protein

Aconitase, Porcine Heart

MBS634715

100 Units

605 USD

Protein

Aconitase, Porcine Heart

Aconitase, Porcine Heart

aconitate hydratase, mitochondrial; Aconitate hydratase, mitochondrial; aconitate hydratase, mitochondrial; heart aconitase; citrate hydro-lyase; Citrate hydro-lyase

ACO2; ACO2; Aconitase

ACON_PIG

bovine

Porcine Heart

Highly Purified. Highly Purified

Supplied as a liquid 50% glycerol pH 7.2

May be stored at 4 degree C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Suitable for use as a calibrator or control serum.

Standard: Aconitase-05. Specific Activity: 10U/mg protein. Activity: 153U/ml

Growth Factors, Cytokines; Growth Factors-Interferon

Citrate (isocitrate) hydro-lyase (EC 4.2.1.3) . Aconitase (aconitate hydratase; EC 4.2.1.3), from pig heart, is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process. By contrast with the majority of iron-sulfur proteins that function as electron carriers, the iron-sulfur cluster of aconitase reacts directly with an enzyme substrate. Aconitase has an active [Fe4S4]2+ cluster, which may convert to an inactive [Fe3S4]+ form. Three cysteine (Cys) residues have been shown to be ligands of the [Fe4S4] centre. In the active state, the labile iron ion of the [Fe4S4] cluster is not coordinated by Cys but by water molecules. The iron-responsive element binding protein (IRE-BP) and 3-isopropylmalate dehydratase (-isopropylmalate isomerase; EC 4.2.1.33), an enzyme catalysing the second step in the biosynthesis of leucine, are known aconitase homologues. Iron regulatory elements (IREs) constitute a family of 28-nucleotide, non-coding, stem-loop structures that regulate iron storage, heme synthesis and iron uptake. They also participate in ribosome binding and control the mRNA turnover (degradation). The specific regulator protein, the IRE-BP, binds to IREs in both 5' and 3' regions, but only to RNA in the apo form, without the Fe-S cluster. Expression of IRE-BP in cultured cells has revealed that the protein functions either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted. Mutant IRE-BPs, in which any or all of the three Cys residues involved in Fe-S formation are replaced by serine, have no aconitase activity, but retain RNA-binding properties. Aconitase is inhibited by fluoroacetate, therefore fluoroacetate is poisonous. The iron sulfur cluster is highly sensitive to oxidation by superoxide[1].

47522738

NP_999119.1

NM_213954.1

P16276

2-Oxocarboxylic Acid Metabolism Pathway (716277); 2-Oxocarboxylic Acid Metabolism Pathway (717400); Biosynthesis Of Amino Acids Pathway (791445); Biosynthesis Of Amino Acids Pathway (795174); Carbon Metabolism Pathway (816324); Carbon Metabolism Pathway (817567); Citrate Cycle (TCA Cycle) Pathway (84362); Citrate Cycle (TCA Cycle) Pathway (288); Citrate Cycle (TCA Cycle, Krebs Cycle) Pathway (855857); Citrate Cycle (TCA Cycle, Krebs Cycle) Pathway (468202)

ACO2: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Monomer. Belongs to the aconitase/IPM isomerase family. Protein type: Lyase; Carbohydrate Metabolism - glyoxylate and dicarboxylate; Carbohydrate Metabolism - citrate (TCA) cycle; EC 4.2.1.3; Mitochondrial. Cellular Component: mitochondrion. Molecular Function: metal ion binding; 4 iron, 4 sulfur cluster binding; aconitate hydratase activity. Biological Process: tricarboxylic acid cycle

100 Units

605 USD