An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. It is one of the citric acid cycle enzymes. EC 4.2.1.3.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
A nonmetallic, diatomic gas that is a trace element and member of the halogen family. It is used in dentistry as flouride (FLUORIDES) to prevent dental caries.
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
An enzyme that catalyzes the reversible hydration of fumaric acid to yield L-malic acid. It is one of the citric acid cycle enzymes. EC 4.2.1.2.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
The state of having multiple leiomyomas throughout the body. (Stedman, 25th ed)
A monomeric protein found in liver peroxisomes that contains two enzymatically active domains; an enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase domain, and an (S)-3-hydroxyacyl-CoA dehydrogenase domain. The enzyme is stereospecific with regards to how cis and trans double bonds are metabolized. It is complemented by PEROXISOMAL MULTIFUNCTIONAL PROTEIN-2, which has the opposite stereospecificity.
A bacterial genus of the order ACTINOMYCETALES.
A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
A dimeric protein found in liver peroxisomes that plays an important role in FATTY ACID metabolism and steroid metabolism. The dimer is formed by cleavage of a single protein precursor and contains an enoyl-CoA hydratase-2 domain and a second domain that displays (S)-3-hydroxyacyl-CoA dehydrogenase and 17-beta-estradiol dehydrogenase activities. The enzyme is stereospecific with regards to arrangement of the substrate double bonds and position of the 3-hydroxy group of the reaction intermediate. It is complemented by PEROXISOMAL BIFUNCTIONAL ENZYME, which has the opposite reaction stereospecificity.
A PEROXISOME-specific enzyme that catalyzes the hydration step of the beta-oxidation pathway.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
Tungsten. A metallic element with the atomic symbol W, atomic number 74, and atomic weight 183.85. It is used in many manufacturing applications, including increasing the hardness, toughness, and tensile strength of steel; manufacture of filaments for incandescent light bulbs; and in contact points for automotive and electrical apparatus.
A mitochondrial protein consisting of four alpha-subunits and four beta-subunits. It contains enoyl-CoA hydratase, long-chain-3-hydroxyacyl-CoA dehydrogenase, and acetyl-CoA C-acyltransferase activities and plays an important role in the metabolism of long chain FATTY ACIDS.
Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
A highly poisonous compound used widely in the manufacture of plastics, adhesives and synthetic rubber.
A genus of gram-negative, rod-shaped bacteria able to anaerobically oxidize and degrade toluene.
Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.
Fatty acid biopolymers that are biosynthesized by microbial polyhydroxyalkanoate synthase enzymes. They are being investigated for use as biodegradable polyesters.
The condition of a pattern of malignancies within a family, but not every individual's necessarily having the same neoplasm. Characteristically the tumor tends to occur at an earlier than average age, individuals may have more than one primary tumor, the tumors may be multicentric, usually more than 25 percent of the individuals in direct lineal descent from the proband are affected, and the cancer predisposition in these families behaves as an autosomal dominant trait with about 60 percent penetrance.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A gram-positive organism found in dairy products, fresh and salt water, marine organisms, insects, and decaying organic matter.
A cytosolic carbonic anhydrase isoenzyme primarily expressed in ERYTHROCYTES, vascular endothelial cells, and the gastrointestinal mucosa. EC 4.2.1.-
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A group of PROTEOBACTERIA represented by morphologically diverse, anaerobic sulfidogens. Some members of this group are considered bacterial predators, having bacteriolytic properties.
Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)
Compounds that either share the structure of fibric acid in their molecular arrangement or are considered variants of the fibric acid structure.
A flavoring agent. It is the intermediate product in the two-step bioconversion of ferulic acid to vanillin. (J Biotechnol 1996;50(2-3):107-13).
Compounds based on fumaric acid.
A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis.

Inactivation of both RNA binding and aconitase activities of iron regulatory protein-1 by quinone-induced oxidative stress. (1/505)

Iron regulatory protein-1 (IRP-1) controls the expression of several mRNAs by binding to iron-responsive elements (IREs) in their untranslated regions. In iron-replete cells, a 4Fe-4S cluster converts IRP-1 to cytoplasmic aconitase. IRE binding activity is restored by cluster loss in response to iron starvation, NO, or extracellular H2O2. Here, we study the effects of intracellular quinone-induced oxidative stress on IRP-1. Treatment of murine B6 fibroblasts with menadione sodium bisulfite (MSB), a redox cycling drug, causes a modest activation of IRP-1 to bind to IREs within 15-30 min. However, IRE binding drops to basal levels within 60 min. Surprisingly, a remarkable loss of both IRE binding and aconitase activities of IRP-1 follows treatment with MSB for 1-2 h. These effects do not result from alterations in IRP-1 half-life, can be antagonized by the antioxidant N-acetylcysteine, and regulate IRE-containing mRNAs; the capacity of iron-starved MSB-treated cells to increase transferrin receptor mRNA levels is inhibited, and MSB increases the translation of a human growth hormone indicator mRNA bearing an IRE in its 5'-untranslated region. Nonetheless, MSB inhibits ferritin synthesis. Thus, menadione-induced oxidative stress leads to post-translational inactivation of both genetic and enzymatic functions of IRP-1 by a mechanism that lies beyond the "classical" Fe-S cluster switch and exerts multiple effects on cellular iron metabolism.  (+info)

The aconitase of yeast. IV. Studies on iron and sulfur in yeast aconitase. (2/505)

Chemical analyses were carried out to determine the active components of the crystalline aconitase [EC 4.2.1.3] of Candida lipolytica. The enzyme contained 2 atoms of non-heme iron, 1 atom of labile sulfur, and 6 sulfhydryl groups per molecule. One atom of the non-heme iron was released by the addition of metal-chelating agents such as sodium citrate, sodium nitrilotriacetate (NTA) or sodium ethylenediaminetetraacetate (EDTA) without loss of the enzyme activity. The non-heme iron and labile sulfur were released by the addition of sulfhydryl reagents such as rho-chloromercuribenzoate (PCMB), sodium mersalyl or urea with loss of the enzyme activity. o-Phenanthroline reacted with the iron atoms in the enzyme at pH 6.0 with loss of the activity. These results show that yeast aconitase is an iron-sulfur protein and that only one of the two non-heme iron atoms is essential for enzyme activity.  (+info)

The aconitase of yeast. V. The reconstitution of yeast aconitase. (3/505)

The apoenzyme of yeast aconitase [EC 4.2.1.3] was prepared by treatment of yeast aconitase with sodium mersalyl, followed by passage by passage of the reaction mixture through a column of Dowex A-1 and gel filtration on Sephadex G-25. The apoenzyme had no aconitase activity, but the active enzyme could be reconstituted by treatment of the apoenzyme with ferrous ions and sodium sulfide in the presence of 2-mercapto-ethanol. The reconstituted active enzyme was isolated by DEAE-Sephadex A-50 column chromatography and Sephadex G-100 gel filtration from the reaction mixture. The reconstituted enzyme was identical with the original untreated enzyme in terms of specific activity, iron content and spectral characteristics, but not in terms of labile sulfur content. A significant difference in visible spectra between the holo- and apoenzymes appeared to be due to the difference in iron and labile sulfur contents between the two proteins.  (+info)

Population structure and genetic divergence in Anopheles nuneztovari (Diptera: Culicidae) from Brazil and Colombia. (4/505)

Anopheles nuneztovari is considered an important vector of human malaria in several localities in Venezuela and Colombia. Its status as a vector of human malaria is still unresolved in areas of the Brazilian Amazon, in spite of have been found infected with Plasmodium sp.. For a better understanding of the genetic differentiation of populations of A. nuneztovari, electrophoretic analysis using 11 enzymes was performed on four populations from Brazil and two from Colombia. The results showed a strong differentiation for two loci: alpha-glycerophosphate dehydrogenase (alpha-Gpd) and malate dehydrogenase (Mdh) from 16 loci analyzed. Diagnostic loci were not detected. The populations of A. nuneztovari from the Brazilian Amazon showed little genetic structure and low geographic differentiation, based on the F(IS) (0.029), F(ST) (0.070), and genetic distance (0.001-0.032) values. The results of the isozyme analysis do not coincide with the indication of two lineages in the Amazon Basin by analysis of mitochondrial DNA, suggesting that this evolutionary event is recent. The mean F(ST) value (0.324) suggests that there is considerable genetic divergence among populations from the Brazilian Amazon and Colombia. The genetic distance among populations from the Brazilian Amazon and Colombia is ranges from 0.047 to 0.148, with the highest values between the Brazilian Amazon and Sitronela (SIT) (0.125-0.148). These results are consistent with those observed among members of anopheline species complexes. It is suggested that geographic isolation has reduced the gene flow, resulting in the genetic divergence of the SIT population. Dendrogram analysis showed three large groups: one Amazonian and two Colombia, indicating some genetic structuring. The present study is important because it attempted to clarify the taxonomic status of A. nuneztovari and provide a better understanding of the role of this mosquito in transmission of human malaria in northern South America.  (+info)

Human cytoplasmic aconitase (Iron regulatory protein 1) is converted into its [3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding. (5/505)

Iron regulatory protein 1 (IRP1) regulates the synthesis of proteins involved in iron homeostasis by binding to iron-responsive elements (IREs) of messenger RNA. IRP1 is a cytoplasmic aconitase when it contains a [4Fe-4S] cluster and an RNA-binding protein after complete removal of the metal center by an unknown mechanism. Human IRP1, obtained as the pure recombinant [4Fe-4S] form, is an enzyme as efficient toward cis-aconitate as the homologous mitochondrial aconitase. The aconitase activity of IRP1 is rapidly lost by reaction with hydrogen peroxide as the [4Fe-4S] cluster is quantitatively converted into the [3Fe-4S] form with release of a single ferrous ion per molecule. The IRE binding capacity of IRP1 is not elicited with H(2)O(2). Ferrous sulfate (but not other more tightly coordinated ferrous ions, such as the complex with ethylenediamine tetraacetic acid) counteracts the inhibitory action of hydrogen peroxide on cytoplasmic aconitase, probably by replenishing iron at the active site. These results cast doubt on the ability of reactive oxygen species to directly increase IRP1 binding to IRE and support a signaling role for hydrogen peroxide in the posttranscriptional control of proteins involved in iron homeostasis in vivo.  (+info)

Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. (6/505)

Deletion of the yeast frataxin homologue, YFH1, elicits accumulation of iron in mitochondria and mitochondrial defects. We report here that in the presence of an iron chelator in the culture medium, the concentration of iron in mitochondria is the same in wild-type and YFH1 deletant strains. Under these conditions, the activity of the respiratory complexes is restored. However, the activity of the mitochondrial aconitase, a 4Fe-4S cluster-containing protein, remains low. The frataxin family bears homology to a bacterial protein family which confers resistance to tellurium, a metal closely related to sulfur. Yfh1p might control the synthesis of iron-sulfur clusters in mitochondria.  (+info)

Bacillus subtilis aconitase is an RNA-binding protein. (7/505)

The aconitase protein of Bacillus subtilis was able to bind specifically to sequences resembling the iron response elements (IREs) found in eukaryotic mRNAs. The sequences bound include the rabbit ferritin IRE and IRE-like sequences in the B. subtilis operons that encode the major cytochrome oxidase and an iron uptake system. IRE binding activity was affected by the availability of iron both in vivo and in vitro. In eukaryotic cells, aconitase-like proteins regulate translation and stability of iron metabolism mRNAs in response to iron availability. A mutant strain of B. subtilis that produces an enzymatically inactive aconitase that was still able to bind RNA sporulated 40x more efficiently than did an aconitase null mutant, suggesting that a nonenzymatic activity of aconitase is important for sporulation. The results support the idea that bacterial aconitases, like their eukaryotic homologs, are bifunctional proteins, showing aconitase activity in the presence of iron and RNA binding activity when cells are iron-deprived.  (+info)

Iron-dependent regulation of transferrin receptor expression in Trypanosoma brucei. (8/505)

Transferrin is an essential growth factor for African trypanosomes. Here we show that expression of the trypanosomal transferrin receptor, which bears no structural similarity with mammalian transferrin receptors, is regulated by iron availability. Iron depletion of bloodstream forms of Trypanosoma brucei with the iron chelator deferoxamine resulted in a 3-fold up-regulation of the transferrin receptor and a 3-fold increase of the transferrin uptake rate. The abundance of expression site associated gene product 6 (ESAG6) mRNA, which encodes one of the two subunits of the trypanosome transferrin receptor, is regulated 5-fold by a post-transcriptional mechanism. In mammalian cells the stability of transferrin receptor mRNA is controlled by iron regulatory proteins (IRPs) binding to iron-responsive elements (IREs) in the 3'-untranslated region (UTR). Therefore, the role of a T. brucei cytoplasmic aconitase (TbACO) that is highly related to mammalian IRP-1 was investigated. Iron regulation of the transferrin receptor was found to be unaffected in Deltaaco::NEO/Deltaaco::HYG null mutants generated by targeted disruption of the TbACO gene. Thus, the mechanism of post-transcriptional transferrin receptor regulation in trypanosomes appears to be distinct from the IRE/IRP paradigm. The transferrin uptake rate was also increased when trypanosomes were transferred from medium supplemented with foetal bovine serum to medium supplemented with sera from other vertebrates. Due to varying binding affinities of the trypanosomal transferrin receptor for transferrins of different species, serum change can result in iron starvation. Thus, regulation of transferrin receptor expression may be a fast compensatory mechanism upon transmission of the parasite to a new host species.  (+info)

Abstract Burn injury causes a major systemic catabolic response that is associated with mitochondrial dysfunction in skeletal muscle. We investigated the effects of the mitochondria-targeted peptide antioxidant Szeto-Schiller 31 (SS-31) on skeletal muscle in a mouse burn model using in vivo phosphorus-31 nuclear magnetic resonance ((31)P NMR) spectroscopy to noninvasively measure high-energy phosphate levels; mitochondrial aconitase activity measurements that directly correlate with TCA cycle flux, as measured by gas chromatography mass spectrometry (GC-MS); and electron paramagnetic resonance (EPR) to assess oxidative stress. At 6 h postburn, the oxidative ATP synthesis rate was increased 5-fold in burned mice given a single dose of SS-31 relative to untreated burned mice (P=0.002). Furthermore, SS-31 administration in burned animals decreased mitochondrial aconitase activity back to control levels. EPR revealed a recovery in redox status of the SS-31-treated burn group compared to the ...
Most common neurodegenerative disorders likely result from complex interactions between genetic and environmental risk factors (Farrer et al., 1997; Munoz and Feldman, 2000; Lindsay et al., 2002). One such factor may be aging-related alterations in the redox state of mitochondria (Hirai et al., 2001; Eckert et al., 2003; Beal, 2005) Our study shows that partial reduction in the main mitochondrial superoxide scavenger Sod2 accelerates the onset of hAPP/Aβ-dependent behavioral abnormalities and worsens a range of AD-related molecular and pathological alterations.. How might Sod2 reduction modulate the phenotype of hAPP mice or AD? An obvious mechanism is increased mitochondrial levels of superoxide radicals and resultant oxidative damage. To assess this possibility, we measured mitochondrial aconitase activity, a well-established mitochondrial sensor of superoxide that is lower in the heart and liver of adult Sod2+/− mice than in Sod2+/+ controls (Williams et al., 1998; Van Remmen et al., ...
Most common neurodegenerative disorders likely result from complex interactions between genetic and environmental risk factors (Farrer et al., 1997; Munoz and Feldman, 2000; Lindsay et al., 2002). One such factor may be aging-related alterations in the redox state of mitochondria (Hirai et al., 2001; Eckert et al., 2003; Beal, 2005) Our study shows that partial reduction in the main mitochondrial superoxide scavenger Sod2 accelerates the onset of hAPP/Aβ-dependent behavioral abnormalities and worsens a range of AD-related molecular and pathological alterations.. How might Sod2 reduction modulate the phenotype of hAPP mice or AD? An obvious mechanism is increased mitochondrial levels of superoxide radicals and resultant oxidative damage. To assess this possibility, we measured mitochondrial aconitase activity, a well-established mitochondrial sensor of superoxide that is lower in the heart and liver of adult Sod2+/− mice than in Sod2+/+ controls (Williams et al., 1998; Van Remmen et al., ...
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5UTR of ferritin, and delta ...
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5UTR of ferritin, and delta ...
Dietitians for men provide expert nutrition and dietary advice to men on how to stay healthy. Read on to learn more on dietitians for men in Macon, GA and get access to healthy diets, supplements for men, dietary intake, weight management, and advice on dietary changes, as well as content on how good nutrition can help boost male fertility.
District Business Office: 660-395-6164. Macon Elementary: 660-385-2118. Macon Middle School: 660-385-2189. Macon High School: 660-385-5748. Macon Career Center: 660-385-2158 ...
District Business Office: 660-395-6164. Macon Elementary: 660-385-2118. Macon Middle School: 660-385-2189. Macon High School: 660-385-5748. Macon Career Center: 660-385-2158 ...
District Business Office: 660-395-6164. Macon Elementary: 660-385-2118. Macon Middle School: 660-385-2189. Macon High School: 660-385-5748. Macon Career Center: 660-385-2158 ...
Looking for aconitase? Find out information about aconitase. An enzyme involved in the Krebs citric acid cycle that catalyzes the breakdown of citric acid to cis -aconitic and isocitric acids Explanation of aconitase
On January 16, 1997, the National Institute for Occupational Safety and Health (NIOSH) received an employee request for a health hazard evaluation (HHE) at the Macon County government facilities in Macon, Missouri, NIOSH was asked to determine if health problems experienced by some building occupants were related to exposure to residual pesticide contamination in Buildings 1 (main courthouse) and
Peroxyni trite also disrupts the ferrous sulfur lively internet site in the tri carboxylic acid cycle enzyme aconitase, resulting in ARQ 197 cell in vivo in vi
Metabolic enzyme. Molecular model of the enzyme aconitase, which is involved in the citric acid (or Krebs) cycle. The citric acid cycle is the process by which mitochondria convert glucose to energy. - Stock Image F009/5998
Macon County Schools is in the process of reviewing its website to ensure compliance with Section 504 of the Rehabilitation Act and Title II of the Americans with Disabilities Act. If you have questions or concerns regarding the accessibility of the website or if you are unable to access a page or document on the website, you may contact the Technology Department via email at [email protected] ...
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p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
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Local social organizations explored the possible link between poverty and human trafficking at a public forum Monday night in Decatur.The organization, Set Free Movement, hosted a 5-person panel and said the realization that poverty is throughout the state
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Communicated by Helmut Beinert, University of Wisconsin, Madison, WI, June 16, 2004 (received for review April 14, 2004) ArticleFigures SIInfo lane 2, WT; lane 3, S711A; lane 4, S711D; lane 5, S711E; lane 6, S711T. Rate of Conversion of Cit
Aconitase 1 antibody (aconitase 1) for IHC-P, WB. Anti-Aconitase 1 pAb (GTX64472) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Quantitative 1-mL UV/Vis spectrophotometric assay detection method, kit sufficient for 100 assays, ready-to-use, quick protocol, ultrahigh accuracy, hypersensitive, reliable, and consistent
マウス・モノクローナル抗体 ab110321 交差種: Ms,Rat,Hu 適用: WB,IP,IHC-P,IHC-Fr,Flow Cyt,ICC/IF,In-Cell ELISA…Aconitase…
TY - JOUR. T1 - The interaction between the iron-responsive element binding protein and its cognate rna is highly dependent upon both RNA sequence and structure. AU - Jaffrey, Samie R.. AU - Haile, David J.. AU - Klausner, Richard D.. AU - Harford, Joe B.. PY - 1993/9/25. Y1 - 1993/9/25. N2 - To assess the influence of RNA sequence2.urule;structure on the interaction RNAs with the iron-responsive element binding protein (IRE-BP), twenty eight altered RNAs were tested as competitors for an RNA corresponding to the ferritin H chain IRE. All changes in the loop of the predicted IRE hairpin and in the unpaired cytosine residue characteristically found in IRE stems significantly decreased the apparent affinity of the RNA for the IRE-BP. Similarly, alteration in the spacing and2.urule;or orientation of the loop and the unpaired cytosine of the stem by either increasing or decreasing the number of base pairs separating them significantly reduced efficacy as a competitor. It is inferred that the IRE-BP ...
The iron-responsive element-binding proteins, also known as IRE-BP, IRBP, IRP and IFR , bind to iron-responsive elements (IREs) in the regulation of human iron metabolism. ACO1, or IRP1, is a bifunctional protein that functions as an iron-responsive element (IRE)-binding protein involved in the control of iron metabolism by binding mRNA to repress translation or degradation. It functions also as the cytoplasmic isoform of aconitase. Aconitases are iron-sulfur proteins that require a 4Fe-4S cluster for their enzymatic activity, in which they catalyze conversion of citrate to isocitrate. This structure was based on x-ray crystal diffraction. The resolution was 2.80 Å. This protein was harvested from the species Oryctolagus cuniculus, or more commonly known as a rabbit. This protein has a couple conformational changes associated with it to explain the alternative functions as either mRNA regulator or as an enzyme. This informations was obtained from the RCSB protein data bank website. IRP2 is less ...
aconitate hydratase/ copper ion binding; FUNCTIONS IN: aconitate hydratase activity, copper ion binding; INVOLVED IN: response to cadmium ion; LOCATED IN: mitochondrion, chloroplast; EXPRESSED IN: 25 plant structures; EXPRESSED DURING: 16 growth stages; CONTAINS InterPro DOMAIN/s: Aconitase family, 4Fe-4S cluster binding site (InterPro:IPR018136), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha (InterPro:IPR001030), Aconitase A/isopropylmalate dehydratase small subunit, swivel (InterPro:IPR000573), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomain 2 (InterPro:IPR015932), Aconitase/Iron regulatory protein 2/2-methylisocitrate dehydratase (InterPro:IPR015934), Aconitase-like core (InterPro:IPR015937), Aconitase/3-isopropylmalate dehydratase, swivel (InterPro:IPR015928), Aconitase/iron regulatory protein 2 (InterPro:IPR006249), Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha, subdomains 1 and 3 (InterPro:IPR015931); ...
Parasites as an Alternative Model for Lipid Metabolism: Gene Expression Analysis of an Oyster Parasite Perkinsus marinus during Lipid Starvation.. Our laboratory is interested in understanding the regulation of fatty acid biosynthesis in Perkinsus marinus. Previous work has shown that this parasite is capable of synthesizing its own fatty acids, a property that is unique among parasites that usually require the acquisition of certain essential fatty acids from their host. Fatty acid synthesis occurs in the cytosol from Acetyl CoA, which is derived from carbohydrate metabolism via citrate. In the cytosol, citrate can be cleaved into oxaloacetate and Acetyl CoA, or be converted to isocitrate by cytosolic aconitase. We are investigating the role of cytosolic aconitase as a potential branch point in this process, as we have evidence for phosphorylation of this enzyme in favoring citrate production. No one to our knowledge has delineated the role of cytosolic aconitase in fatty acid biosynthesis. We ...
The ACO1 gene, encoding mitochondrial aconitase of Saccharomyces cerevisiae, is required both for oxidative metabolism and for glutamate prototrophy. This gene is subject to catabolite repression; the ACO1 mRNA level is further reduced when glutamate is supplied with glucose. To further explore regulation of ACO1 expression, we have screened for mutations that reduce expression of an ACO1-lacZ fusion borne on a multicopy vector. We identified a gene required for wild-type expression of ACO1 only under catabolite repression conditions. Sequencing of the corresponding cloned gene revealed that it is identical to RTG2 previously cloned as a pivotal gene in controlling interorganelle retrograde communication. Cells containing either the original rtg2-2 mutation or a null rtg2 allele are not petite but show a residual growth on minimum glucose medium with ammonium sulfate as the sole nitrogen source. This growth defect is partially restored by supplying aspartate or threonine, and fully with ...
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Dr. James Lennon, DO is a medical oncology specialist in Macon, GA. He currently practices at Georgia Cancer Specialists and is affiliated with Coliseum Medical Centers. He accepts multiple insurance plans. Dr. Lennon is board certified in Hematology.
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This requires not only cyymbalta of the activity of the glycolytic and citric acid cycle enzymes, but also adequate oxygen and glucose delivery. 89266в270.
Chern Lim, S., Friemel, M., Marum, J.E., Tucker, E.J., Bruno, D.L., Riley, L.G., Christodoulou, J., Kirk, E.P., Boneh, A., DeGennaro, Ch.M., Springer, M., Mootha, V.K., Rouault, T.A., Leimkühler, S., Thorburn, D.R., Compton, A.G. (2013) Mutations in LYRM4, encoding iron-sulfur cluster biogenesis factor ISD11, cause, deficiency of multiple respiratory chain complexes. Human Molecular Genetics, 1-14, doi:10.1093/hmg/ ...
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_1246 (SAUSA300_RS06765); symbol: citB; product: aconitate hydratase
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The tech said that she was fairly confident that this would turn out to be nothing. And that most of the time, these cysts are gone by 32 weeks. She said that she doesnt seem them weekly, or even monthly, but that theyre not crazy uncommon. After talking with her, she took us to see Vickie for the rest of our appointment. Usually I ONLY see Marie, but she left sick that day, so Vickie was taking her appointments. Ive never met Vickie before. And under a normal visit, I might like her. But I was NOT impressed at this visit. Basically, she told us NOTHING. We learned more from the ultrasound tech than we did from her. She barely said anything to us at all and was not informative or comforting. They do want to refer us to Macon to see a specialist for a level 2 ultrasound. This will give us just a better idea of whats going on in there with Baby C. That appointment has been scheduled and we will be going to Macon on February 20th at 1:30. PLEASE keep this appointment and Baby C in your prayers. ...
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Things are still going well with Karis but she has hit a minor bump in the road. Heres the good news: she has come COMPLETELY off of oxygen and her breathing is doing much better! They have also removed the feeding tube from her throat and replaced it with one through her nose that wont gag and aggravate her. Less than good news: shes not progressing quite as quickly as the doctor would like to see. She is still retracting a little when she breathes and the second set of x-rays still show some stuff in her lungs. She also has something going on with her bowels that could be causing some stomach problems and preventing her from digesting her milk like she should. Because of these things, the doctor is keeping her in the nursery another day and feeding her only through IV - no nursing with her mom or even getting milk through the tube. The doctor has consulted with another doctor at the NICU in Macon and they feel that its best to give her another day to move things along through her ...
Over the past week or so, it seems the discussion has heated up over who can and should--and has to be--included in the formation of an accountable care organization (ACO), FiercePracticeManagment
... (aconitate hydratase; EC 4.2.1.3) is an enzyme that catalyses the stereo-specific isomerization of citrate to ... One theory is that, in the rate-limiting step of the mechanism, the cis-aconitate is released from the enzyme, then reattached ... Another hypothesis is that cis-aconitate stays bound to the enzyme while it flips from the citrate to the isocitrate mode. In ... PDB: 1ACO​; Lauble, H; Kennedy, MC; Beinert, H; Stout, CD (1994). "Crystal Structures of Aconitase with Trans-aconitate and ...
The enzymes missing from the TCA cycle are citrate synthase, aconitate hydratase, and isocitrate dehydrogenase. Haemophilus ...
Fluorocitrate can inhibit aconitate hydratase, which is needed for the conversion of citrate, by competitive inhibition. This ...
... aconitate hydratase MeSH D08.811.520.241.300.050.500 - iron regulatory protein 1 MeSH D08.811.520.241.300.050.750 - iron ... enoyl-coa hydratase MeSH D08.811.520.241.300.300 - fumarate hydratase MeSH D08.811.520.241.300.500 - phosphopyruvate hydratase ... urocanate hydratase MeSH D08.811.520.241.300.950 - uroporphyrinogen iii synthetase MeSH D08.811.520.241.700 - polysaccharide- ...
... aconitate hydratase EC 4.2.1.4: Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase EC 4.2.1.5: ... 2-hydratase EC 4.2.1.132: 2-hydroxyhexa-2,4-dienoate hydratase EC 4.2.1.133: copal-8-ol diphosphate hydratase EC 4.2.1.134: ... 4-oxalmesaconate hydratase EC 4.2.1.84: nitrile hydratase EC 4.2.1.85: dimethylmaleate hydratase EC 4.2.1.86: identical to EC ... 2-methylfumaryl-CoA hydratase * EC 4.2.1.149: crotonobetainyl-CoA hydratase * EC 4.2.1.150: short-chain-enoyl-CoA hydratase * ...
... citrate with aconitase in the presence of 2-methyl-cis-aconitate. This reaction produced both unlabeled cis-aconitate and 2- ... Isotope scrambling experiments using tritium, deuterium, and 18O were carried out on the aconitase hydratase reaction by I.A. ...
See EC 4.2.1.133, copal-8-ol diphosphate hydratase EC 5.5.1.22: (-)-bornyl diphosphate synthase * EC 5.5.1.23: aklanonic acid ... aconitate Δ-isomerase EC 5.3.3.8: Δ3-Δ2-enoyl-CoA isomerase EC 5.3.3.9: prostaglandin-A1 Δ-isomerase EC 5.3.3.10: 5- ...
... trans-aconitate 2-methyltransferase EC 2.1.1.145: trans-aconitate 3-methyltransferase EC 2.1.1.146: (iso)eugenol O- ... lycopene elongase/hydratase (flavuxanthin-forming) EC 2.5.1.150: lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin- ...
Deficiency of aconitate hydratase (disorder). Code System Preferred Concept Name. Deficiency of aconitate hydratase (disorder) ...
Aconitate hydratase mitochondrial. EgrG_000158240.1. 0,00365168. 0. -. -. Succinate dehydrogenase ubiquinone. EgrG_000422600.1 ... Aconitate hydratase mitochondrial; and 7) Succinate dehydrogenase ubiquinone.. A functional annotation of the NSPs is presented ...
Aconitate delta-isomerase (substance) {44125002 , SNOMED-CT } Aconitate hydratase (substance) {54239002 , SNOMED-CT } Adenosine ... hydratase (substance) {78400000 , SNOMED-CT } Cyanamide hydratase (substance) {10914009 , SNOMED-CT } Cyanide hydratase ( ... Acetylenecarboxylate hydratase (substance) {20371000 , SNOMED-CT } Acetylenedicarboxylate hydratase (substance) {53468009 , ... Enoyl-CoA hydratase (substance) {87504000 , SNOMED-CT } Enzyme variant (substance) {340005 , SNOMED-CT } Epimerase (substance ...
Aconitate decarboxylase (substance) {112056001 , SNOMED-CT } Aconitate hydratase (substance) {54239002 , SNOMED-CT } Adenosine ... Cyanamide hydratase (substance) {10914009 , SNOMED-CT } Cyanate hydrolase (substance) {83342006 , SNOMED-CT } Cyanide hydratase ... Crotonobetainyl-CoA hydratase (substance) {785897001 , SNOMED-CT } Crotonoyl-[acyl-carrier-protein] hydratase (substance) { ... Isohexenylglutaconyl-coenzyme A hydratase (substance) {51880001 , SNOMED-CT } Itaconyl-coenzyme A hydratase (substance) { ...
Deficiency of aconitate hydratase (disorder) {124617006 , SNOMED-CT } Deficiency of acylphosphatase (disorder) {124533003 , ... Deficiency of fumarate hydratase (disorder) {124616002 , SNOMED-CT } Deficiency of fumarylacetoacetase (disorder) {124536006 , ... Deficiency of methylglutaconyl-coenzyme A hydratase (disorder) {124622006 , SNOMED-CT } Deficiency of methylmalonyl-coenzyme A ... Deficiency of enoyl-coenzyme A hydratase (disorder) {124621004 , SNOMED-CT } Deficiency of enteropeptidase (disorder) { ...
Aconitate hydratase (substance). Code System Preferred Concept Name. Aconitate hydratase (substance). Concept Status. Published ...
dbr:Aconitate_decarboxylase. *dbr:Felinine. *dbr:Crotonoyl-(acyl-carrier-protein)_hydratase. *dbr:Diaminobutyrate_decarboxylase ...
... which is promptly dehydrated and re-hydrated to isocitrate thanks to the action of the aconitate hydratase. This hydration/ ... critical hydration step during the TCA cycle is the reverse conversion of fumarate to L-malate catalyzed by fumarate hydratase. ...
FTO D6D XBP1 OGT NQO ADP-ribosyltransferase ERAP LRH-1 PASK PME-NMT PDE-NMT PEPCK Cardiolipin Peroxidase Aconitate hydratase ... Thrombin Transferase VD/VDR Xanthine Oxidase ACMSD Arginase ATP synthase Cholesterol Transporter CYP51 Fumarate hydratase ...
Align aconitate hydratase (EC 4.2.1.3) (characterized) to candidate PfGW456L13_3378 Aconitate hydratase 2 (EC 4.2.1.3) @ 2- ... Query= BRENDA::P36683 (865 letters) >lcl,FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3378 Aconitate hydratase 2 (EC 4.2.1.3 ...
aconitate hydratase Agriculture & Biology 33% View full fingerprint Cite this. * APA * Standard ...
FTO D6D XBP1 OGT NQO ADP-ribosyltransferase ERAP LRH-1 PASK PME-NMT PDE-NMT PEPCK Cardiolipin Peroxidase Aconitate hydratase ... Thrombin Transferase VD/VDR Xanthine Oxidase ACMSD Arginase ATP synthase Cholesterol Transporter CYP51 Fumarate hydratase ...
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase YP_002268725 unclonable 0.0000016622 normal 1 Escherichia ...
Aconitate hydratase (Aconitase) (EC 4.2.1.3). 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO: ...
4.2.1.117 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) 4.2.1.3 aconitate hydratase - - ... 4.2.1.119 enoyl-CoA hydratase 2 4.2.1.150 short-chain-enoyl-CoA hydratase 4.2.1.17 enoyl-CoA hydratase 4.2.1.55 3- ... 4.2.1.148 2-methylfumaryl-CoA hydratase 4.2.1.153 3-methylfumaryl-CoA hydratase - - ... 4.2.1.2 fumarate hydratase 4.2.1.32 L(+)-tartrate dehydratase 4.2.1.34 (S)-2-methylmalate dehydratase 4.2.1.81 D(-)-tartrate ...
Aconitate hydratase 2. 76. SEQF2580,ANNF01000038.1. ERJ21133.1 jb [NA] [AA] 747/248. 10146-10892. hypothetical protein. ...
4.2.1.117 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) 4.2.1.3 aconitate hydratase - - ... 4.2.1.148 2-methylfumaryl-CoA hydratase 4.2.1.153 3-methylfumaryl-CoA hydratase - - ...
4.2.1.117 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) 4.2.1.3 aconitate hydratase - - ...
PDB Compounds: (A:) aconitate hydratase. SCOPe Domain Sequences for d1b0ja2:. Sequence; same for both SEQRES and ATOM records ...
Aconitase (aconitate hydratase; EC 4.2.1.3) is an enzyme that catalyses the stereo-specific isomerization of citrate to ... One theory is that, in the rate-limiting step of the mechanism, the cis-aconitate is released from the enzyme, then reattached ... Another hypothesis is that cis-aconitate stays bound to the enzyme while it flips from the citrate to the isocitrate mode. In ... PDB: 1ACO​; Lauble, H; Kennedy, MC; Beinert, H; Stout, CD (1994). "Crystal Structures of Aconitase with Trans-aconitate and ...
PDB Compounds: (A:) aconitate hydratase. SCOPe Domain Sequences for d1b0ja2:. Sequence; same for both SEQRES and ATOM records ...
Aconitate Hydratase Preferred Term Term UI T000440. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1973). ... Aconitate Hydratase Preferred Concept UI. M0000233. Registry Number. EC 4.2.1.3. Related Numbers. 9024-25-3. Scope Note. An ... Aconitate Hydratase [D08.811.520.241.300.050] * Iron Regulatory Protein 1 [D08.811.520.241.300.050.500] ... Aconitate Hydratase. Tree Number(s). D08.811.520.241.300.050. Unique ID. D000154. RDF Unique Identifier. http://id.nlm.nih.gov/ ...
At4g35830.1 68411.m04626 aconitate hydratase (citrate hydro-lyase/aconitase/ACO) [cytoplasmic] identical to SP,Q42560.... ... At4g26970.1 68411.m03533 aconitate hydratase (citrate hydro-lyase/aconitase) [cytoplasmic], putative strong similarit.... ... At2g05710.1 68409.m00546 aconitate hydratase (citrate hydro-lyase/aconitase) [cytoplasmic], putative nearly identical.... ... At4g13430.1 68411.m01898 aconitase family contains Pfam profile PF00330: Aconitase family (aconitate hydratase ...
Aconitate hydratase mitochondrial. EgrG_000158240.1. 0,00365168. 0. -. -. Succinate dehydrogenase ubiquinone. EgrG_000422600.1 ... Aconitate hydratase mitochondrial; and 7) Succinate dehydrogenase ubiquinone.. A functional annotation of the NSPs is presented ...
Aconitate hydratase (Aconitase) (EC 4.2.1.3). 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO: ... Other DEPs of ferredoxin I, superoxide dismutase and aconitatehydratase were identified to be related to the Glyoxylate and ... A peptide of aconitatehydratase (aconitase, ACO), which is related to the glyoxylate and dicarboxylate metabolism (ko00630), ... pyruvate kinase I and aconitatehydratase peptides were changed during the degumming of kanef bast. These findings provide ...
Aconitate hydratase A. 97. SEQF2940,KI515728.1. SEQF2940_00100 jb [NA] [AA] 576/191. 99827-100402. HTH-type transcriptional ...
Aconitate hydratase (substance). Code System Preferred Concept Name. Aconitate hydratase (substance). Concept Status. Published ...
Aconitate HydrataseCandidaCitrate (si)-SynthaseCitratesIsocitrate DehydrogenaseIsocitrate LyaseIsocitratesSpecies Specificity ... The activities of the enzymes citrate synthase, aconitate hydratase, isocitrate dehydrogenase and isocitrate lyase in cell ... aconitate hydratase, isocitrate dehydrogenase and isocitrate lyase in cell homogenates of n-paraffin grown citrate plus ...
Aconitate hydratase 2. 76. SEQF2580,ANNF01000038.1. ERJ21133.1 jb [NA] [AA] 747/248. 10146-10892. hypothetical protein. ...
... which is promptly dehydrated and re-hydrated to isocitrate thanks to the action of the aconitate hydratase. This hydration/ ... critical hydration step during the TCA cycle is the reverse conversion of fumarate to L-malate catalyzed by fumarate hydratase. ...
... aconitate hydratase; citC, citrate dehydrogenase; citG, fumarate hydratase; citZ, citrate synthase; eno, enolase; fbpA, ... In the presence of glucose, CcpA repressed several genes of the TCA cycle, including aconitate hydratase (citB), isocitrate ...
Molecular Function:iron ion binding; 4 iron, 4 sulfur cluster binding; aconitate hydratase activity; 3 iron, 4 sulfur cluster ... It is an enzyme that catalyzes the interconversion of citrate to isocitrate via cis-aconitate in the second step of the TCA ... ACO2 (Aconitase 2) is an enzyme that catalyzes the interconversion of citrate to isocitrate via cis-aconitate in the second ... ACO2: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Monomer. Belongs to the aconitase/IPM isomerase ...
Aconitate Hydratase Medicine & Life Sciences 59% * Genes Medicine & Life Sciences 32% * Growth Medicine & Life Sciences 30% ...
Aconitate hydratase 163 25 0.043 Cytoplasm Up Up Storage substance biosynthesis G10 Sucrose synthase type 2 809 31 0.002 ...
Trans-aconitate salts appear to be excreted readily by the kidneys. There is no direct evidence that trans-aconitic acid is ...
aconitate hydratase. 3-isopropylmalate dehydratase small subunit; EC 4.2.1.33; Alpha-IPM isomerase; IPMI; Isopropylmalate ... Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate ... Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99. 72%. 1302.7. ...
... by inhibiting aconitate hydratase (EC 4.2.1.3), interrupts the synthesis of the 2-oxoglutarate required for the assimilation of ...
aconitate hydratase-related / citrate hydro-lyase-related / aconitase-related. F:molecular_function unknown;P:metabolic process ...
aconitate hydratase activity. IEP. Enrichment. MF. GO:0004356. glutamate-ammonia ligase activity. IEP. Enrichment. ...
Aconitate hydratase, mitochondrial (4) * UTP--glucose-1-phosphate uridylyltransferase (4) * Isocitrate lyase (4) ...
aconitate hydratase 1 (NCBI). 97, 160. GSU1031. GSU1031. hypothetical protein (VIMSS). 14, 337. ...
ACO2 Aconitate hydratase, mitochondrial precursor (Aconitase). Prabakaran et al. (2004). Beasley et al. (2006). Martins-de- ... Tagged: Aconitate, ATP Synthase, ATP5A1, ATP5A1 ATP synthase, ATP6V1A, ATPase, Carbonic Anhydrase 2, Creatine kinase, Fructose ...
Iijima, H., Watanabe, A., Sukigara, H., Iwazumi, K., Shirai, T., Kondo, A. & Osanai, T., May 2021, In: Metabolic Engineering. 65, p. 88-98 11 p.. Research output: Contribution to journal › Article › peer-review ...
Aconitate hydratase, mitochondrial (4) * UTP--glucose-1-phosphate uridylyltransferase (4) * Isocitrate lyase (4) ...
aconitate hydratase 1 (RefSeq). 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) (EC 4.2.1.117) (characterized). ... Aconitate hydratase (EC 4.2.1.3). 61%. 1134.0. Confidence: high confidence medium confidence low confidence. transporter - ... Ignore hits to Q937N8 when looking for other hits (Aconitate hydratase A; Aconitase; (2R,3S)-2-methylisocitrate dehydratase ... Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99) ...
AutoFact: Aconitate hydratase (Fragment) n=8 Tax=Pinaceae RepID=E3V1P1_PINSY 1.0e-15 ... AutoFact: Aconitate hydratase (Fragment) n=8 Tax=Pinaceae RepID=E3V1P1_PINSY 0.0 ... AutoFact: Aconitate hydratase (Fragment) n=8 Tax=Pinaceae RepID=E3V1P1_PINSY 0.0 ...
  • ACO2 (Aconitase 2) is an enzyme that catalyzes the interconversion of citrate to isocitrate via cis-aconitate in the second step of the TCA cycle. (assaygenie.com)
  • EC 4.2.1.3) 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. (wikipedia.org)
  • His-101 protonates the hydroxyl group on C3 of citrate, allowing it to leave as water, and Ser-642 concurrently abstracts the proton on C2, creating a double bond between C2 and C3, and forming the so-called cis-aconitate intermediate (the two carboxyl groups on the double bond are cis). (wikipedia.org)
  • Another hypothesis is that cis-aconitate stays bound to the enzyme while it flips from the citrate to the isocitrate mode. (wikipedia.org)
  • An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. (nih.gov)
  • The activities of the enzymes citrate synthase, aconitate hydratase, isocitrate dehydrogenase and isocitrate lyase in cell homogenates of n-paraffin grown citrate plus isocitrate accumulating yeasts (C. lipolytica high rate accumulating strain and C. guilliermondii low rate accumulating strain) were determined. (unboundmedicine.com)
  • ACO2: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. (assaygenie.com)
  • We identified four proteins implicated in mitochondrial biogenesis and metabolism regulation as candidate substrates of mOGT, including leucine-rich PPR-containing protein and mitochondrial aconitate hydratase. (mcw.edu)
  • In either case, flipping cis-aconitate allows the dehydration and hydration steps to occur on opposite faces of the intermediate. (wikipedia.org)
  • To complete the reaction, the serine and histidine residues reverse their original catalytic actions: the histidine, now basic, abstracts a proton from water, priming it as a nucleophile to attack at C2, and the protonated serine is deprotonated by the cis-aconitate double bond to complete the hydration, producing isocitrate. (wikipedia.org)