Aconitate Hydratase
Hydro-Lyases
Fluorine
Enoyl-CoA Hydratase
Isocitrate Dehydrogenase
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.
Fumarate Hydratase
3-Hydroxyacyl CoA Dehydrogenases
Peroxisomal Bifunctional Enzyme
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.
Dodecenoyl-CoA Isomerase
Carbon-Carbon Double Bond Isomerases
Peroxisomal Multifunctional Protein-2
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.
Enoyl-CoA Hydratase 2
Isomerases
Racemases and Epimerases
Microbodies
Acyl Coenzyme A
Tungsten
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.
Mitochondrial Trifunctional Protein
Crotonates
Multienzyme Complexes
Acrylonitrile
Thauera
Epoxide Hydrolases
Polyhydroxyalkanoates
Neoplastic Syndromes, Hereditary
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.
17-Hydroxysteroid Dehydrogenases
Molecular Sequence Data
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.
Brevibacterium
Carbonic Anhydrase I
Amino Acid Sequence
Deltaproteobacteria
Peroxisomes
Fibric Acids
Vanillic Acid
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)
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Aconitase | Article about aconitase by The Free Dictionary
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DI49 2832 - Aconitate hydratase, mitochondrial - Saccharomyces eubayanus (Yeast) - DI49 2832 gene & protein
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Selective inhibition of the citrate-to-isocitrate reaction o 2020
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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 ...
Haemophilus influenzae
The enzymes missing from the TCA cycle are citrate synthase, aconitate hydratase, and isocitrate dehydrogenase. Haemophilus ...
Methyl fluoroacetate
Fluorocitrate can inhibit aconitate hydratase, which is needed for the conversion of citrate, by competitive inhibition. This ...
List of MeSH codes (D08)
... 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- ...
List of EC numbers (EC 4)
... 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 * ...
Crossover experiment (chemistry)
... 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. ...
List of EC numbers (EC 5)
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- ...
List of EC numbers (EC 2)
... 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- ...
Code System Concept
Deficiency of aconitate hydratase (disorder). Code System Preferred Concept Name. Deficiency of aconitate hydratase (disorder) ...
Background
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 ...
IMSEAR at SEARO: Search
1 Aconitate Hydratase --antagonists.... *1 Animals. *1 Armadillos. *1 Citrates --pharmacology. *1 Glucosephosphate ...
IMSEAR at SEARO: Search
1 Aconitate Hydratase --antagonists.... *1 Animals. *1 Armadillos. *1 Citrates --pharmacology. *1 Culture Media ...
IMSEAR at SEARO: Search
1 Aconitate Hydratase --antagonists.... *1 Citrates --pharmacology. *1 Citric Acid Cycle. *1 Electrophoresis, Polyacrylamide ...
Code System Concept
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 ...
Code System Concept
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) { ...
Code System Concept
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) { ...
Code System Concept
Aconitate hydratase (substance). Code System Preferred Concept Name. Aconitate hydratase (substance). Concept Status. Published ...
About: Lyase
dbr:Aconitate_decarboxylase. *dbr:Felinine. *dbr:Crotonoyl-(acyl-carrier-protein)_hydratase. *dbr:Diaminobutyrate_decarboxylase ...
Let there be water: How hydration/dehydration reactions accompany key Earth and life processes
... 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. ...
Mitochondrial Electron Transport Chain
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 ...
Aligments for a candidate for acn in Pseudomonas fluorescens GW456-L13
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 ...
Geographic patterns of mtDNA and Z-linked sequence variation in the Common Chiffchaff and the 'chiffchaff complex'<...
aconitate hydratase Agriculture & Biology 33% View full fingerprint Cite this. * APA * Standard ...
HIPK2
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 ...
Browse
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase YP_002268725 unclonable 0.0000016622 normal 1 Escherichia ...
Insights on bio-degumming of kenaf bast based on metagenomi and proteomics | Research Square
Aconitate hydratase (Aconitase) (EC 4.2.1.3). 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO: ...
MMTB
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 ...
HOMD :: SEQF2580
Aconitate hydratase 2. 76. SEQF2580,ANNF01000038.1. ERJ21133.1 jb [NA] [AA] 747/248. 10146-10892. hypothetical protein. ...
MMTB
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 - - ...
MMTB
4.2.1.117 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) 4.2.1.3 aconitate hydratase - - ...
SCOPe 2.04: Domain d1b0ja2: 1b0j A:2-528
PDB Compounds: (A:) aconitate hydratase. SCOPe Domain Sequences for d1b0ja2:. Sequence; same for both SEQRES and ATOM records ...
Aconitase - Wikipedia
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 ...
Subject: citrates and aluminum / Subject term: cycloheximide / Text Availability: Citation in PubAg - PubAg Search Results
SCOPe 2.04: Domain d1b0ja2: 1b0j A:2-528
MeSH Browser
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/ ...
SGN Unigene - Show All Stored BLAST Hits - Sol Genomics Network
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 ...
Background
Insights on bio-degumming of kenaf bast based on metagenomi and proteomics | Research Square
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 ...
HOMD :: SEQF2940
Code System Concept
PRIME PubMed | [Enzymatic examination of citrate-isocitrate accumulation in yeasts]
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 ...
HOMD :: SEQF2580
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Let there be water: How hydration/dehydration reactions accompany key Earth and life processes
Effect of a glucose impulse on the CcpA regulon in Staphylococcus aureus | BMC Microbiology | Full Text
Human ACO2 (Aconitase 2) ELISA Kit (HUFI04692)
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 ...
Anaerobic regulation of Bacillus subtilis Krebs cycle genes<...
Identification of phosphorylation proteins in response to water deficit during wheat flag leaf and grain development |...
ACONITIC ACID, (E)
Finding step leuD for L-leucine biosynthesis in Sinorhizobium meliloti 1021
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. ...
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CoP: Co-expressed Biological Processes
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H+ transporting | Science and Nuts
Osanai, T.<...
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Finding step acnD for L-threonine catabolism in Dinoroseobacter shibae DFL-12
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) ...
Aconitase1
- 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)
Citrate6
- 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)
Mitochondrial1
- 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)
Hydration2
- 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)