Structural basis fot the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I : a two metal ion mechanism
- Author
- BEESE, L. S; STEITZ, T. A
Yale univ., Howard Hughes medical inst., dep. molecular biophysics, New Haven CT 06511, United States - Source
EMBO journal (Print). 1991, Vol 10, Num 1, pp 25-33, 9 p ; ref : 47 ref
- CODEN
- EMJODG
- ISSN
- 0261-4189
- Scientific domain
- Biochemistry, molecular biology, biophysics
- Publisher
- Nature Publishing Group, London
- Publication country
- United Kingdom
- Document type
- Article
- Language
- English
- Keyword (fr)
- Activité catalytique Cristallographie DNA polymerase 1 Diffraction RX Enzyme Escherichia coli Exonuclease Ion métallique Mécanisme action Structure 3 dimensions Structure cristalline Fragment Klenow Bactérie Enterobacteriaceae
- Keyword (en)
- Catalyst activity Crystallography DNA polymerase 1 X ray diffraction Enzyme Escherichia coli Exonuclease Metal ion Mechanism of action Spatial structure Crystalline structure Bacteria Enterobacteriaceae
- Keyword (es)
- Actividad catalítica Cristalografía DNA polymerase 1 Difracción RX Enzima Escherichia coli Exonuclease Ión metálico Mecanismo acción Estructura 3 dimensiones Estructura cristalina Bacteria Enterobacteriaceae
- 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 / 002A02E03 Transferases
- Discipline
- Analytical, structural and metabolic biochemistry
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 19535467
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
10.1002/j.1460-2075.1991.tb07917.x 
https://dx.doi.org/10.1002/j.1460-2075.1991.tb07917.x
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