Substitutions for Glu-537 of β-galactosidase from Escherichia coli cause large decreases in catalytic activity
- Author
- JINGMING YUAN; MARTINEZ-BILBAO, M; HUBER, R. E
Univ. Calgary, div. biochemistry, Calgary AB T2N 1N4, Canada - Source
Biochemical journal (London. 1984). 1994, Vol 299, pp 527-531 ; 2 ; ref : 18 ref
- ISSN
- 0264-6021
- Scientific domain
- Biochemistry, molecular biology, biophysics
- Publisher
- Portland Press, Colchester
- Publication country
- United Kingdom
- Document type
- Article
- Language
- English
- Keyword (fr)
- Activité enzymatique Escherichia coli Glutamate Mutation Paramètre cinétique Propriété physicochimique Relation structure activité β-Galactosidase Bactérie Enterobacteriaceae Enzyme Glycosidases Hydrolases O-Glycosidases
- Keyword (en)
- Enzymatic activity Escherichia coli Glutamate Mutation Kinetic parameter Physicochemical properties Structure activity relation β-Galactosidase Bacteria Enterobacteriaceae Enzyme Glycosidases Hydrolases O-Glycosidases
- Keyword (es)
- Actividad enzimática Escherichia coli Glutamato Mutación Parámetro cinético Propiedad fisicoquímica Relación estructura actividad β-Galactosidase Bacteria Enterobacteriaceae Enzima Glycosidases Hydrolases O-Glycosidases
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02E Enzymes and enzyme inhibitors / 002A02E04 Hydrolases
- Discipline
- Analytical, structural and metabolic biochemistry
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 4169774
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1042/bj2990527 
https://dx.doi.org/10.1042/bj2990527
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