The Crystal Structure of a Bacterial l -Arabinonate Dehydratase Contains a [2Fe-2S] Cluster

Autor: Janne Jänis, Mohammad Mubinur Rahman, Merja Penttilä, Martina Andberg, Senthil K. Thangaraj, Nina Hakulinen, Tarja Parkkinen, Juha Rouvinen, Anu Koivula

Publikováno v: Rahman, M, Andberg, M, Thangaraj, S, Parkkinen, T, Penttilä, M, Jänis, J, Koivula, A, Rouvinen, J & Hakulinen, N 2017, ' The Crystal Structure of a Bacterial l-Arabinonate Dehydratase Contains a [2Fe-2S] Cluster ', ACS Chemical Biology, vol. 12, no. 7, pp. 1919-1927 . https://doi.org/10.1021/acschembio.7b00304

We present a novel crystal structure of the IlvD/EDD family enzyme, l-arabinonate dehydratase from Rhizobium leguminosarum bv. trifolii (RlArDHT, EC 4.2.1.25), which catalyzes the conversion of l-arabinonate to 2-dehydro-3-deoxy-L-arabinonate. The en

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http://juuli.fi/Record/0284346517

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase fromAgrobacterium tumefaciens

Autor: Martina Andberg, Peter Richard, Juha Rouvinen, Helena Taberman, Nina Hakulinen, Anu Koivula, Tarja Parkkinen

Publikováno v: Taberman, H, Andberg, M, Parkkinen, T, Richard, P, Hakulinen, N, Koivula, A & Rouvinen, J 2014, ' Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens ', Acta Crystallographica Section F: Structural Biology Communications, vol. 70, pp. 49-52 . https://doi.org/10.1107/S2053230X13031361

D-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-D-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of

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https://doi.org/10.1107/s2053230x13031361

Crystal structures of an enantioselective Fab-fragment in free and complex forms

Autor: Anu Koivula, Tarja K. Nevanen, Tarja Parkkinen, Juha Rouvinen

Publikováno v: Parkkinen, T, Nevanen, T, Koivula, A & Rouvinen, J 2006, ' Crystal structures of an enantioselective Fab-fragment in free and complex forms ', Journal of Molecular Biology, vol. 357, no. 2, pp. 471-480 . https://doi.org/10.1016/j.jmb.2005.12.045

Enantioselective antibodies can separate the enantiomers of a chiral compound in a highly specific manner. We have recently reported the cloning and applications of a recombinant Fab-fragment, ENA11His, in the enantioseparation of a drug candidate, f

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https://cris.vtt.fi/en/publications/ed8bdd53-2557-41ed-9bd0-05493593411a

Structure and function of a decarboxylating Agrobacterium tumefaciens keto-deoxy-d-galactarate dehydratase

Autor: Janne Jänis, Juha Rouvinen, Tarja Parkkinen, Martina Andberg, Helena Taberman, Merja Penttilä, Nina Hakulinen, Anu Koivula

Publikováno v: Taberman, H, Andberg, M, Parkkinen, T, Jänis, J, Penttilä, M, Hakulinen, N, Koivula, A & Rouvinen, J 2014, ' Structure and function of a decarboxylating Agrobacterium tumefaciens Keto-deoxy-D-galactarate dehydratase ', Biochemistry, vol. 53, no. 51, pp. 8052-8060 . https://doi.org/10.1021/bi501290k

(Figure Presented) Agrobacterium tumefaciens (At) strain C58 contains an oxidative enzyme pathway that can function on both D-glucuronic and D-galacturonic acid. The corresponding gene coding for At keto-deoxy-D-galactarate (KDG) dehydratase is locat

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https://pubmed.ncbi.nlm.nih.gov/25454257

Crystallization and preliminary X-ray characterization ofTrichoderma reeseihydrophobin HFBII

Autor: Markus Linder, Tarja Parkkinen, Juha Rouvinen, Johanna Hakanpää, Nina Hakulinen

Publikováno v: Hakanpää, J, Parkkinen, T, Hakulinen, N, Linder, M & Rouvinen, J 2004, ' Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII ', Acta Crystallographica Section D: Biological Crystallography, vol. 60, no. 1, pp. 163-165 . https://doi.org/10.1107/S0907444903024430
EMBL-EBI

Hydrophobins are small proteins found in filamentous fungi and characterized by their ability to change the character of a surface by spontaneous self-assembly on a hydrophobic-hydrophilic interface. Hydrophobin HFBII from Trichoderma reesei was crys

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https://doi.org/10.1107/s0907444903024430