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Träfflista för sökning "WFRF:(Engelmark R.) srt2:(2010-2014)"

Search: WFRF:(Engelmark R.) > (2010-2014)

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1.
  • Cederberg, B., et al. (author)
  • Tvåvingar
  • 2010
  • In: Rödlistade arter i Sverige 2010. - 9789188506351 ; , s. 185-202
  • Book chapter (other academic/artistic)abstract
    • Abstract is not available
  •  
2.
  • Gaffney, Darragh, et al. (author)
  • Preparation and characterisation of a Ni2+/Co2+-cyclam modified mesoporous cellular foam for the specific immobilisation of His(6)-alanine racemase
  • 2014
  • In: Journal of Molecular Catalysis B. - : Elsevier BV. - 1381-1177 .- 1873-3158. ; 109, s. 154-160
  • Journal article (peer-reviewed)abstract
    • Nickel and cobalt cyclam modified mesocellular foam (MCF) materials were prepared and characterised. The metal cyclam modified materials displayed reduced surface areas and pore diameters in comparison to MCF. The modified materials were used to specifically anchor a histidine tagged form of the enzyme, alanine racemase (HT-AlaR). Non-specific adsorption was predominantly hydrophobic//hydrophilic in nature and could be significantly reduced in the presence of 2% polyethylene glycol. The activity of HT-AlaR immobilised on Ni and Co-MCF was essentially the same as that of the free enzyme, demonstrating that enzymes can be specifically immobilised within the pores of mesoporous materials in a stable and catalytically active manner.
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3.
  • Svedendahl Humble, Maria, et al. (author)
  • Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.
  • 2012
  • In: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 279:5, s. 779-792
  • Journal article (peer-reviewed)abstract
    • The bacterial ω-transaminase from Chromobacterium violaceum (Cv-ωTA, EC2.6.1.18) catalyses industrially important transamination reactions by use of the coenzyme pyridoxal 5'-phosphate (PLP). Here, we present four crystal structures of Cv-ωTA: two in the apo form, one in the holo form and one in an intermediate state, at resolutions between 1.35 and 2.4 Å. The enzyme is a homodimer with a molecular mass of ∼ 100 kDa. Each monomer has an active site at the dimeric interface that involves amino acid residues from both subunits. The apo-Cv-ωTA structure reveals unique 'relaxed' conformations of three critical loops involved in structuring the active site that have not previously been seen in a transaminase. Analysis of the four crystal structures reveals major structural rearrangements involving elements of the large and small domains of both monomers that reorganize the active site in the presence of PLP. The conformational change appears to be triggered by binding of the phosphate group of PLP. Furthermore, one of the apo structures shows a disordered 'roof ' over the PLP-binding site, whereas in the other apo form and the holo form the 'roof' is ordered. Comparison with other known transaminase crystal structures suggests that ordering of the 'roof' structure may be associated with substrate binding in Cv-ωTA and some other transaminases. DATABASE: The atomic coordinates and structure factors for the Chromobacterium violaceumω-transaminase crystal structures can be found in the RCSB Protein Data Bank (http://www.rcsb.org) under the accession codes 4A6U for the holoenzyme, 4A6R for the apo1 form, 4A6T for the apo2 form and 4A72 for the mixed form STRUCTURED DIGITAL ABSTRACT: •  -transaminases and -transaminases bind by dynamic light scattering (View interaction) •  -transaminase and -transaminase bind by x-ray crystallography (View interaction) •  -transaminase and -transaminase bind by x-ray crystallography (View interaction).
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