Anion binding at the active site of trypanosomal triosephosphate isomerase: monohydrogen phosphate does not mimic sulphate

The three-dimensional structure of triosephosphate isomerase complexed with the competitive inhibitor HP024- was determined by x-ray crystallography to a resolution of 0.24 nm. A comparison with the native crystal structure, where, SO24- is bound, revealed five changes: (a) a 0.10-nm shift of the an...

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Veröffentlicht in:	European journal of biochemistry 1991-05, Vol.198 (1), p.53-57
Hauptverfasser:	Verlinde, C.L.M.J. (University of Groningen, Groningen, The Netherlands), Noble, M.E.M, Kalk, K.H, Groendijk, H, Wierenga, R.K, Hol, W.G.J
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals ANION ANIONES Anions - metabolism AZUFRE Binding Sites Biological and medical sciences CHIMIE Enzymes and enzyme inhibitors FOSFATOS FOSFORO Fundamental and applied biological sciences. Psychology ISOMERASAS ISOMERASE Isomerases Molecular Structure MONOSACARIDOS MONOSACCHARIDE ORGANITE CELLULAIRE Organophosphorus Compounds - metabolism ORGANULOS CITOPLASMATICOS PHOSPHATE PHOSPHORE QUIMICA SOUFRE Sulfuric Acids - metabolism Triose-Phosphate Isomerase - metabolism TRYPANOSOMA BRUCEI Trypanosoma brucei brucei - enzymology X-Ray Diffraction
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