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Analyse structurale du site actif de trois métallopeptidases à zinc: Endopeptidase Neutre-24. II, Aminopeptidase N et Enzyme de Conversion de l'Angiotensine

Other title
Structural analysis of the active site of three Zinc-metallopeptidases: Neutral Endopeptidase-24.11, Aminopeptidase N and Angiotensin Converting Enzyme (en)
Author
Helene, Armelle; Ascher, P (Advisor (for a thesis or dissertation)) ; Roques, B.-P (Advisor (for a thesis or dissertation))
Université de Paris 06, Paris, France (Degree-grantor)
Source

Analyse structurale du site actif de trois métallopeptidases à zinc: Endopeptidase Neutre-24. II, Aminopeptidase N et Enzyme de Conversion de l'Angiotensine. 1993, 160 p., ref : 481 ref

Thesis number
93 PA06 6569
Document type
Thesis (New Ph.D. thesis)
Language
French
Keyword (fr)
Analyse structurale Composition chimique Membrane alanyl aminopeptidase Neprilysin Peptidyl-dipeptidase A Site actif Spécificité Séquence aminoacide Aminopeptidases Enzyme Hydrolases Metalloendopeptidases Peptidyl-dipeptidases Proteinases
Keyword (en)
Structural analysis Chemical composition Membrane alanyl aminopeptidase Neprilysin Peptidyl-dipeptidase A Active site Specificity Aminoacid sequence Aminopeptidases Enzyme Hydrolases Metalloendopeptidases Peptidyl-dipeptidases Proteinases
Keyword (es)
Análisis estructural Composición química Membrane alanyl aminopeptidase Neprilysin Peptidyl-dipeptidase A Lugar activo Especificidad Secuencia aminoácido Aminopeptidases Enzima Hydrolases Metalloendopeptidases Peptidyl-dipeptidases Proteinases
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
163816

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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