Design of Biofunctional Assemblies on Solids through Recombinant Spherical Bacterial Protein Lumazine Synthase

Fischer, Markus; Bacher, Adelbert; Haase, Ilka; Tristl, M.; Sackmann, E.

doi:10.1002/1439-7641(20011015)2:10<623::aid-cphc623>3.0.co;2-r

Cited by 8 publications

(7 citation statements)

References 33 publications

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“…Such a model resembles the physical situation where an actin filament binds to a membrane through anchoring proteins. [14] The discreteness of the binding sites allows us to employ a different kind of thermodynamic limit which avoids the inconsistencies that appear in some previous works. For fixed total length and persistence length (with L ≪ L p ), we take the density of binding sites to infinity under the constraint that the probability of finding such a site inside the binding region remains constant.…”

Section: Introductionmentioning

confidence: 99%

Depinning of semiflexible polymers

Benetatos¹,

Frey

2003

Phys. Rev. E

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We present a theoretical analysis of a simple model of the depinning of an anchored semiflexible polymer from a fixed planar substrate in 1+1 dimensions. We consider a polymer with a discrete sequence of pinning sites along its contour. Using the scaling properties of the conformational distribution function in the stiff limit and applying the necklace model of phase transitions in quasi-one-dimensional systems, we obtain a melting criterion in terms of the persistence length, the spacing between pinning sites, a microscopic effective length that characterizes a bond, and the bond energy. The limitations of this and other similar approaches are discussed. We also consider the general problem of thermal depinning in 1+d dimensions. In the case of force-induced unbinding, it is shown that the bending rigidity favors the unbinding through a "lever-arm effect."

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Section: Introductionmentioning

confidence: 99%

Depinning of semiflexible polymers

Benetatos¹,

Frey

2003

Phys. Rev. E

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“…A more elegant approach to the preparation of isotopomer libraries by parallel synthesis is possible by enzyme-assisted procedures. The enzymes of the riboflavin biosynthetic pathway can be expressed in high yields in recombinant microbial hosts. − As shown in this paper, they can be used for the preparation of numerous different riboflavin isotopomers with overall yields of 35−50% by convenient one-pot procedures using 13 C-labeled glucose as starting material.…”

Section: Introductionmentioning

confidence: 99%

Rapid One-Pot Synthesis of Riboflavin Isotopomers

et al. 2002

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Flavocoenzymes labeled with stable isotopes are important reagents for the study of flavoproteins using isotope-sensitive methods such as NMR, ENDOR, infrared, and Raman spectroscopy. We describe highly versatile one-pot methods for the preparation of riboflavin isotopomers labeled with (13)C in every desired position of the xylene moiety. The starting materials are commercially available (13)C-labeled glucose samples, which are converted into riboflavin using enzymes of the oxidative pentose phosphate pathway in combination with recombinant enzymes of the riboflavin biosynthetic pathway. The overall reaction comprises six enzyme-catalyzed reaction steps for the synthesis of the vitamin and two auxiliary enzymes for in situ recycling of cofactors. The overall yields of riboflavin based on isotope-labeled glucose are 35-50%.

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“…199 Both termini of each lumazine synthase subunit are located on the outer surface of the capsid, thus both termini are accessible for recombinant modifications (such as peptides, or biotin). 200 It was shown that the functionalised lumazine synthase monomers can be assembled into capsids by in vitro renaturation; differently functionalised protomers can be mixed to generate multifunctional capsids. 201 Furthermore, it has been shown that the cavity of recombinant icosahedral lumazine synthase capsids can be used in vitro as a containment of nanocrystalline iron oxide.…”

Section: The Lumazine Synthase-riboflavin Synthase Complexmentioning

confidence: 99%

Biosynthesis of flavocoenzymes

2005

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The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate. The imidazole ring of GTP is hydrolytically opened, yielding a 2,5-diaminopyrimidine that is converted to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione by a sequence of deamination, side chain reduction, and dephosphorylation. Condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone 4-phosphate obtained from ribulose 5-phosphate affords 6,7-dimethyl-8-ribityllumazine. Dismutation of the lumazine derivative yields riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, which is recycled in the biosynthetic pathway. The enzymes of the riboflavin pathway are potential targets for antibacterial agents.

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Design of Biofunctional Assemblies on Solids through Recombinant Spherical Bacterial Protein Lumazine Synthase

Cited by 8 publications

References 33 publications

Depinning of semiflexible polymers

Depinning of semiflexible polymers

Rapid One-Pot Synthesis of Riboflavin Isotopomers

Biosynthesis of flavocoenzymes

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