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Merck

A5384

Sigma-Aldrich

Aconitase from porcine heart

Synonym(e):

Aconitate hydratase, Citrate (isocitrate) hydrolyase

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About This Item

CAS-Nummer:
EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

Porcine heart

Form

solid

Mol-Gew.

~66 kDa by gel filtration

Lagertemp.

−20°C

Anwendung

Aconitase may be usefull in diabetes research as well as to study structural conservation between iron-responsive element binding proteins (IRE-BP) and isomerases .

Biochem./physiol. Wirkung

Aconitase catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle. Aconitase is inhibited by cyanide, sulfide and copper and mercury at low concentrations. It is competitively inhibited by trans-aconitate. Aconitase contains an internal Fe-S cluster which is responsible for its activity.

Einheitendefinition

One unit will convert 1.0 μmole of citrate (via cis-aconitate) to isocitrate per min at pH 7.4 at 25 °C.

Hinweis zur Analyse

Crude preparation containing aconitase activity

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Megan J Morgan et al.
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Ewelina Michta et al.
Environmental microbiology, 14(12), 3203-3219 (2012-11-03)
In many organisms, aconitases have dual functions; they serve as enzymes in the tricarboxylic acid cycle and as regulators of iron metabolism. In this study we defined the role of the aconitase AcnA in Streptomyces viridochromogenes Tü494, the producer of
Lucy M Hinder et al.
The Journal of endocrinology, 216(1), 1-11 (2012-10-23)
Diabetic neuropathy (DN) is the most common complication of diabetes and is characterized by distal-to-proximal loss of peripheral nerve axons. The idea of tissue-specific pathological alterations in energy metabolism in diabetic complications-prone tissues is emerging. Altered nerve metabolism in type
Béatrice Py et al.
Molecular microbiology, 86(1), 155-171 (2012-09-13)
Biosynthesis of iron-sulphur (Fe-S) proteins is catalysed by multi-protein systems, ISC and SUF. However, 'non-ISC, non-SUF' Fe-S biosynthesis factors have been described, both in prokaryotes and eukaryotes. Here we report in vitro and in vivo investigations of such a 'non-ISC
Bassel Dawod et al.
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