Amino Acid Sequence: 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.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Patents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Nucleic Acid Hybridization: Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)Oligonucleotide Probes: Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Pyruvate Dehydrogenase Complex: A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Pyruvate Dehydrogenase Complex Deficiency Disease: An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.Acetyl-CoA Carboxylase: A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Carbon-Nitrogen Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.Acinetobacter baumannii: A species of gram-negative, aerobic bacteria, commonly found in the clinical laboratory, and frequently resistant to common antibiotics.Fatty Acid Synthase, Type II: The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.Atlases as Topic: Collections of illustrative plates, charts, etc., usually with explanatory captions.Palmitoyl-CoA Hydrolase: Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.Thiolester HydrolasesProteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Acetyl-CoA Hydrolase: An enzyme that catalyzes reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids. EC 3.1.2.1.Cervical Atlas: The first cervical vertebra.Early Detection of Cancer: Methods to identify and characterize cancer in the early stages of disease and predict tumor behavior.Neoplasms: New abnormal growth of tissue. Malignant neoplasms show a greater degree of anaplasia and have the properties of invasion and metastasis, compared to benign neoplasms.Breast Neoplasms: Tumors or cancer of the human BREAST.Prostatic Neoplasms: Tumors or cancer of the PROSTATE.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Peroxisomes: 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)Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.Genome, Human: The complete genetic complement contained in the DNA of a set of CHROMOSOMES in a HUMAN. The length of the human genome is about 3 billion base pairs.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Acyl Coenzyme A: 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.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Methanosarcina barkeri: A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Semiconductors: Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.Aspergillus oryzae: An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Software: Sequential operating programs and data which instruct the functioning of a digital computer.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Adie Syndrome: A syndrome characterized by a TONIC PUPIL that occurs in combination with decreased lower extremity reflexes. The affected pupil will respond more briskly to accommodation than to light (light-near dissociation) and is supersensitive to dilute pilocarpine eye drops, which induce pupillary constriction. Pathologic features include degeneration of the ciliary ganglion and postganglionic parasympathetic fibers that innervate the pupillary constrictor muscle. (From Adams et al., Principles of Neurology, 6th ed, p279)Engineering: The practical application of physical, mechanical, and mathematical principles. (Stedman, 25th ed)Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)IllinoisPublications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Rehabilitation: Restoration of human functions to the maximum degree possible in a person or persons suffering from disease or injury.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)ChicagoCommunity Integration: Policies and programs which ensure that DISPLACED PERSONS and chronic illnesses receive the support and SOCIAL SERVICES needed to live in their communities.Grateful Med: A microcomputer-based software package providing a user-friendly interface to the MEDLARS system of the National Library of Medicine.Desulfovibrio vulgaris: A species of gram-negative, anaerobic, rod-shaped bacteria isolated from soil, animal intestines and feces, and fresh and salt water.Desulfovibrio: A genus of gram-negative, anaerobic, rod-shaped bacteria capable of reducing sulfur compounds to hydrogen sulfide. Organisms are isolated from anaerobic mud of fresh and salt water, animal intestines, manure, and feces.Staphylococcaceae: Family of gram-positive, facultatively anaerobic bacteria, in the order Bacillales. Genera include Gemella, Macrococcus, Salinicoccus, and STAPHYLOCOCCUS.Computational Biology: A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Hydrogenase: An enzyme found in bacteria. It catalyzes the reduction of FERREDOXIN and other substances in the presence of molecular hydrogen and is involved in the electron transport of bacterial photosynthesis.Desulfitobacterium: A genus of anaerobic, gram-positive bacteria in the family Peptococcaceae, that reductively dechlorinates CHLOROPHENOLS.Oxidoreductases, O-Demethylating: Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.Corrinoids: Cyclic TETRAPYRROLES based on the corrin skeleton.Tetrachloroethylene: A chlorinated hydrocarbon used as an industrial solvent and cooling liquid in electrical transformers. It is a potential carcinogen.Halogens: A family of nonmetallic, generally electronegative, elements that form group 17 (formerly group VIIa) of the periodic table.Clostridium bifermentans: A species of gram-positive bacteria in the family Clostridiaceae that ferments both CARBOHYDRATES and AMINO ACIDS.Chlorophenols: Phenols substituted with one or more chlorine atoms in any position.Pentachlorophenol: An insecticide and herbicide that has also been used as a wood preservative. Pentachlorphenol is a widespread environmental pollutant. Both chronic and acute pentachlorophenol poisoning are medical concerns. The range of its biological actions is still being actively explored, but it is clearly a potent enzyme inhibitor and has been used as such as an experimental tool.Dichloroethylenes: Toxic chlorinated unsaturated hydrocarbons. Include both the 1,1- and 1,2-dichloro isomers. Both isomers are toxic, but 1,1-dichloroethylene is the more potent CNS depressant and hepatotoxin. It is used in the manufacture of thermoplastic polymers.IndolizinesAspergillus niger: An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.Starch: Any of a group of polysaccharides of the general formula (C6-H10-O5)n, composed of a long-chain polymer of glucose in the form of amylose and amylopectin. It is the chief storage form of energy reserve (carbohydrates) in plants.Aspergillus: A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.Mycotoxins: Toxic compounds produced by FUNGI.Industrial Microbiology: The study, utilization, and manipulation of those microorganisms capable of economically producing desirable substances or changes in substances, and the control of undesirable microorganisms.Ochratoxins: Isocoumarins found in ASPERGILLUS OCHRACEUS and other FUNGI. Ochratoxin contaminated FOOD has been responsible for cases of FOODBORNE DISEASES.Fermentation: Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.Fumonisins: A group of MYCOTOXINS found in CORN contaminated with FUSARIUM fungus. They are chains of about 20 carbons with acidic ester, acetylamino and sometimes other substituents. They inhibit ceramide synthetase conversion of SPHINGOLIPIDS to CERAMIDES.Proteome: The protein complement of an organism coded for by its genome.Culture Media: Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.Helping Behavior: Behaviors associated with the giving of assistance or aid to individuals.Language Development: The gradual expansion in complexity and meaning of symbols and sounds as perceived and interpreted by the individual through a maturational and learning process. Stages in development include babbling, cooing, word imitation with cognition, and use of short sentences.Research Support as Topic: Financial support of research activities.Research Design: A plan for collecting and utilizing data so that desired information can be obtained with sufficient precision or so that an hypothesis can be tested properly.Language Disorders: Conditions characterized by deficiencies of comprehension or expression of written and spoken forms of language. These include acquired and developmental disorders.Ethics, Research: The moral obligations governing the conduct of research. Used for discussions of research ethics as a general topic.Research Personnel: Those individuals engaged in research.Language Development Disorders: Conditions characterized by language abilities (comprehension and expression of speech and writing) that are below the expected level for a given age, generally in the absence of an intellectual impairment. These conditions may be associated with DEAFNESS; BRAIN DISEASES; MENTAL DISORDERS; or environmental factors.Sign Language: A system of hand gestures used for communication by the deaf or by people speaking different languages.
(1/30) Porcine kidney microsomal cysteine S-conjugate N-acetyltransferase-catalyzed N-acetylation of haloalkene-derived cysteine S-conjugates.

N-Acetylation of xenobiotic-derived cysteine S-conjugates is a key step in the mercapturic acid pathway. The aim of this study was to investigate the N-acetylation of haloalkene-derived S-haloalkyl and S-haloalkenyl cysteine S-conjugates by porcine kidney cysteine S-conjugate N-acetyltransferase (NAcT). A radioactive assay for the quantification of NAcT activity was developed as a new method for partial purification of the enzyme, which was necessitated by the substantial loss of activity during the immunoaffinity chromatography method. 3-[(3-Cholamidopropyl)dimethylammonio]-1-propane-sulfonate, rather than N,N-bis[3-gluconamidopropyl]deoxycholamide, was used to solubilize the NAcT from porcine kidney microsomes in the revised procedure. The partially purified NAcT was free of detectable aminoacylase activity. Although low acetyl-coenzyme A hydrolase activity was observed, its effect on the assay was minimized by addition of excess acetyl-coenzyme A in the NAcT assay mixture. Attempts to separate the residual hydrolase activity from NAcT by different chromatographic procedures were either unsuccessful or lead to inactivation of NAcT. Most of the cysteine S-conjugates studied were N-acetylated by NAcT. Although the apparent K(m) values for the cysteine S-conjugates studied differed by a factor of approximately 2.5 (124-302 microM), a greater than 15-fold difference in the apparent V(max) (0.75-15.6 nmol/h) and V(max)/K(m) (0.008-0.126 x 10(-3) l h(-1)) values was observed. These data show that a range of haloalkene-derived cysteine S-conjugates serve as substrates for pig kidney NAcT. The significant differences in cytotoxicity of these conjugates may be a result of more variable deacetylation rates of the corresponding mercapturates.  (+info)

(2/30) Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase.

A cytosolic acetyl-CoA hydrolase (CACH) was purified from rat liver to homogeneity by a new method using Triton X-100 as a stabilizer. We digested the purified enzyme with an endopeptidase and determined the N-terminal amino-acid sequences of the two proteolytic fragments. From the sequence data, we designed probes for RT-PCR, and amplified CACH cDNA from rat liver mRNA. The CACH cDNA contains a 1668-bp ORF encoding a protein of 556 amino-acid residues (62 017 Da). Recombinant expression of the cDNA in insect cells resulted in overproduction of functional acetyl-CoA hydrolase with comparable acyl-CoA chain-length specificity and Michaelis constant for acetyl-CoA to those of the native CACH. Database searching shows no homology to other known proteins, but reveals high similarities to two mouse expressed sequence tags (91% and 93% homology) and human mRNA for KIAA0707 hypothetical protein (50% homology) of unknown function.  (+info)

(3/30) Production of acetate in the liver and its utilization in peripheral tissues.

In experimental rat liver perfusion we observed net production of free acetate accompanied by accelerated ketogenesis with long-chain fatty acids. Mitochondrial acetyl-CoA hydrolase, responsible for the production of free acetate, was found to be inhibited by the free form of CoA in a competitive manner and activated by reduced nicotinamide adenine dinucleotide (NADH). The conditions under which the ketogenesis was accelerated favored activation of the hydrolase by dropping free CoA and elevating NADH levels. Free acetate was barely metabolized in the liver because of low affinity, high K(m), of acetyl coenzyme A (acetyl-CoA) synthetase for acetate. Therefore, infused ethanol was oxidized only to acetate, which was entirely excreted into the perfusate. The acetyl-CoA synthetase in the heart mitochondria was much lower in K(m) than it was in the liver, thus the heart mitochondria was capable of oxidizing free acetate as fast as other respiratory substrates, such as succinate. These results indicate that rat liver produces free acetate as a byproduct of ketogenesis and may supply free acetate, as in the case of ketone bodies, to extrahepatic tissues as fuel.  (+info)

(4/30) Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression.

A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells resulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic approaches.  (+info)

(5/30) Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae.

Acetyl-CoA hydrolase (Ach1p), catalyzing the hydrolysis of acetyl-CoA, is presumably involved in regulating intracellular acetyl-CoA or CoASH pools; however, its intracellular functions and distribution remain to be established. Using site-directed mutagenesis analysis, we demonstrated that the enzymatic activity of Ach1p is dependent upon its putative acetyl-CoA binding sites. The ach1 mutant causes a growth defect in acetate but not in other non-fermentable carbon sources, suggesting that Ach1p is not involved in mitochondrial biogenesis. Overexpression of Ach1p, but not constructs containing acetyl-CoA binding site mutations, in ach1-1 complemented the defect of acetate utilization. By subcellular fractionation, most of the Ach1p in yeast was distributed with mitochondria and little Ach1p in the cytoplasm. By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. Moreover, the onset of pseudohyphal development in homozygote ach1-1 diploids was abolished. We infer that Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast.  (+info)

(6/30) Physiological difference between dietary obesity-susceptible and obesity-resistant Sprague Dawley rats in response to moderate high fat diet.

The primary aim of the present study was to define central and peripheral physiological differences between dietary obesity-susceptible (DOS) and obesity-resistant (DOR) outbred Sprague Dawley (SD) rats when given a moderate high fat diet containing 32.34% of energy as a fat. After a 9-week feeding period, the DOS-SD rats consumed significantly more feed (11.1%) and had higher abdominal (39.9%) and epididymal (27.5%) fat pads than the DOR-SD rats. In addition, serum leptin and insulin levels were significantly increased in the DOS-SD rats compared with those in the DOR-SD rats. However, we did not observe significant differences in serum triglyceride, cholesterol and glucose. No differences in hypothalamic OB-Ra and Rb mRNA expressions were found between the two groups. In contrast, arcuate NPY immunohistochemical expression was much higher in the DOS-SD rats than in the DOR-SD rats, though NPY expression in the supraoptic and paraventricular nuclei was not different between the two phenotypes. In peripheral tissues, the DOS-SD rats showed noticeably increased acetyl CoA carboxylase (ACC) mRNA expression in the liver, not epididymal fat. However, Western blot of peroxisomal proliferator activated factor gamma (PPAR gamma) in the liver and epididymal fat was not different between the two phenotypes of SD rats. It was concluded that different body weight phenotypes within outbred SD population responded differently to the development of dietary induced obesity via altered anabolic features in the hypothalamus and liver.  (+info)

(7/30) An acetate-sensitive mutant of Neurospora crassa deficient in acetyl-CoA hydrolase.

The predicted amino acid sequence of the product of the acetate-inducible acu-8 gene of Neurospora crassa, previously of unknown function, has close homology to the recently published sequence of Saccharomyces cerevisiae acetyl-CoA hydrolase. An acu-8 mutant strain, previously characterized as acetate non-utilizing, shows strong growth-inhibition by acetate, but will use it as carbon source at low concentrations. The mutant was shown to be deficient in acetyl-CoA hydrolase and to accumulate acetyl-CoA when supplied with acetate. As in Saccharomyces, the Neurospora enzyme is acetate-inducible.  (+info)

(8/30) Brassica juncea 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase 1: expression and characterization of recombinant wild-type and mutant enzymes.

3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS; EC 2.3.3.10) is the second enzyme in the cytoplasmic mevalonate pathway of isoprenoid biosynthesis, and catalyses the condensation of acetyl-CoA with acetoacetyl-CoA (AcAc-CoA) to yield S-HMG-CoA. In this study, we have first characterized in detail a plant HMGS, Brassica juncea HMGS1 (BjHMGS1), as a His6-tagged protein from Escherichia coli. Native gel electrophoresis analysis showed that the enzyme behaves as a homodimer with a calculated mass of 105.8 kDa. It is activated by 5 mM dithioerythreitol and is inhibited by F-244 which is specific for HMGS enzymes. It has a pH optimum of 8.5 and a temperature optimum of 35 degrees C, with an energy of activation of 62.5 J x mol(-1). Unlike cytosolic HMGS from chicken and cockroach, cations like Mg2+, Mn2+, Zn2+ and Co2+ did not stimulate His6-BjHMGS1 activity in vitro; instead all except Mg2+ were inhibitory. His6-BjHMGS1 has an apparent K(m-acetyl-CoA) of 43 microM and a V(max) of 0.47 micromol x mg(-1) x min(-1), and was inhibited by one of the substrates (AcAc-CoA) and by both products (HMG-CoA and HS-CoA). Site-directed mutagenesis of conserved amino acid residues in BjHMGS1 revealed that substitutions R157A, H188N and C212S resulted in a decreased V(max), indicating some involvement of these residues in catalytic capacity. Unlike His6-BjHMGS1 and its soluble purified mutant derivatives, the H188N mutant did not display substrate inhibition by AcAc-CoA. Substitution S359A resulted in a 10-fold increased specific activity. Based on these kinetic analyses, we generated a novel double mutation H188N/S359A, which resulted in a 10-fold increased specific activity, but still lacking inhibition by AcAc-CoA, strongly suggesting that His-188 is involved in conferring substrate inhibition on His6-BjHMGS1. Substitution of an aminoacyl residue resulting in loss of substrate inhibition has never been previously reported for any HMGS.  (+info)

*  ACOT11
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, ...
*  Acetyl-CoA hydrolase
... acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol ... In enzymology, an acetyl-CoA hydrolase (EC 3.1.2.1) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is acetyl-CoA hydrolase. Other names in common use include acetyl-CoA deacylase, ... the two substrates of this enzyme are acetyl-CoA and H2O, whereas its two products are CoA and acetate. It is present in many ...
*  ACOT12
Suematsu N, Isohashi F (2007). "Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase". Acta ... 2001). "Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase". Eur. J. Biochem. 268 (9): ... rat liver cytosolic acetyl-coenzyme A hydrolase". J. Chromatogr. B. 790 (1-2): 239-44. doi:10.1016/s1570-0232(03)00167-3. PMID ... "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029-32. doi:10.1194/jlr.E500003- ...
*  Thioesterase
Acetyl-CoA hydrolase, palmitoyl-CoA hydrolase, succinyl-CoA hydrolase, formyl-CoA hydrolase, acyl-CoA hydrolase are a few ... Esterases, in turn, are one type of the several hydrolases known. Thioesterases exhibit Esterase activity (splitting of an ... Thioesterases or thiolester hydrolases are identified as members of E.C.3.1.2. ... "Evolutionary divergence and functions of the human acyl-CoA thioesterase gene ( ACOT ) family". Human Genomics. 4 (6): 411-20. ...
*  List of MeSH codes (D08)
... thiolester hydrolases MeSH D08.811.277.352.897.075 --- acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 --- palmitoyl-coa ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... acetyl-CoA C-acetyltransferase MeSH D08.811.913.050.134.105 --- amino-acid n-acetyltransferase MeSH D08.811.913.050.134.150 ... N-acetyl-beta-glucosaminyl)asparagine amidase MeSH D08.811.277.087.760 --- pyroglutamate hydrolase MeSH D08.811.277.087.831 ...
*  List of EC numbers (EC 3)
... acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA ... bile-acid-CoA hydrolase EC 3.1.2.27: choloyl-CoA hydrolase EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase EC 3.1.2.29: ... formyl-CoA hydrolase EC 3.1.2.11: acetoacetyl-CoA hydrolase EC 3.1.2.12: S-formylglutathione hydrolase EC 3.1.2.13: S- ... ADP-dependent short-chain-acyl-CoA hydrolase EC 3.1.2.19: ADP-dependent medium-chain-acyl-CoA hydrolase EC 3.1.2.20: acyl-CoA ...
*  Succinyl-CoA hydrolase
This enzyme participates in citrate cycle (tca cycle). Gergely J, Hele P, Ramakrishnan CV (1952). "Succinyl and acetyl coenzyme ... In enzymology, a succinyl-CoA hydrolase (EC 3.1.2.3) is an enzyme that catalyzes the chemical reaction succinyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is succinyl-CoA hydrolase. Other names in common use include succinyl-CoA acylase, ... whereas its two products are CoA and succinate. This enzyme belongs to the family of hydrolases, specifically those acting on ...
*  acetyl-CoA carboxylase)-phosphatase
... whereas its two products are acetyl-CoA carboxylase and phosphate. This enzyme belongs to the family of hydrolases, ... acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) is an enzyme that catalyzes the chemical reaction [acetyl-CoA carboxylase] ... acetyl-CoA carboxylase] + phosphate Thus, the two substrates of this enzyme are acetyl-CoA carboxylase phosphate and H2O, ... Krakower GR; Kim K-H (1980). "Purification and properties of acetyl-CoA carboxylase phosphatase". J. Biol. Chem. 256 (5): 2408- ...
*  Formyl-CoA hydrolase
I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl phosphate in Clostridium kluyveri". J. ... The systematic name of this enzyme class is formyl-CoA hydrolase. This enzyme is also called formyl coenzyme A hydrolase. This ... In enzymology, a formyl-CoA hydrolase (EC 3.1.2.10) is an enzyme that catalyzes the chemical reaction formyl-CoA + H2O ⇌ {\ ... whereas its two products are CoA and formate. This enzyme belongs to the family of hydrolases, specifically those acting on ...
*  N-Acetylglutamic acid
... (abbreviated NAcGlu) is biosynthesized from glutamic acid and acetyl-CoA by the enzyme N-acetylglutamate ... The reverse reaction, hydrolysis of the acetyl group, is catalyzed by a specific hydrolase. NAcGlu activates carbamoyl ... Glutamate Glutamic acid "N-Acetyl-DL-glutamic acid - Compound Summary". PubChem Compound. USA: National Center for ...
*  Alkylacetylglycerophosphatase
Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen". J. Biol. Chem. 261 ( ... whereas its two products are 1-alkyl-2-acetyl-sn-glycerol and phosphate. This enzyme belongs to the family of hydrolases, ... Other names in common use include 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase, and alkylacetylglycerophosphate ... 1-alkyl-2-acetyl-sn-glycerol + phosphate Thus, the two substrates of this enzyme are 1-alkyl-2-acetyl-sn-glycero-3-phosphate ...
*  Citrate synthase
The enzyme is inhibited by high ratios of ATP:ADP, acetyl-CoA:CoA, and NADH:NAD, as high concentrations of ATP, acetyl-CoA, and ... These experiments have revealed that this single site alternates between two forms, which participate in ligase and hydrolase ... acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SH acetyl-CoA Oxaloacetic acid Citric acid Oxaloacetate is regenerated after ... This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citroyl-CoA ...
*  Tyrosine
Acetoacetate is a ketone body, which is activated with succinyl-CoA, and thereafter it can be converted into acetyl-CoA, which ... Fumarylacetoacetate is finally split by the enzyme fumarylacetoacetate hydrolase through the addition of a water molecule. ...
*  Metabolism
... acetyl-CoA), which releases some energy. Finally, the acetyl group on the CoA is oxidised to water and carbon dioxide in the ... These digestive enzymes include proteases that digest proteins into amino acids, as well as glycoside hydrolases that digest ... and this breakdown process involves the release of significant amounts of acetyl-CoA, propionyl-CoA, and pyruvate, which can ... The glycerol enters glycolysis and the fatty acids are broken down by beta oxidation to release acetyl-CoA, which then is fed ...
*  ACOT13
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, ...
*  Acyl-CoA thioesterase 9
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase ...
*  Hydrogenobacter thermophilus
The cleavage of citryl-CoA to acetyl-CoA and oxaloacetate occurs in a two step process. First, citryl-coA synthetase catalyzes ... pathways while typical PSPs need Mg2+ for activity and are considered to be part of the haloacid dehalogenase-like hydrolase ... Novel proteins such as citryl-CoA synthetase (CCS) and ciitryl-CoA (CLL)are utilized within the reductive TCA cycle (Reverse ... 2004). "A novel enzyme, citryl-CoA lyase, catalyzing the second step of the citrate cleavage reaction in Hydrogenobacter ...
*  Biotin deficiency
... propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, pyruvate carboxylase, and 2 forms of acetyl-CoA carboxylase.) ... peptidyl hydrolase biotinidase (BTD), and the protein ligase holocarboxylase synthetase. When any of these regulatory factors ... excretion of 3-hydroxyisovaleric acid and biotin in urine activity of propionyl-CoA carboxylase in lymphocytes In the United ...
*  Juvenile hormone
Three acetyl-CoAs are converted inoto HMG-CoA by the cytosolic isoforms of thiolase and 3-hydroxy-3-methylglutaryl-CoA synthase ... JH acid is attached by JH epoxide hydrolase, which converts the epoxide group to a diol. The order of cleavage depends on the ... It is converted into acetyl-CoA, ADP, CO2, and oxaloacetate by ATP-citrate lyase, together with ATP and CoASH as substrates. ... The HMG-CoA is then reduced by NADPH to mevalonate by HMG-CoA reductase, the rate controlling enzyme of cholesterol ...
*  ACOT2
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... It is most active on myristoyl-CoA but also shows high activity on palmitoyl-CoA, stearoyl-CoA, and arachidoyl-CoA. The protein ... CoA) esters, such as acyl-CoAs, bile CoAs, and CoA esters of prostaglandins, to the corresponding free acid and CoA. ACOT2 ...
*  Acetylcholinesterase
The liberated choline is taken up again by the pre-synaptic neuron and ACh is synthesized by combining with acetyl-CoA through ... AChE is a hydrolase that hydrolyzes choline esters. It has a very high catalytic activity - each molecule of AChE degrades ...
*  Chromosome 11 (human)
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase) ACRV1: encoding protein Acrosomal protein SP-10 ... fatty acyl-coA reductase 1 FAT3: fat atypical cadherin 3 FHIP: FTS and Hook-interacting protein FNBP4: Formin-binding protein 4 ... encoding protein Ester hydrolase C11orf54 C11orf58: small acidic protein C11orf73: chromosome 11, open reading frame 73 ...
*  Aspartoacylase
... is a hydrolase enzyme responsible for catalyzing the deacylation of N-acetyl-l-aspartate (N-acetylaspartate,NAA) into aspartate ... one hypothesis is that it is potentially used as a chemical reservoir that can be tapped into for acetate for acetyl-CoA ... Aspartoacylase prevents the build up of N-acetyl-L-aspartate in the brain. N-acetyl-L-aspartate is one of the most abundant ... The zinc cofactor is used to lower the pKa of a ligated water so that an attack on N-acetyl-L-aspartate may occur and to ...
*  CYP2E1
In the conversion sequence of acetyl-CoA to glucose, CYP2E1 transforms acetone via hydroxyacetone (acetol) into propylene ... He J, Wang C, Zhu Y, Ai D (Dec 2015). "Soluble epoxide hydrolase: A potential target for metabolic diseases". Journal of ... EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by epoxide hydrolases, ... Fleming I (Oct 2014). "The pharmacology of the cytochrome P450 epoxygenase/soluble epoxide hydrolase axis in the vasculature ...
*  Tumor metabolome
Fatty acid synthesis is an anabolic process that starts from the conversion of acetyl-CoA to malonyl-CoA by acetyl-CoA ... both of which can inhibit dioxygenases or prolyl hydrolases that mediate the degradation of HIF proteins. HIF-1 could be ... Malonyl CoA leads to fatty acid synthesis (FAS) and is involved in the elongation of fatty acids through Fatty acid synthase ( ...
*  Valproate
Acetyl-L-carnitine lowers hyperammonemia less markedly than L-carnitine. Although the mechanism of action of valproate is not ... and epoxide hydrolase and is highly protein bound and hence may interact with drugs that are substrates for any of these ... and valproyl-CoA, among others. Valproic acid is a branched short-chain fatty acid and a derivative of valeric acid. Valproic ... Matsuoka M, Igisu H (1993). "Comparison of the effects of L-carnitine, D-carnitine and acetyl-L-carnitine on the neurotoxicity ...
*  Biosynthesis
... the enzyme serine acetyltransferase catalyzes the transfer of acetyl group from acetyl-CoA onto L-serine to yield O-acetyl-L- ... Orotate phosphoribosyl hydrolase (OMP pyrophosphorylase) condenses orotate with PRPP to form orotidine-5'-phosphate. OMP ... In the case of NADH, the molecule transfers a hydrogen, whereas acetyl CoA transfers an acetyl group, and ATP transfers a ... The following reaction step, catalyzed by the enzyme O-acetyl serine (thiol) lyase, replaces the acetyl group of O-acetyl-L- ...
Acetyl-CoA hydrolase - Wikipedia  Acetyl-CoA hydrolase - Wikipedia
... acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol ... In enzymology, an acetyl-CoA hydrolase (EC 3.1.2.1) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is acetyl-CoA hydrolase. Other names in common use include acetyl-CoA deacylase, ... the two substrates of this enzyme are acetyl-CoA and H2O, whereas its two products are CoA and acetate. It is present in many ...
more infohttps://en.wikipedia.org/wiki/Acetyl-CoA_hydrolase
Expression of a yeast acetyl CoA hydrolase in the mitochondrion, Plant Molecular Biology | 10.1007/s11103-004-1557-4 | DeepDyve  Expression of a yeast acetyl CoA hydrolase in the mitochondrion, Plant Molecular Biology | 10.1007/s11103-004-1557-4 | DeepDyve
"Expression of a yeast acetyl CoA hydrolase in the mitochondrion, Plant Molecular Biology" on DeepDyve, the largest online ... Expression of a yeast acetyl CoA hydrolase in the mitochondrion. Expression of a yeast acetyl CoA hydrolase in the ... specific role of acetyl CoA in the mitochondria we exploited a transgenic approach to introduce a yeast acetyl CoA hydrolase ( ... specific role of acetyl CoA in the mitochondria we exploited a transgenic approach to introduce a yeast acetyl CoA hydrolase ( ...
more infohttps://www.deepdyve.com/lp/springer_journal/expression-of-a-yeast-acetyl-coa-hydrolase-in-the-mitochondrion-MCf2xYCIJm
From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN...  From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN...
... revealing that the disappearance of acetyl CH3 from acetyl Coenzyme A occurred concomitantly with the appearance of a CH3 peak ... This folate-dependent activity is exclusive to these two isoforms; no acetyl Coenzyme A hydrolysis was found when murine ... These data, together with the characterisation of a naphthoquinone inhibitor of folate-dependent acetyl Coenzyme A hydrolysis ... and facilitate acetyl Coenzyme A hydrolysis. The evidence presented in this paper adds to our growing understanding of the ...
more infohttps://pharm.ox.ac.uk/publications/465131
Acylase | definition of acylase by Medical dictionary  Acylase | definition of acylase by Medical dictionary
acetyl-CoA hydrolase. References in periodicals archive ? Reversible immobilization of glutaryl acylase on sepabeads coated ...
more infohttp://medical-dictionary.thefreedictionary.com/acylase
EC 3.1.2  EC 3.1.2
... acetyl-CoA hydrolase. Reaction: acetyl-CoA + H2O = CoA + acetate. Other name(s): acetyl-CoA deacylase; acetyl-CoA acylase; ... EC 3.1.2.1 acetyl-CoA hydrolase. EC 3.1.2.2 palmitoyl-CoA hydrolase. EC 3.1.2.3 succinyl-CoA hydrolase. EC 3.1.2.4 3- ... acetyl coenzyme A deacylase; acetyl coenzyme A acylase; acetyl-CoA thiol esterase. Systematic name: acetyl-CoA hydrolase. Links ... palmitoyl-CoA hydrolase. Reaction: palmitoyl-CoA + H2O = CoA + palmitate. Other name(s): long-chain fatty-acyl-CoA hydrolase; ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC3/0102.html
Patent US4394443 - Method for cloning genes - Google Patents  Patent US4394443 - Method for cloning genes - Google Patents
Glucose-regulated promoter of yeast acetyl-CoA hydrolase. US5500361 *. Nov 12, 1992. Mar 19, 1996. E. I. Du Pont De Nemours And ... Procaryotic carbonyl hydrolases. US5316925 *. Dec 3, 1992. May 31, 1994. Davis Mark M. T-cell receptor specific for antigen ...
more infohttp://www.google.com/patents/US4394443?dq=6,460,050
Patent US4394443 - Method for cloning genes - Google Patents  Patent US4394443 - Method for cloning genes - Google Patents
Glucose-regulated promoter of yeast acetyl-CoA hydrolase. US5500361 *. Nov 12, 1992. Mar 19, 1996. E. I. Du Pont De Nemours And ... Procaryotic carbonyl hydrolases. US5316925 *. Dec 3, 1992. May 31, 1994. Davis Mark M. T-cell receptor specific for antigen ...
more infohttp://www.google.com/patents/US4394443?dq=4484186
Acot9 - Acyl-coenzyme A thioesterase 9, mitochondrial precursor - Mus musculus (Mouse) - Acot9 gene & protein  Acot9 - Acyl-coenzyme A thioesterase 9, mitochondrial precursor - Mus musculus (Mouse) - Acot9 gene & protein
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... acetyl-CoA hydrolase activity Source: HGNC ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the ... acyl-CoA hydrolase activity Source: MGI ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ... acyl-CoA metabolic process Source: HGNC ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ...
more infohttp://www.uniprot.org/uniprot/Q9R0X4
ACOT12 - Wikipedia  ACOT12 - Wikipedia
Suematsu N, Isohashi F (2007). "Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase". Acta ... 2001). "Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase". Eur. J. Biochem. 268 (9): ... rat liver cytosolic acetyl-coenzyme A hydrolase". J. Chromatogr. B. 790 (1-2): 239-44. doi:10.1016/s1570-0232(03)00167-3. PMID ... "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029-32. doi:10.1194/jlr.E500003- ...
more infohttps://en.wikipedia.org/wiki/ACOT12
KEGG ENZYME: 3.1.2.32  KEGG ENZYME: 3.1.2.32
2-aminobenzoyl)acetyl-CoA hydrolase. Reaction(IUBMB). (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA [RN: ... Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response ...
more infohttps://www.genome.jp/dbget-bin/www_bget?ec:3.1.2.32
KEGG BRITE: KEGG Orthology (KO) - Acinetobacter baumannii AYE  KEGG BRITE: KEGG Orthology (KO) - Acinetobacter baumannii AYE
ABAYE0257 putative acetyl-CoA hydrolase/transferase ABAYE3797 lldD; L-lactate dehydrogenase, FMN linked ABAYE3796 dld; D- ... K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA ... acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2. ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00632 fadA; acetyl- ...
more infohttp://www.genome.jp/kegg-bin/get_htext?aby00001+ABAYE2333
EC 3.1.2.1  EC 3.1.2.1
Acetyl-CoA hydrolase.. EC 3.1.2.1 Profiles. 1psg274_3.1.2.1 (PRI000686). 2psg274_3.1.2.1 (PRI002810). ...
more infohttp://priam.prabi.fr/cgi-bin/PRIAM_profiles_CurrentRelease.pl?EC=3.1.2.1
Expression of ACOT8 in cancer - Summary - The Human Protein Atlas  Expression of ACOT8 in cancer - Summary - The Human Protein Atlas
GO:0003986 [acetyl-CoA hydrolase activity]. GO:0005102 [receptor binding]. GO:0005515 [protein binding]. GO:0005737 [cytoplasm] ... CoA hydrolase activity]. GO:0016290 [palmitoyl-CoA hydrolase activity]. GO:0016559 [peroxisome fission]. GO:0016787 [hydrolase ... acyl-CoA hydrolase activity]. GO:0052689 [carboxylic ester hydrolase activity]. GO:0052815 [medium-chain acyl-CoA hydrolase ... GO:0033540 [fatty acid beta-oxidation using acyl-CoA oxidase]. GO:0033882 [choloyl-CoA hydrolase activity]. GO:0035338 [long- ...
more infohttp://www.proteinatlas.org/ENSG00000101473-ACOT8/pathology
Londhe A[au] - PubMed - NCBI  Londhe A[au] - PubMed - NCBI
Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.. Khandokar YB, Londhe A, ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=Londhe+A%5Bau%5D&dispmax=50
ACOT9 Gene - GeneCards | ACOT9 Protein | ACOT9 Antibody  ACOT9 Gene - GeneCards | ACOT9 Protein | ACOT9 Antibody
Acyl-CoA Thioesterase 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human ... GO annotations related to this gene include carboxylic ester hydrolase activity and acetyl-CoA hydrolase activity. ... A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. (PMID: 16103133) Hunt MC … Alexson SE (Journal of lipid ... acetyl-CoA hydrolase activity. ISS. --. GO:0016787. hydrolase activity. IEA. --. GO:0047617. acyl-CoA hydrolase activity. TAS. ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=ACOT9
KEGG SSDB Best Search Result: tgu:100218258  KEGG SSDB Best Search Result: tgu:100218258
oho:Oweho_3154 acetyl-CoA hydrolase 423 103 ( -) 29 0.579 38 -, 1 smon:AWR27_23735 hypothetical protein 158 103 ( -) 29 0.408 ... cdiv:CPM_1104 acyl-CoA synthetase (AMP-forming)/AMP-aci K01897 566 123 ( -) 34 0.315 73 -, 1 ble:BleG1_2449 hypothetical ... ddh:Desde_1771 acyl-CoA synthetase (AMP-forming)/AMP-ac K01897 548 112 ( -) 31 0.303 66 -, 1 seon:BWZ22_14460 mechanosensitive ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=tgu:100218258
IJMS  | Free Full-Text | On the Free Energy That Drove Primordial Anabolism | HTML  IJMS | Free Full-Text | On the Free Energy That Drove Primordial Anabolism | HTML
Expression of a yeast acetyl CoA hydrolase in the mitochondrion of tobacco plants inhibits growth and restricts photosynthesis ... Almost all metabolites can be degraded to Acetyl-CoA, and Acetyl-CoA itself is the building block of many biochemical ... Russell, MJ; Martin, W. The rocky roots of the acetyl-CoA pathway. Trends Biochem. Sci 2004, 29, 358-363. [Google Scholar] ... Further candidate high energy compounds are thioesters such as Acetyl-CoA which is a central molecule of present metabolism [ ...
more infohttps://www.mdpi.com/1422-0067/10/4/1853/htm
The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands | BMC Evolutionary Biology | Full...  The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands | BMC Evolutionary Biology | Full...
Suematsu N, Isohashi F: Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase. Acta Biochim Pol. ... Multi-domain proteins that contain a START domain are mammalian cytosolic acetyl-CoA hydrolases [17] and some members of the HD ...
more infohttps://bmcevolbiol.biomedcentral.com/articles/10.1186/1471-2148-8-286
  • Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. (genome.jp)
  • 3. Miyazawa, S., Furuta, S. and Hashimoto, T. Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators. (qmul.ac.uk)
  • From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN)NAT1 and its homologue (MOUSE)NAT2. (ox.ac.uk)
  • In summary these results suggest that the content of acetyl CoA is under tight control and that alterations in the level of this central metabolite have severe metabolic and developmental consequences in tobacco. (deepdyve.com)
  • Changes in the balance of intracellular metabolites towards a higher level of carbon passing through acetyl-CoA and a high capacity to regenerate NADPH during growth on medium with starch and lactate were found to be the likely cause of this effect. (biomedcentral.com)