Crystallographic refinement of interleukin 1 beta at 2.0 A resolution.
- J. Priestle, H. Schär, M. Grütter
- ChemistryProceedings of the National Academy of Sciences…
- 1 December 1989
Comparison of theIL-1 beta structure with IL-1 alpha sequences indicates that IL- 1 alpha probably has a similar overall folding as IL-2 beta but binds to the receptor in a different fashion.
Purification and characterization of dihydrodipicolinate synthase from pea.
Dihydrodipicolinate synthase from pea is highly specific for the substrates pyruvate and l-aspartate-beta-semialdehyde; it follows Michaelis-Menten kinetics for both substrates.
Biodegradation of chemical waste by specialized methylotrophs, an alternative to physical methods of waste disposal
New target enzyme(s) for bisphosphonates: inhibition of geranylgeranyl diphosphate synthase
The results clearly show that a group of bisphosphonates inhibit the chlorophyll- and carotenoid-biosynthesis pathways by blocking geranylgeranyl diphosphate synthase without interfering with the shikimate pathway as previously published.
Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
Structures have been determined of Bacillus stearothermophilus “apo” and holo lactate dehydrogenase. The holo-enzyme had been co-crystallized with the activator fructose 1,6-biosphosphate. The “apo”…
Purification and characterization of N,N-dimethylformamidase from Pseudomonas DMF 3/3.
- H. Schär, W. Holzmann, G. M. Ramos Tombo, O. Ghisalba
- Chemistry, BiologyEuropean journal of biochemistry
- 1 August 1986
Emission and atomic absorption spectroscopy measurements showed that iron is present in significant amounts in DMFase, indicating that it is an iron-containing amidohydrolase.
Crystal structure of the cytokine interleukin‐1 beta.
The crystal structure of human recombinant interleukin‐1 beta has been determined by the isomorphous replacement method in conjunction with solvent flattening techniques and no strong internal sequence homology between topologically corresponding residues exists.
Structure determination and refinment of Bacillus stearothermophilus lactate dehydrogenase
The “apo” lactate dehydration structure was solved by use of the known apo‐M4 dogfish lactate dehydrogenase molecule as a starting model and phases were refined and extended from 4 Å resolution by means of the noncrystallographic molecular 222 symmetry.
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. I) Isolation and characterization of lactate dehydrogenases from thermophilic and mesophilic bacilli.
Preliminary structural data show the expected close phylogenetic relationship, but also typical differences between thermophilic and mesophilic dehydrogenases, a suitable basis for further comparative studies.