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

BRENDA support

Literature summary extracted from

  • Tsuchiya, D.; Shimizu, N.; Tomita, M.
    Versatile architecture of a bacterial aconitase B and its catalytic performance in the sequential reaction coupled with isocitrate dehydrogenase (2008), Biochim. Biophys. Acta, 1784, 1847-1856.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.3 gene acnB, expression of wild-type enzyme and the fusion protein ICDH-AcnB in Escherichia coli strain BL21 (DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.3 additional information construction of a fusion protein of aconitase B and isocitrate dehydrogenase, ICDH and AcnB, i.e. ICDH-AcnB, structure determination of ICDH-AcnB, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.3 additional information
-
additional information steady-state kinetics Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.3 Mg2+
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.42 46200
-
2 * 46200, estimated from amino acid sequence Escherichia coli
1.1.1.42 85000
-
Guinier analysis 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
-
isocitrate
-
?
4.2.1.3 citrate Escherichia coli
-
cis-aconitate + H2O
-
?
4.2.1.3 additional information Escherichia coli weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.42 Escherichia coli P08200
-
-
4.2.1.3 Escherichia coli P36683
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.42 His-tagged enzyme is purified by TALON resin column chromatography, ICDH fused maltose-binding protein is purified by amylose resin chromatography Escherichia coli
4.2.1.3 recombinant enzymes from Escherichia coli strain BL21(DE3) by gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.42 isocitrate + NADP+
-
Escherichia coli 2-oxoglutarate + CO2 + NADPH + H+
-
?
1.1.1.42 additional information does not use citrate as substrate Escherichia coli ?
-
?
4.2.1.3 cis-aconitate + H2O
-
Escherichia coli isocitrate
-
?
4.2.1.3 citrate
-
Escherichia coli cis-aconitate + H2O
-
?
4.2.1.3 additional information weak interactions, which affects structure and function of the proteins, of aconitase B and isocitrate dehydrogenase, overview. Two monomeric AcnB regions associate with the homodimeric ICDH region. The versatile architecture of AcnB may alter the metabolic process involving the Krebs cycle Escherichia coli ?
-
?
4.2.1.3 additional information the active sites within ICDH-AcnB catalyze the three consecutive reactions, in which citrate is converted to 2-oxoglutarate, via cisaconitate and isocitrate Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.42 homodimer 2 * 46200, estimated from amino acid sequence Escherichia coli
4.2.1.3 homodimer structural analysis by X-ray scattering and modelling of wild-type and mutant enzymes, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.1.1.42 ICDH
-
Escherichia coli
1.1.1.42 isocitrate dehydrogenase
-
Escherichia coli
4.2.1.3 AcnB
-
Escherichia coli
4.2.1.3 aconitase B
-
Escherichia coli
4.2.1.3 More AcnB is a member of the aconitase family Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.3 8
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.42 NADP+
-
Escherichia coli