TY - JOUR. T1 - Identification of a cysteine residue at the active site of Escherichia coli isocitrate lyase. AU - Nimmo, H. G.. AU - Douglas, F.. AU - Kleanthous, C.. AU - Campbell, D. G.. AU - MacKintosh, C. PY - 1989. Y1 - 1989. N2 - Escherichia coli isocitrate lyase was inactivated by iodacetate in a pseudo-first-order process. Complete inactivation was associated with the incorporation of only one carboxymethyl group per enzyme subunit. The substrate and products of the enzyme protected against inactivation, suggesting that the reactive group may be located at the active site. Isolation and sequencing of a carboxymethylated peptide showed that the modified residue was a cysteine, in the sequence Cys-Gly-His-Met-Gly-Gly-Lys. The reactivity of isocitrate lyase to iodoacetate declined with pH, following a titration curve for a group of pKa 7.1. The Km of the enzyme for isocritrate declined over the same pH range. AB - Escherichia coli isocitrate lyase was inactivated by iodacetate in a ...

Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.

Isocitrate lyase family protein / Nucleotidyltransferase family protein; K01841 phosphoenolpyruvate phosphomutase [EC:5.4.2.9] ...

Plancke et al., 2014] C. Plancke, H. Vigeolas, R. Hohner, S. Roberty, B. Emonds-Alt, V. Larosa, R. Willamme, F. Duby, D. Onga Dhali, P. Thonart, S. Hiligsmann, F. Franck, G. Eppe, P. Cardol, M. Hippler, and C. Remacle. (2014) Lack of isocitrate lyase in chlamydomonas leads to changes in carbon metabolism and in the response to oxidative stress under mixotrophic growth. Plant J, 77(3):404-417, Feb 2014 ...

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BACKGROUND: The glyoxylate cycle is thought to be present in bacteria, protists, plants, fungi, and nematodes, but not in other Metazoa. However, activity of the glyoxylate cycle enzymes, malate synthase (MS) and isocitrate lyase (ICL), in animal tissues has been reported. In order to clarify the status of the MS and ICL genes in animals and get an insight into their evolution, we undertook a comparative-genomic study. RESULTS: Using sequence similarity searches, we identified MS genes in arthropods, echinoderms, and vertebrates, including platypus and opossum, but not in the numerous sequenced genomes of placental mammals. The regions of the placental mammals genomes expected to code for malate synthase, as determined by comparison of the gene orders in vertebrate genomes, show clear similarity to the opossum MS sequence but contain stop codons, indicating that the MS gene became a pseudogene in placental mammals. By contrast, the ICL gene is undetectable in animals other than the nematodes ...

The level of activity of the NADP-dependent isocitrate dehydrogenase (ICDH) of E. coli ML308 is controlled by a reversible phosphorylation mechanism during growth on acetate as sole carbon source. Under such conditions the enzymes of the glyoxylate bypass, isocitrate lyase (ICL) and malate synthase are induced. This results in competition between ICDH and ICL for the available isocitrate. To allow efficient use of isocitrate via the glyoxylate bypass ICDH is phosphorylated on a single serine residue per subunit which completely inactivates it. Phosphorylation of ICDH is believed to occur at the NADP+ binding site, and so the enzyme is inactive because it cannot bind its cofactor.. ...

In micro-organisms growing on acetate, isocitrate can be metabolized either by the tricarboxylic acid cycle or by the glyoxylate bypass. In Escherichia coli this branch-point is controlled by reversible phosphorylation and inactivation of isocitrate dehydrogenase. Both phosphorylation and dephosphorylation are catalysed by a single bifunctional kinase/phosphatase. The properties of this enzyme suggest that phosphorylation of isocitrate dehydrogenase is controlled by the concentrations of several central metabolites, including isocitrate, the adenine nucleotides and phoenolpyruvate. ...

The regulatory properties of NAD(+)-isocitrate dehydrogenase and oxoglutarate dehydrogenase in extracts of yeast and rat heart mitochondria were studied under identical conditions. Yeast NAD(+)-isocitrate dehydrogenase exhibits a low K0.5 for isocitrate and is activated by AMP and ADP, but is insensitive to ATP and Ca2+. In contrast, the rat heart NAD(+)-isocitrate dehydrogenase was insensitive to AMP, but was activated by ADP and by Ca2+ in the presence of ADP or ATP. Both yeast and rat heart oxoglutarate dehydrogenase were stimulated by ADP, but only the heart enzyme was activated by Ca2+. All the enzymes studied were activated by decreases in pH, but to differing extents. The effects of Ca2+, adenine nucleotides and pH were through K0.5 for isocitrate or 2-oxoglutarate. These observations are discussed with reference to the deduced amino acid sequences of the constituent subunits of the enzymes, where they are available. ...

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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the gamma subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. This gene is a candidate gene for periventricular heterotopia. Several alternatively spliced transcript variants of this gene have been described, but only ...

Gene expression is regulated through a complex interplay of different transcription factors (TFs) which can enhance or inhibit gene transcription. ArcA is a global regulator that regulates genes involved in different metabolic pathways, while IclR as a local regulator, controls the transcription of the glyoxylate pathway genes of the aceBAK operon. This study investigates the physiological and metabolic consequences of arcA and iclR deletions on E. coli K12 MG1655 under glucose abundant and limiting conditions and compares the results with the metabolic characteristics of E. coli BL21 (DE3). The deletion of arcA and iclR results in an increase in the biomass yield both under glucose abundant and limiting conditions, approaching the maximum theoretical yield of 0.65 c-mole/c-mole glucose under glucose abundant conditions. This can be explained by the lower flux through several CO2 producing pathways in the E. coli K12 ΔarcAΔiclR double knockout strain. Due to iclR gene deletion, the glyoxylate pathway

The glyxoylate shunt consists of two enzymes, isocitrate lyase and malate synthase. Its function is generally anaplerotic, meaning that it replenishes TCA cycle intermediates. Isocitrate (one intermediate) becomes succinate (one intermediate) plus glyoxylate. Glyoxylate plus an acetyl group from acetyl-CoA becomes malate, a second intermediate, for a gain of one. Acetyl groups, such as from fatty acid metabolism, by means of this pathway, can provide TCA cycle intermediates for use in amino acid biosynthesis and other biosynthetic pathways ...

Compare Isocitrate Dehydrogenase 3 (NAD ) alpha Isocitrate Dehydrogenase 3 (NAD+) alpha ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.

Involved in the biosynthesis of the exopolysaccharide acetan, a water-soluble polysaccharide involved in production of bacterial cellulose (BC).

Patients with myeloproliferative neoplasms (MPNs) frequently progress to bone marrow failure or acute myeloid leukemia (AML), and mutations in epigenetic regulators such as the metabolic enzyme isocitrate dehydrogenase (IDH) are associated with poor outcomes. Here, we showed that combined expression of Jak2V617F and mutant IDH1R132H or Idh2R140Q induces MPN progression, alters stem/progenitor cell function, and impairs differentiation in mice. Jak2V617F Idh2R140Q-mutant MPNs were sensitive to small-molecule inhibition of IDH. Combined inhibition of JAK2 and IDH2 normalized the stem and progenitor cell compartments in the murine model and reduced disease burden to a greater extent than was seen with JAK inhibition alone. In addition, combined JAK2 and IDH2 inhibitor treatment also reversed aberrant gene expression in MPN stem cells and reversed the metabolite perturbations induced by concurrent JAK2 and IDH2 mutations. Combined JAK2 and IDH2 inhibitor therapy also showed cooperative efficacy in ...

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Such studies are expected to shed light on PD pathogenesis and reveal connections between heritable and sporadic PD.For example, GSTP is an isoform of GST involved in many cellular processes including xenobiotic clearance and apoptosis. These reports suggest that GSTP plays an important role in dopaminergic nerve cell survival.Future studies are necessary to test this hypothesis.Engineered variation in GSH content itself has been associated with neuronal death.Consistent with the hypothesis of altered thioldisulfide homeostasis, glutathionylation of isocitrate dehydrogenase is reported to occur in mouse brains after treatment with MPTP, linking it to a model of PD; and knockdown of isocitrate dehydrogenase expression by siRNA increases susceptibility to apoptotic stimuli. Thus, the enzymatic activity of isocitrate dehydrogenase appears to play an important role in regulating cell survival.Taken together these observations suggest that oxidantinduced deactivation of isocitrate dehydrogenase could ...

nbr:O3I_005215 K00031 isocitrate dehydrogenase [EC:1.1.1.42] , (GenBank) isocitrate dehydrogenase (A) MSKIKVEGTVVELDGDEMTRIIWQFIKDKLIHPYLDVNLEYYDLGIEYRDKTDDQVTIDA AEAIKRHGVGVKCATITPDEARVKEFGLKKMWRSPNGTIRNILGGTIFRAPIIISNVPRL VPGWTKPIIIGRHAFGDQYRATDFKVYQAGTVTVTFTPEDGSEPIQHEVVKMPEDGGVVM GMYNFKNSIIDFARASFNYGLQQNYPVYLSTKNTILKAYDGMFKDTFQDVFDAEFKTQFD AAGLTYEHRLIDDMVASSMKWEGGYVWACKNYDGDVQSDTVAQGFGSLGLMTSVLLTPDG KTCEAEAAHGTVTRHYRQHQQGKPTSTNPIASIFAWTRGLEHRGKLDNTPEVIGFSQTLE DVVIKTVEGGQMTKDLALLVGGDQGYLSTEEFLGALDANLARALR ...

Homo sapiens isocitrate dehydrogenase 3 (NAD+) gamma (IDH3G), nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA. (H00003421-R02) - Products - Abnova

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Get information, facts, and pictures about glyoxylate cycle at Encyclopedia.com. Make research projects and school reports about glyoxylate cycle easy with credible articles from our FREE, online encyclopedia and dictionary.

Toxoplasma gondii belongs to the coccidian-subgroup of the Apicomplexa phylum. The Coccidia are obligate intracellular pathogens that establish infection in their mammalian host via the enteric route. These parasites lack a mitochondrial pyruvate dehydrogenase complex but have preserved the degradation of branched-chain amino acids (BCAA) as a possible pathway to generate acetyl-CoA. Importantly, degradation of leucine, isoleucine and valine could lead to concomitant accumulation of propionyl-CoA, a toxic metabolite that inhibits cell growth. Like fungi and bacteria, the Coccidia possess the complete set of enzymes necessary to metabolize and detoxify propionate by oxidation to pyruvate via the 2-methylcitrate cycle (2-MCC). Phylogenetic analysis provides evidence that the 2-MCC was acquired via horizontal gene transfer. In T. gondii tachyzoites, this pathway is split between the cytosol and the mitochondrion. Although the rate-limiting enzyme 2-methylisocitrate lyase is dispensable for parasite ...

Tuberculosis remains a major threat to human health accounting for 2 million annual deaths worldwide. M. bovis causes TB in cattle which is a serious issue in the UK. Mycobacteria are widely distributed in the environments that are also colonized by free living amoebae. In the present study, free-living amoeba (A. castellanii) has been used to study the genetic factors required for the intracellular survival of M. bovis. Role of region of difference 1 (RD1), isocitrate lyase (Rv0467), ClgR (Rv2745) and the VapC (Rv2548) toxin-antitoxin system was examined for survival in amoebae. While the role of RD1 in mycobacterial survival in amoebae could not be observed, isocitrate lyase and a transcriptional regulator (ClgR) might play some part in survival of M. bovis in A. castellanii. It was found that although the mycobacteria were able to remain inside the amoebae vacuoles, they were unable to control the pH as the vacuoles remained acidic. This is very interesting as it is in contrast to macrophages ...

Glyoxylic acid or oxoacetic acid is an organic compound that is both an aldehyde and a carboxylic acid. It is an intermediate of the glyoxylate cycle, which enables certain organisms to convert fatty acids into carbohydrates.The conjugate base of gloxylic acid is known as glyoxylate. This compound is an intermediate of the glyoxylate cycle, which enables organisms, such as bacteria, fungi and plants to convert fatty acids into carbohydrates. Glyoxylate is the byproduct of the amidation process in biosynthesis of several amidated peptides. The glyoxylate cycle is a metabolic pathway occurring in plants, and several microorganisms, such as E. coli and yeast. (PMID: 16396466 ...

Under the severe glucose limitation at the low dilution rate used here, substantial fluxes through the PEP-glyoxylate cycle were expected (12, 25, 35). The precise regulation mechanism that effectively controlled this major flux rerouting from the TCA cycle to the PEP-glyoxylate cycle, however, was unclear. Based on in vivo flux and in vitro enzyme data on global regulator mutants, we demonstrate that PEP-glyoxylate cycle activity is strongly controlled by induction through the cAMP-CRP complex under the conditions applied. This finding is consistent with the reported increased mRNA and protein levels of PEP carboxykinase and glyoxylate shunt enzymes at a dilution rate of 0.1 h−1, relative to higher growth rates (25). Thus, growth rate-dependent PEP-glyoxylate cycle fluxes under glucose limitation (35) are apparently controlled by the intracellular cAMP level, which is elevated at dilution rates below 0.1 h−1 (32, 37). Strain-dependent differences in fluxes through the PEP-glyoxylate cycle ...

Abcam provides general protocols for Isocitrate Dehydrogenase Assay Kit (Colorimetric) (ab102528). Please download our pdf protocol booklet

STEP 1: Acetyl-CoA (not shown) donates its acetyl group to an oxaloacetate molecule in a condensation reaction that creates a molecule of citrate. One molecule of water is consumed. The CoA molecule floats away to fetch another acetyl group. We are left with a 6-carbon molecule of citrate, which takes us into step two. STEP 2: Aconitase converts citrate into isocitrate using a dehydration reaction that moves the hydroxyl group (OH) from the 3rd carbon to the 4th carbon.. STEP 3: Isocitrate dehydrogenase converts isocitrate into alpha ketoglutarate by severing a C-C bond in isocitrate. This discards a CO2 molecule in a reaction called oxidative decarboxylation. The discarded carbon atom trades its freed-up C-C bond for a C=O double bond in the new CO2, which releases free energy. This energy is used to produce a molecule of NADH from NAD+ through a hydride (H-) transfer to NAD+.. STEP 4: Oxidative decarboxylation is used again to discard another molecule of CO2 and create another molecule of ...

To search by structure, left click in the box below to display the chemdraw toolbar. Then, draw the chemical structure of interest in the box using the toolbar. When your structure is complete, click Search by Name or Search by SMILES to generate the product name or SMILES respectively. This feature will search within the Gelest product database for matching chemical names or SMILES. Note: In cases where Gelest uses alternate chemical names, it may be necessary to search for the product of interest by its CAS#.. ...

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New life-saving treatments for Myeloid | leukemia | isocitrate dehydrogenase in clinical trial on An Efficacy and Safety Study of AG-221 (CC-90007) Versus Conventional Care Regimens in Older Subjects With Late Stage Acute Myeloid Leukemia Harboring an Isocitrate Dehydrogenase 2 Mutation

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1ISO: Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutant.

1. Living systems, their composition and organization 2. Amino acids (properties, determination and reaction) and peptides 3. Proteins (relation between structure and function) 4. Enzymes: Structure, nomenclature, classification into classes 5. Reaction kinetics of enzymatic reactions, regulation of enzyme activity 6. Chemistry of nucleotides and nucleic acids; replication 7. Transcription, translation, and posttranslational modifications 8. Chemistry of lipids. Biomembranes and membrane transport 9. The principles of metabolism and energy conversion; bioenergetics 10. Aerobic and anaerobic respiration, Light phase of photosynthesis 11. Citrate and glyoxylate cycle 12. Chemistry of carbohydrates. Metabolism of Carbohydrates I. 13. Metabolism of Carbohydrates II. Metabolism of lipids. 14. Metabolism of nitrogenous substances ...

Enzyme-reduced coenzyme binary complexes produce previously unreported shifts in the spectrum of the free coenzyme. These shifts give rise to difference spectra which resemble a general environmental change for reduced diphosphopyridine nucleotide (DPNH) in the glutamic dehydrogenase-DPNH complex, and indicate a more specific enzyme-coenzyme interaction for yeast alcohol dehydrogenase-DPNH, isocitrate dehydrogenase-TPNH, and lactic dehydrogenase-DPNH complexes. ...

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The arginine-specific reagent phenylglyoxal inactivated the active, dephosphorylated, form of Escherichia coli isocitrate dehydrogenase rapidly in a pseudo-first-order process. Both NADP+ and NADPH protected the enzyme against inactivation. Phenylglyoxal appeared to react with one arginine residue per subunit, and the extent of the reaction was proportional to the extent of the inactivation. In contrast, the phosphorylated form of isocitrate dehydrogenase did not react detectably with phenylglyoxal. The data indicate that the coenzyme-binding site of isocitrate dehydrogenase contains a reactive arginine residue that is protected by phosphorylation, and are consistent with the hypothesis that phosphorylation of the enzyme occurs close to or at its active site. ...

Isocitrate dehydrogenases (IDHs) convert isocitrate to α-ketoglutarate by oxidative decarboxylation and are thereby involved in multiple metabolic processes. Mutations in the genes encoding IDH1 and IDH2 were first reported in human gliomas in 2008 and later on also identified in a minority of patients with acute myeloid leukemia. The mutations universally affect codons 132 in IDH1 and 172 in IDH2 and result in decreased enzymatic activity. The oncogenic pathway triggered by IDH mutations may involve the activation of hypoxia-inducible factor pathway as well as the acquisition of a novel (gain of enzymatic) function consuming NADPH and generating α-hydroxyglutarate. Most intriguingly, IDH mutations are observed in ∼70-80% of grade II/III gliomas and the majority of secondary glioblastomas, but only 10% of primary glioblastomas, suggesting a different cellular origin of the gliomas, which had previously been viewed as a multistep process of malignant progression. Understanding the oncogenic ...

Classical activation of macrophages (M(LPS+IFNγ)) elicits the expression of inducible nitric oxide synthase (iNOS), generating large amounts of NO and inhibiting mitochondrial respiration. Upregulation of glycolysis and a disrupted tricarboxylic acid (TCA) cycle underpin this switch to a pro-inflammatory phenotype. We show that the NOS cofactor tetrahydrobiopterin (BH4) modulates IL-1β production and key aspects of metabolic remodeling in activated murine macrophages via NO production. Using two complementary genetic models, we reveal that NO modulates levels of the essential TCA cycle metabolites citrate and succinate, as well as the inflammatory mediator itaconate. Furthermore, NO regulates macrophage respiratory function via changes in the abundance of critical N-module subunits in Complex I. However, NO-deficient cells can still upregulate glycolysis despite changes in the abundance of glycolytic intermediates and proteins involved in glucose metabolism. Our findings reveal a fundamental role for

Pro-inflammatory macrophages sustain pyruvate oxidation through pyruvate dehydrogenase for the synthesis of itaconate and to enable cytokine ...

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el-Mansi EM. Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli. FEMS Microbiol Lett. 1998 Sep 15166(2):333-9.PubMed ID9770290 ...

Looking for online definition of glyoxylate in the Medical Dictionary? glyoxylate explanation free. What is glyoxylate? Meaning of glyoxylate medical term. What does glyoxylate mean?

1CW4: Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase.

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Goat polyclonal Isocitrate dehydrogenase antibody validated for WB and tested in Sc. Immunogen corresponding to synthetic peptide

February 17, 2015 - Will Hawkes The way Robin Appel tells it, Maris Otter was lucky to make it to 30, let alone 50. Fewer and fewer farmers were growing it, Appel, a grain merchant, says of the famous barleys plight in 1990. No one was encouraging them to. I asked Paul Robertshaw, production director at Wolverhampton & Dudley Breweries, if... View Article ...

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