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Difference between revisions of "User:Vincent Eijsink"
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| − | Vincent Eijsink obtained an MSc in Molecular Sciences (Biochemistry) from Wageningen University and completed his PhD at the Groningen Biomolecular Sciences and Biotechnology Institute under the supervision of Gerard Venema in 1991. During his Ph.D. studies, focusing on the engineering of protein stability, he was co-supervised by Herman Berendsen, Bauke Dijkstra and Gert Vriend and he had several short stays in the Bioinformatics group at EMBL. In 1993, he moved to what is now called the Norwegian University of Life Sciences, in Ås, Norway, where he became a full professor of Biochemistry in 1997. Work on CAZymes started off with work on [http://www.cazy.org/GH18.html family 18 chitinases] in the late 1990s, resulting in several papers on the structure and function of these enzymes <cite>VanAalten2000 VanAalten2001</cite>. Current work focuses on [http://www.cazy.org/GH18.html family 18 chitinases] <cite>Horn2006 | + | Vincent Eijsink obtained an MSc in Molecular Sciences (Biochemistry) from Wageningen University and completed his PhD at the Groningen Biomolecular Sciences and Biotechnology Institute under the supervision of Gerard Venema in 1991. During his Ph.D. studies, focusing on the engineering of protein stability, he was co-supervised by Herman Berendsen, Bauke Dijkstra and Gert Vriend and he had several short stays in the Bioinformatics group at EMBL. In 1993, he moved to what is now called the Norwegian University of Life Sciences (NMBU), in Ås, Norway, where he became a full professor of Biochemistry in 1997. Work on CAZymes started off with work on [http://www.cazy.org/GH18.html family 18 chitinases] in the late 1990s, resulting in several papers on the structure and function of these enzymes <cite>VanAalten2000 VanAalten2001</cite>. Current chitin-related work focuses on [http://www.cazy.org/GH18.html family 18 chitinases] <cite>Horn2006 Zakariassen2009 Vaaje-Kolstad2013 </cite> and family 19 chitinases <cite>Hoell2006</cite>, whereas the group has a growing interest and activity in chitin deacetylases ([http://www.cazy.org/CE4.html CE family 4]) <cite>Liu2017 Tuveng2017</cite>. Recent research includes CAZyme discovery <cite>Pope2012 Larsbrink2016 Tuvengb2017</cite>. Another research focus concerns proteins belonging to [http://www.cazy.org/CBM33.html CBM family 33] that facilitate degradation of crystalline polymeric substrates such as chitin by glycoside hydrolases <cite>Kolstad2005 Kolstadb2005 Kolstad2009</cite>. |
References | References | ||
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#VanAalten2000 pmid=10823940 | #VanAalten2000 pmid=10823940 | ||
#VanAalten2001 pmid=11481469 | #VanAalten2001 pmid=11481469 | ||
| − | #Horn2006 | + | #Horn2006 pmid=17116887 |
| − | |||
#Zakariassen2009 pmid=19244232 | #Zakariassen2009 pmid=19244232 | ||
| + | #Vaaje-Kolstad2013 pmid=23398882 | ||
#Hoell2006 pmid=17010167 | #Hoell2006 pmid=17010167 | ||
| − | # | + | #Liu2017 pmid=28496100 |
| − | # | + | #Tuveng2017 pmid=29107991 |
| + | #Pope2012 pmid=22701672 | ||
| + | #Larsbrink2016 pmid=27933102 | ||
| + | #Tuvengb2017 pmid=27169553 | ||
#Kolstad2005 pmid=15590674 | #Kolstad2005 pmid=15590674 | ||
#Kolstadb2005 pmid=15929981 | #Kolstadb2005 pmid=15929981 | ||
| − | + | ||
</biblio> | </biblio> | ||
[[Category:Contributors|Eijsink, Vincent]] | [[Category:Contributors|Eijsink, Vincent]] | ||
Revision as of 09:57, 15 January 2018
Vincent Eijsink obtained an MSc in Molecular Sciences (Biochemistry) from Wageningen University and completed his PhD at the Groningen Biomolecular Sciences and Biotechnology Institute under the supervision of Gerard Venema in 1991. During his Ph.D. studies, focusing on the engineering of protein stability, he was co-supervised by Herman Berendsen, Bauke Dijkstra and Gert Vriend and he had several short stays in the Bioinformatics group at EMBL. In 1993, he moved to what is now called the Norwegian University of Life Sciences (NMBU), in Ås, Norway, where he became a full professor of Biochemistry in 1997. Work on CAZymes started off with work on family 18 chitinases in the late 1990s, resulting in several papers on the structure and function of these enzymes [1, 2]. Current chitin-related work focuses on family 18 chitinases [3, 4, 5] and family 19 chitinases [6], whereas the group has a growing interest and activity in chitin deacetylases (CE family 4) [7, 8]. Recent research includes CAZyme discovery [9, 10, 11]. Another research focus concerns proteins belonging to CBM family 33 that facilitate degradation of crystalline polymeric substrates such as chitin by glycoside hydrolases [12, 13, 14].
References
- van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, and Wierenga RK. (2000). Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proc Natl Acad Sci U S A. 2000;97(11):5842-7. DOI:10.1073/pnas.97.11.5842 |
- van Aalten DM, Komander D, Synstad B, Gåseidnes S, Peter MG, and Eijsink VG. (2001). Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci U S A. 2001;98(16):8979-84. DOI:10.1073/pnas.151103798 |
- Horn SJ, Sikorski P, Cederkvist JB, Vaaje-Kolstad G, Sørlie M, Synstad B, Vriend G, Vårum KM, and Eijsink VG. (2006). Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc Natl Acad Sci U S A. 2006;103(48):18089-94. DOI:10.1073/pnas.0608909103 |
- Zakariassen H, Aam BB, Horn SJ, Vårum KM, Sørlie M, and Eijsink VG. (2009). Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency. J Biol Chem. 2009;284(16):10610-7. DOI:10.1074/jbc.M900092200 |
- Vaaje-Kolstad G, Horn SJ, Sørlie M, and Eijsink VG. (2013). The chitinolytic machinery of Serratia marcescens--a model system for enzymatic degradation of recalcitrant polysaccharides. FEBS J. 2013;280(13):3028-49. DOI:10.1111/febs.12181 |
- Hoell IA, Dalhus B, Heggset EB, Aspmo SI, and Eijsink VG. (2006). Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes. FEBS J. 2006;273(21):4889-900. DOI:10.1111/j.1742-4658.2006.05487.x |
- Liu Z, Gay LM, Tuveng TR, Agger JW, Westereng B, Mathiesen G, Horn SJ, Vaaje-Kolstad G, van Aalten DMF, and Eijsink VGH. (2017). Structure and function of a broad-specificity chitin deacetylase from Aspergillus nidulans FGSC A4. Sci Rep. 2017;7(1):1746. DOI:10.1038/s41598-017-02043-1 |
- Tuveng TR, Rothweiler U, Udatha G, Vaaje-Kolstad G, Smalås A, and Eijsink VGH. (2017). Structure and function of a CE4 deacetylase isolated from a marine environment. PLoS One. 2017;12(11):e0187544. DOI:10.1371/journal.pone.0187544 |
- Pope PB, Mackenzie AK, Gregor I, Smith W, Sundset MA, McHardy AC, Morrison M, and Eijsink VG. (2012). Metagenomics of the Svalbard reindeer rumen microbiome reveals abundance of polysaccharide utilization loci. PLoS One. 2012;7(6):e38571. DOI:10.1371/journal.pone.0038571 |
- Larsbrink J, Zhu Y, Kharade SS, Kwiatkowski KJ, Eijsink VG, Koropatkin NM, McBride MJ, and Pope PB. (2016). A polysaccharide utilization locus from Flavobacterium johnsoniae enables conversion of recalcitrant chitin. Biotechnol Biofuels. 2016;9:260. DOI:10.1186/s13068-016-0674-z |
- Tuveng TR, Arntzen MØ, Bengtsson O, Gardner JG, Vaaje-Kolstad G, and Eijsink VG. (2016). Proteomic investigation of the secretome of Cellvibrio japonicus during growth on chitin. Proteomics. 2016;16(13):1904-14. DOI:10.1002/pmic.201500419 |
- Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, and van Aalten DM. (2005). Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J Biol Chem. 2005;280(12):11313-9. DOI:10.1074/jbc.M407175200 |
- Vaaje-Kolstad G, Horn SJ, van Aalten DM, Synstad B, and Eijsink VG. (2005). The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem. 2005;280(31):28492-7. DOI:10.1074/jbc.M504468200 |