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Difference between revisions of "User:Marcelo Liberato"
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| − | + | Marcelo Liberato is a postdoctoral fellow in the Brazilian Bioethanol Science and Technology Laboratory (CTBE). He obtained his B. Sc. in Biology from the Federal University of São Carlos and his master and PhD were obtained in Biomolecular Physics at University of São Paulo under the supervision of Prof. Igor Polikarpov. His work is focused on multimodular enzymes, more specifically in comprehending the influence of accessory modules on catalytic domains. He has determined the crystal structures of | |
| − | |||
| − | + | '''Glycoside Hydrolases:''' | |
| − | * | + | * GH5 ''Bacillus licheniformis'' endoglucanase [1] |
| − | |||
| − | |||
| − | '' | + | * GH12 ''Trichoderma harzianum'' endoglucanase [2] |
| + | * GH62 ''Aspergillus nidulans'' arabinofuranosidase [3] | ||
| + | '''Carbohydrate-binding modules:''' | ||
| − | + | * CBM46 ''Bacillus licheniformis'' [1] | |
| − | + | * CBM81 from sugar cane soil metagenome [4] | |
| − | |||
| − | + | '''References''' | |
| − | + | # Liberato MV, Silveira RL, Prates ÉT, De Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS and Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Sci Rep. 2016 Apr 1; 6:23473. DOI:10.1038/srep23473 | PubMed ID:27032335 | HubMed [Liberato2016] | |
| − | + | ||
| + | # Prates ÉT, Stankovic I, Silveira RL, Liberato MV, Henrique-Silva F, Pereira N, Polikarpov I and Skaf MS. X-ray structure and molecular dynamics simulations of endoglucanase 3 from trichoderma harzianum: structural organization and substrate recognition by endoglucanases that lack cellulose binding module. Plos One. 2013 Mar;8(3):e59069. DOI:10.1371/journal.pone.0059069 | PubMed ID:23516599 | HubMed [Prates2013] | ||
Revision as of 17:12, 18 November 2017
Marcelo Liberato is a postdoctoral fellow in the Brazilian Bioethanol Science and Technology Laboratory (CTBE). He obtained his B. Sc. in Biology from the Federal University of São Carlos and his master and PhD were obtained in Biomolecular Physics at University of São Paulo under the supervision of Prof. Igor Polikarpov. His work is focused on multimodular enzymes, more specifically in comprehending the influence of accessory modules on catalytic domains. He has determined the crystal structures of
Glycoside Hydrolases:
- GH5 Bacillus licheniformis endoglucanase [1]
- GH12 Trichoderma harzianum endoglucanase [2]
- GH62 Aspergillus nidulans arabinofuranosidase [3]
Carbohydrate-binding modules:
- CBM46 Bacillus licheniformis [1]
- CBM81 from sugar cane soil metagenome [4]
References
- Liberato MV, Silveira RL, Prates ÉT, De Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS and Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Sci Rep. 2016 Apr 1; 6:23473. DOI:10.1038/srep23473 | PubMed ID:27032335 | HubMed [Liberato2016]
- Prates ÉT, Stankovic I, Silveira RL, Liberato MV, Henrique-Silva F, Pereira N, Polikarpov I and Skaf MS. X-ray structure and molecular dynamics simulations of endoglucanase 3 from trichoderma harzianum: structural organization and substrate recognition by endoglucanases that lack cellulose binding module. Plos One. 2013 Mar;8(3):e59069. DOI:10.1371/journal.pone.0059069 | PubMed ID:23516599 | HubMed [Prates2013]