Characterization of recombinant Arabidopsis thaliana threonine synthaseB Laber
Hoechst Schering AgrEvo GmbH, Biochemical Research, Frankfurt am Main, Germany
Eur J Biochem 263:212-21. 1999
..The crystals diffracted to beyond 0.28 nm resolution and belonged to the space group P222 (unit cell parameters: a = 6.16 nm, b = 10.54 nm, c = 14.63 nm, alpha = beta = gamma = 90 degrees)...
Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ proteinB Laber
Hoechst Schering AgrEvo GmbH, Biochemical Research, Frankfurt am Main, Germany
FEBS Lett 449:45-8. 1999
..The sugar used as substrate by PdxJ is 1-deoxy-D-xylulose-5-phosphate rather than the previously assumed 1-deoxy-D-xylulose. The first vitamin B6 vitamer synthesised is PNP, and not pyridoxine...
Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyaseB Laber
Hoechst Schering AgrEvo GmbH, Berlin, Germany
FEBS Lett 379:94-6. 1996
..The crystals are suitable for X-ray analysis and a complete native date set to 1.83 A resolution has been collected using synchrotron radiation...
Structural basis for the function of pyridoxine 5'-phosphate synthaseM G Franco
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, D 82152 Planegg Martinsried, Germany
Structure 9:245-53. 2001
..PNP synthase (commonly referred to as PdxJ) is a homooctameric enzyme that catalyzes the final step in this pathway, a complex intramolecular condensation reaction between 1-deoxy-D-xylulose-5'-phosphate and 1-amino-acetone-3-phosphate...
Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzymeM Garrido Franco
Max Planck Institute of Biochemistry, Department of Structural Investigation, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Acta Crystallogr D Biol Crystallogr 56:1045-8. 2000
..The 12 mercury sites located are related by 222 symmetry and, in combination with self-rotation search analyses and gel-filtration experiments, indicate the quaternary assembly of PdxJ into octamers with 422 symmetry...
Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray studyT Clausen
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D 82152 Martinsried, Germany
Biochemistry 36:12633-43. 1997
..e. protonation of PLP-C4', resulting in the "dead-end" ketimine PLP derivative. The CBLAVG structure furthermore suggests a binding mode for rhizobitoxine and explains the failure of MVG to inhibit CBL...
Mode of action of cystathionine beta-lyaseT Clausen
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried, Germany
Biol Chem 378:321-6. 1997
..In combination with further spectroscopic data, crystallographic evidence permits the formulation of a likely reaction mechanism...
Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopyS Blickling
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried, FRG
Biochemistry 36:24-33. 1997
..By this method, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid is identified as the only product. A reaction mechanism for DHDPS is proposed, and important features for inhibition are identified...
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 AT Clausen
Max Planck Institut fur Biochemie, Abteilung Strukturforschung, Martinsried Germany
J Mol Biol 262:202-24. 1996
..3 A resolution to an R-factor of 16.2%. It suggests that Lys210, the PLP-binding residue, mediates the proton transfer between C alpha and S gamma...
Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallizationB Laber
Max Planck Institute für Biochemie, Martinsried, Federal Republic of Germany
Biochem J 288:691-5. 1992
..26 nm and c = 11.19 nm. The density of the crystals indicates the presence of a dimer of DHDPS subunits per asymmetric unit...