Dimerization and bifunctionality confer robustness to the isocitrate dehydrogenase regulatory system in escherichia coli

Journal of Biological Chemistry

Volumn 288, Issue 8, 2013, Pages 5770-5778

  Dexter, Joseph P ^a,b   Gunawardena, Jeremy ^a,b  

^a PRINCETON UNIVERSITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HOMODIMERIZATION; ISOCITRATE DEHYDROGENASE; REGULATORY SYSTEMS; SYSTEMS BIOLOGY;

ENZYMES; ESCHERICHIA COLI; MATHEMATICAL MODELS;

DIMERIZATION;

CARBON; GLYOXYLIC ACID; ISOCITRATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE PHOSPHATASE; PHOSPHATASE; TRICARBOXYLIC ACID; UNCLASSIFIED DRUG;

BACTERIAL GROWTH; BIOCHEMISTRY; CITRIC ACID CYCLE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ESCHERICHIA COLI; MATHEMATICAL MODEL; NONHUMAN; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; REVIEW; STEADY STATE; SYSTEMS BIOLOGY;

BIOCHEMISTRY; CATALYTIC DOMAIN; CITRIC ACID CYCLE; DIMERIZATION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLYOXYLATES; ISOCITRATE DEHYDROGENASE; KINETICS; MODELS, CHEMICAL; MODELS, THEORETICAL; MOLECULAR CONFORMATION; SYSTEMS BIOLOGY;

EID: 84874298505     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.339226     Document Type: Review

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