Identification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors

Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase (EC 3.2.1.73) was modified by the mechanism-based, affinity-labeling reagent [14C](3,4)-epoxybutyl beta-D-cellobioside. Following partial inactivation a completely inactivated enzyme preparation containing 1.1 mol of covalently boun...

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Veröffentlicht in:	The Journal of biological chemistry 1992-12, Vol.267 (35), p.25059-25066
Hauptverfasser:	Høj, P B, Condron, R, Traeger, J C, McAuliffe, J C, Stone, B A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacillus - enzymology Binding Sites Biological and medical sciences Chromatography, High Pressure Liquid Enzymes and enzyme inhibitors Epoxy Compounds - pharmacology Fundamental and applied biological sciences. Psychology General aspects, investigation methods Glutamates Glutamic Acid Glycoside Hydrolases - antagonists & inhibitors Glycoside Hydrolases - metabolism Mass Spectrometry Molecular Sequence Data Peptide Fragments - isolation & purification Peptide Mapping Sequence Homology, Amino Acid Serine Endopeptidases
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