.6 from FMN N5 atom, a suitable orientation for facile hydride transfer. binds folded conformation at interface TIM-barrel domain and extended enzyme. Comparison enzyme-NAD+ that ligand-free enzyme revealed different short loop (75-86) part -binding pocket. P78, P82, P84 provide internal rigidity loop, whereas Q80 serves as an active site latch secures...
Effective use of plant biomass as an abundant and renewable feedstock for biofuel production biorefinery requires efficient enzymatic mobilization cell wall polymers. Knowledge composition architecture has been exploited to develop novel multifunctional enzymes with improved activity against lignocellulose, where a left-handed β–3-prism synthetic scaffold (BeSS) was designed insertion multiple protein domains at the prism vertices. This allowed construction series chimeras fusing variable...
The enzyme dihydroorotate dehydrogenase (DHODH) is a flavoenzyme that catalyses the oxidation of to orotate in de novo pyrimidine-biosynthesis pathway. In this study, reproducible protocol for heterologous expression active from Leishmania (Viannia) braziliensis (LbDHODH) was developed and its crystal structure determined at 2.12 Å resolution. L. (V.) species responsible mucosal form leishmaniasis, neglected disease which no cure or effective therapy available. Analyses sequence, structural...
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, was purified and its biochemical kinetic properties were characterized. Absorption spectroscopy mass spectrometry demonstrated tightly, noncovalently bound FMN in active site of enzyme. Analytical ultracentrifugation showed that enzyme exists dimer solution. Despite annotation, did not exhibit...