Sensitivity analysis of metabolic cascades catalyzed by bifunctional enzymes

Molecular Biology Reports

Volumn 29, Issue 1-2, 2002, Pages 211-215

  Ortega, Fernando ^a   Ehrenberg, Måns ^b   Acerenza, Luis ^c   Westerhoff, Hans V ^d   Mas, Francesc ^a   Cascante, Marta ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b UPPSALA UNIVERSITY   (Sweden)

^c UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

^d VU UNIVERSITY AMSTERDAM   (Netherlands)

Author keywords

Bifunctional enzymes; Metabolic cascades; Sensitivity analysis; Zero order ultrasensitivity

Indexed keywords

ENZYME INHIBITOR; MULTIENZYME COMPLEX;

ARTICLE; BIOLOGICAL MODEL; CATALYSIS; DRUG ANTAGONISM; KINETICS; MATHEMATICS; METABOLISM;

CATALYSIS; ENZYME INHIBITORS; KINETICS; MATHEMATICS; MODELS, BIOLOGICAL; MULTIENZYME COMPLEXES;

EID: 0036037681     PISSN: 03014851     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020334014497     Document Type: Article

References (9)

1. Fluctuations and quality of control in biological cells: Zero-order ultrasensitivity reinvestigated
2. Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector
3. Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
4. An amplified sensitivity arising from covalent modification in biological systems
5. Ultrasensitivity in biochemical systems controlled by covalent modification
6. The control of flux
7. Product dependence and bifunctionality compromise the ultrasensitivity of signal transduction cascades
8. Covalent modification and metabolic control analysis. Modification to the theorems and their application to metabolic systems containing covalently modifiable enzymes