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Literature summary for 4.2.1.3 extracted from

  • Tang, Y.; Guest, J.R.; Artymiuk, P.J.; Green, J.
    Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation (2005), Mol. Microbiol., 56, 1149-1158.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
AcnB domain 5-4 polypeptide is expressed in Escherichia coli as a GST-AcnB5-4 fusion protein Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe a iron-mediated dimerization mechanism for switching AcnB between its catalytic and regulatory form is proposed Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant AcnB5-4 polypeptide Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information aconitase B is the major citric acid cycle aconitase and also a post-transcriptional regulator Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
AcnB
-
Escherichia coli
aconitase B
-
Escherichia coli