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Literature summary for 4.2.1.3 extracted from

  • Gupta, P.; Mishra, S.; Chaudhuri, T.K.
    Reduced stability and enhanced surface hydrophobicity drive the binding of apo-aconitase with GroEL during chaperone assisted refolding (2010), Int. J. Biochem. Cell Biol., 42, 683-692.
    View publication on PubMed
Search for more literature for 4.2.1.3

Activating Compound

Activating Compound Comment Organism Structure
Fe4-S4 cluster active enzyme contains an iron-sulfur cluster Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
the recombinant yeast mitochondrial aconitase is expressed in Escherichia coli as soluble, biologically active enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
citrate
-
 Saccharomyces cerevisiae cis-aconitate + H2O
-
 ?

Synonyms

Synonyms Comment Organism
aconitase
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function aconitase is destabilized in the absence of the Fe4S4 cluster. Apo-form has higher surface hydrophobicity than the holo-form. The lower ground state stability and higher solvent exposed hydrophobic surface of the apo-form makes it aggregation prone. Binding of apo-aconitase to GroEL (molecular chaperone) not only rescues it from the aggregation, but also assists in the final stage of maturation by orienting the cluster insertion site of GroEL bound apo-protein Saccharomyces cerevisiae