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Difference between revisions of "User:Beatrice Cobucci-Ponzano"
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Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR). | Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase ([[GH1]]) from the archaeon ''Sulfolobus solfataricus'', under the supervision of Mosè Rossi at the [http://www.ibp.cnr.it/ Institute of Protein Biochemistry] (IBP) of the italian [http://www.cnr.it/sitocnr/Englishversion/Englishversion.html National Research Council] (CNR). | ||
She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of Marco Moracci at IBP. | She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles ([[GH1]] and [[GH31]]) under the supervision of Marco Moracci at IBP. | ||
| − | From 2001 she is staff scientist at IBP in the group of [[Marco Moracci]]. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases. | + | From 2001 she is staff scientist at IBP in the group of [[User:Marco Moracci|Marco Moracci]]. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases. |
| − | She | + | She determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases. |
| − | Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the | + | Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family [[GH116]] <cite>PMID20427274</cite>. |
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#PMID20427274 pmid=20427274 | #PMID20427274 pmid=20427274 | ||
</biblio> | </biblio> | ||
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| + | [[Category:Contributors|Cobucci-Ponzano,Beatrice]] | ||
Latest revision as of 13:34, 18 December 2021
Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase (GH1) from the archaeon Sulfolobus solfataricus, under the supervision of Mosè Rossi at the Institute of Protein Biochemistry (IBP) of the italian National Research Council (CNR).
She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles (GH1 and GH31) under the supervision of Marco Moracci at IBP.
From 2001 she is staff scientist at IBP in the group of Marco Moracci. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
She determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases (GH29) [1, 2, 3], and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases [4]. This method could be of general applicability to all alpha-glycosidases.
Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family GH116 [5].
Reference list
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- Error fetching PMID 12569098:
- Error fetching PMID 12911294:
- Error fetching PMID 15835922:
- Error fetching PMID 19875083:
- Error fetching PMID 20427274: