Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tsuchiya, D.; Shimizu, N.; Tomita, M.
    Cooperativity of two active sites in bacterial homodimeric aconitases (2009), Biochem. Biophys. Res. Commun., 379, 485-488.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.3 gene AcnA, overexpression of the His-tagged protein in an ASKA library, i.e. the 'a complete set of Escherichia coli K-12 ORF archive library Escherichia coli
4.2.1.3 gene ACnB, overexpression of the His-tagged protein in an ASKA library Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.3 Fe2+ the iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three enzyme domains, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.3 cis-aconitate + H2O Escherichia coli aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle isocitrate
-
 r
4.2.1.3 citrate Escherichia coli aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle cis-aconitate + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.3 Escherichia coli P25516 AcnA; gene AcnA
-
4.2.1.3 Escherichia coli P36683 AcnB; gene AcnB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.3 recombinant His-tagged AcnA by metal affinity chromatography Escherichia coli
4.2.1.3 recombinant His-tagged AcnB by metal affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.3 cis-aconitate + H2O
-
 Escherichia coli isocitrate
-
 r
4.2.1.3 cis-aconitate + H2O aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle Escherichia coli isocitrate
-
 r
4.2.1.3 citrate
-
 Escherichia coli cis-aconitate + H2O
-
 r
4.2.1.3 citrate aconitase catalyzes a reversible isomerization of citrate into isocitrate in the Krebs cycle Escherichia coli cis-aconitate + H2O
-
 r
4.2.1.3 additional information the substrate binding may induce a rearrangement of their relative positions. Such a conformational change may result in the negative cooperativity Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.3 homodimer structural modeling, homo-oligomerization of AcnA yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview Escherichia coli
4.2.1.3 homodimer structural modeling, homo-oligomerization of AcnB yields negative cooperativities in isomerization of isocitrate. In the AcnA homodimer, the intersubunit interface is composed of domains II and III. The iron-sulfur cluster, which constitutes the active site, is located at the interdomain boundary among the three domains, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.2.1.3 aconitase
-
 Escherichia coli