Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Acetyl Coenzyme A: Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.Choline O-Acetyltransferase: An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC 2.3.1.6.Chloramphenicol O-Acetyltransferase: An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.p300-CBP Transcription Factors: A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.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.Serine O-Acetyltransferase: An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.Zoogloea: A genus of RHODOCYCLACEAE occurring as rod-shaped cells embedded in a gelatinous matrix. It includes Z. filipendula.Acetyl-CoA C-Acetyltransferase: An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.Pseudomonadaceae: A family of gram-negative bacteria usually found in soil or water and including many plant pathogens and a few animal pathogens.DiazomethaneSewage: Refuse liquid or waste matter carried off by sewers.Acetyl-CoA C-Acyltransferase: Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.Coenzyme APlatelet Activating Factor: A phospholipid derivative formed by PLATELETS; BASOPHILS; NEUTROPHILS; MONOCYTES; and MACROPHAGES. It is a potent platelet aggregating agent and inducer of systemic anaphylactic symptoms, including HYPOTENSION; THROMBOCYTOPENIA; NEUTROPENIA; and BRONCHOCONSTRICTION.Polyesters: Polymers of organic acids and alcohols, with ester linkages--usually polyethylene terephthalate; can be cured into hard plastic, films or tapes, or fibers which can be woven into fabrics, meshes or velours.Bacterial Proteins: Proteins found in any species of bacterium.Flagellin: A protein with a molecular weight of 40,000 isolated from bacterial flagella. At appropriate pH and salt concentration, three flagellin monomers can spontaneously reaggregate to form structures which appear identical to intact flagella.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Alkaline Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Sigma Factor: A protein which is a subunit of RNA polymerase. It effects initiation of specific RNA chains from DNA.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Phosphates: Inorganic salts of phosphoric acid.Operon: In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.Interleukin-18 Receptor beta Subunit: A subunit of the interleukin-18 receptor that plays a role in receptor signaling by association of its cytoplasmic domain with SIGNAL TRANSDUCING ADAPTOR PROTEINS such as MYELOID DIFFERENTIATION FACTOR 88.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.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.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.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.Receptors, Interleukin-1: Cell surface receptors that are specific for INTERLEUKIN-1. Included under this heading are signaling receptors, non-signaling receptors and accessory proteins required for receptor signaling. Signaling from interleukin-1 receptors occurs via interaction with SIGNAL TRANSDUCING ADAPTOR PROTEINS such as MYELOID DIFFERENTIATION FACTOR 88.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.Alkanes: The generic name for the group of aliphatic hydrocarbons Cn-H2n+2. They are denoted by the suffix -ane. (Grant & Hackh's Chemical Dictionary, 5th ed)Candida: A genus of yeast-like mitosporic Saccharomycetales fungi characterized by producing yeast cells, mycelia, pseudomycelia, and blastophores. It is commonly part of the normal flora of the skin, mouth, intestinal tract, and vagina, but can cause a variety of infections, including CANDIDIASIS; ONYCHOMYCOSIS; vulvovaginal candidiasis (CANDIDIASIS, VULVOVAGINAL), and thrush (see CANDIDIASIS, ORAL). (From Dorland, 28th ed)Candida tropicalis: A species of MITOSPORIC FUNGI that is a major cause of SEPTICEMIA and disseminated CANDIDIASIS, especially in patients with LYMPHOMA; LEUKEMIA; and DIABETES MELLITUS. It is also found as part of the normal human mucocutaneous flora.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.Acetoacetates: Salts and derivatives of acetoacetic acid.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)Diploidy: The chromosomal constitution of cells, in which each type of CHROMOSOME is represented twice. Symbol: 2N or 2X.Hydroxymethylglutaryl-CoA Synthase: An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. This enzyme was formerly listed as EC 4.1.3.5.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Oligonucleotide Array Sequence Analysis: Hybridization of a nucleic acid sample to a very large set of OLIGONUCLEOTIDE PROBES, which have been attached individually in columns and rows to a solid support, to determine a BASE SEQUENCE, or to detect variations in a gene sequence, GENE EXPRESSION, or for GENE MAPPING.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Computer Graphics: The process of pictorial communication, between human and computers, in which the computer input and output have the form of charts, drawings, or other appropriate pictorial representation.Click Chemistry: Organic chemistry methodology that mimics the modular nature of various biosynthetic processes. It uses highly reliable and selective reactions designed to "click" i.e., rapidly join small modular units together in high yield, without offensive byproducts. In combination with COMBINATORIAL CHEMISTRY TECHNIQUES, it is used for the synthesis of new compounds and combinatorial libraries.Data Display: The visual display of data in a man-machine system. An example is when data is called from the computer and transmitted to a CATHODE RAY TUBE DISPLAY or LIQUID CRYSTAL display.Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.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.Hevea: A plant genus of the family EUPHORBIACEAE, order Euphorbiales, subclass Rosidae. Commercial natural RUBBER is mainly obtained from Hevea brasiliensis but also from some other plants.Latex: A milky, product excreted from the latex canals of a variety of plant species that contain cauotchouc. Latex is composed of 25-35% caoutchouc, 60-75% water, 2% protein, 2% resin, 1.5% sugar & 1% ash. RUBBER is made by the removal of water from latex.(From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed). Hevein proteins are responsible for LATEX HYPERSENSITIVITY. Latexes are used as inert vehicles to carry antibodies or antigens in LATEX FIXATION TESTS.Rubber: A high-molecular-weight polymeric elastomer derived from the milk juice (LATEX) of HEVEA brasiliensis and other trees and plants. It is a substance that can be stretched at room temperature to at least twice its original length and after releasing the stress, retract rapidly, and recover its original dimensions fully.Transformation, Genetic: Change brought about to an organisms genetic composition by unidirectional transfer (TRANSFECTION; TRANSDUCTION, GENETIC; CONJUGATION, GENETIC, etc.) and incorporation of foreign DNA into prokaryotic or eukaryotic cells by recombination of part or all of that DNA into the cell's genome.Bioreactors: Tools or devices for generating products using the synthetic or chemical conversion capacity of a biological system. They can be classical fermentors, cell culture perfusion systems, or enzyme bioreactors. For production of proteins or enzymes, recombinant microorganisms such as bacteria, mammalian cells, or insect or plant cells are usually chosen.BrazilEuphorbiaceae: The spurge family of flowering plants, in the order Euphorbiales, contains some 7,500 species in 275 genera. The family consists of annual and perennial herbs and woody shrubs or trees.Asclepiadaceae: The milkweed plant family of the order Gentianales, subclass Asteridae, class Magnoliopsida. It includes many tropical herbs and shrubby climbers; most with milky juice. Flowers have five united petals. Fruits are podlike, usually with tufted seeds.Transformation, Bacterial: The heritable modification of the properties of a competent bacterium by naked DNA from another source. The uptake of naked DNA is a naturally occuring phenomenon in some bacteria. It is often used as a GENE TRANSFER TECHNIQUE.Apocynaceae: The dogbane family of the order Gentianales. Members of the family have milky, often poisonous juice, smooth-margined leaves, and flowers in clusters. Asclepiadacea (formerly the milkweed family) has been included since 1999 and before 1810.
(1/222) Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic.

Poly(3-hydroxyalkanoates) (PHAs) are a class of microbially produced polyesters that have potential applications as conventional plastics, specifically thermoplastic elastomers. A wealth of biological diversity in PHA formation exists, with at least 100 different PHA constituents and at least five different dedicated PHA biosynthetic pathways. This diversity, in combination with classical microbial physiology and modern molecular biology, has now opened up this area for genetic and metabolic engineering to develop optimal PHA-producing organisms. Commercial processes for PHA production were initially developed by W. R. Grace in the 1960s and later developed by Imperial Chemical Industries, Ltd., in the United Kingdom in the 1970s and 1980s. Since the early 1990s, Metabolix Inc. and Monsanto have been the driving forces behind the commercial exploitation of PHA polymers in the United States. The gram-negative bacterium Ralstonia eutropha, formerly known as Alcaligenes eutrophus, has generally been used as the production organism of choice, and intracellular accumulation of PHA of over 90% of the cell dry weight have been reported. The advent of molecular biological techniques and a developing environmental awareness initiated a renewed scientific interest in PHAs, and the biosynthetic machinery for PHA metabolism has been studied in great detail over the last two decades. Because the structure and monomeric composition of PHAs determine the applications for each type of polymer, a variety of polymers have been synthesized by cofeeding of various substrates or by metabolic engineering of the production organism. Classical microbiology and modern molecular bacterial physiology have been brought together to decipher the intricacies of PHA metabolism both for production purposes and for the unraveling of the natural role of PHAs. This review provides an overview of the different PHA biosynthetic systems and their genetic background, followed by a detailed summation of how this natural diversity is being used to develop commercially attractive, recombinant processes for the large-scale production of PHAs.  (+info)

(2/222) Pregnenolone esterification in Saccharomyces cerevisiae. A potential detoxification mechanism.

While studying the effect of steroids on the growth of the yeast Saccharomyces cerevisiae, we found that pregnenolone was converted into the acetate ester. This reaction was identified as a transfer of the acetyl group from acetyl-CoA to the 3beta-hydroxyl group of pregnenolone. The corresponding enzyme, acetyl-CoA:pregnenolone acetyltransferase (APAT) is specific for Delta5- or Delta4-3beta-hydroxysteroids and short-chain acyl-CoAs. The apparent Km for pregnenolone is approximately 0.5 microm. The protein associated with APAT activity was partially purified and finally isolated from an SDS/polyacrylamide gel. Tryptic peptides were generated and N-terminally sequenced. Two peptide sequences allowed the identification of an open reading frame (YGR177c, in the S. cerevisiae genome database) translating into a 62-kDa protein of hitherto unknown function. This protein encoded by a gene known as ATF2 displays 37% identity with an alcohol acetyltransferase encoded by the yeast gene ATF1. Disruption of ATF2 led to the complete elimination of APAT activity and consequently abolished the esterification of pregnenolone. In addition, a toxic effect of pregnenolone linked to the disruption of ATF2 was observed. Pregnenolone toxicity is more pronounced when the atf2-Delta mutation is introduced in a yeast strain devoid of the ATP-binding cassette transporters, PDR5 and SNQ2. Our results suggest that Atf2p (APAT) plays an active role in the detoxification of 3beta-hydroxysteroids in association with the efflux pumps Pdr5p and Snq2p.  (+info)

(3/222) A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1.

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself.  (+info)

(4/222) Origin of gene overlap: the case of TCP1 and ACAT2.

The human acetyl-CoA acetyltransferase 2 gene, ACAT2, codes for a thiolase, an enzyme involved in lipid metabolism. The human T-complex protein 1 gene, TCP1, encodes a molecular chaperone of the chaperonin family. The two genes overlap by their 3'-untranslated regions, their coding sequences being located on opposite DNA strands in a tail-to-tail orientation. To find out how the overlap might have arisen in evolution, the homologous genes of the zebrafish, the African toad, caiman, platypus, opossum, and wallaby were identified. In each species, standard or long polymerase chain reactions were used to determine whether the ACAT2 and TCP1 homologs are closely linked and, if so, whether they overlap. The results reveal that the overlap apparently arose during the transition from therapsid reptiles to mammals and has been retained for >200 million years. Part of the overlapping untranslated region shows remarkable sequence conservation. The overlap presumably arose during the chromosomal rearrangement that brought the two unrelated and previously separated genes together. One or both of the transposed genes found by chance signals that are necessary for the processing of their transcripts to be present on the noncoding strand of the partner gene.  (+info)

(5/222) Development and characterization of a gene expression reporter system for Clostridium acetobutylicum ATCC 824.

A gene expression reporter system (pHT3) for Clostridium acetobutylicum ATCC 824 was developed by using the lacZ gene from Thermoanaerobacterium thermosulfurogenes EM1 as the reporter gene. In order to test the reporter system, promoters of three key metabolic pathway genes, ptb (coding for phosphotransbutyrylase), thl (coding for thiolase), and adc (coding for acetoacetate decarboxylase), were cloned upstream of the reporter gene in pHT3 in order to construct vectors pHT4, pHT5, and pHTA, respectively. Detection of beta-galactosidase activity in time course studies performed with strains ATCC 824(pHT4), ATCC 824(pHT5), and ATCC 824(pHTA) demonstrated that the reporter gene produced a functional beta-galactosidase in C. acetobutylicum. In addition, time course studies revealed differences in the beta-galactosidase specific activity profiles of strains ATCC 824(pHT4), ATCC 824(pHT5), and ATCC 824(pHTA), suggesting that the reporter system developed in this study is able to effectively distinguish between different promoters. The stability of the beta-galactosidase produced by the reporter gene was also examined with strains ATCC 824(pHT4) and ATCC 824(pHT5) by using chloramphenicol treatment to inhibit protein synthesis. The data indicated that the beta-galactosidase produced by the lacZ gene from T. thermosulfurogenes EM1 was stable in the exponential phase of growth. In pH-controlled fermentations of ATCC 824(pHT4), the kinetics of beta-galactosidase formation from the ptb promoter and phosphotransbutyrylase formation from its own autologous promoter were found to be similar.  (+info)

(6/222) A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.

BACKGROUND: Thiolases are ubiquitous and form a large family of dimeric or tetrameric enzymes with a conserved, five-layered alphabetaalphabetaalpha catalytic domain. Thiolases can function either degradatively, in the beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic thiolases catalyze the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in a wide range of biosynthetic pathways, including those that generate cholesterol, steroid hormones, and various energy-storage molecules. RESULTS: The crystal structure of the tetrameric biosynthetic thiolase from Zoogloea ramigera has been determined at 2.0 A resolution. The structure contains a striking and novel 'cage-like' tetramerization motif, which allows for some hinge motion of the two tight dimers with respect to each other. The protein crystals were flash-frozen after a short soak with the enzyme's substrate, acetoacetyl-CoA. A reaction intermediate was thus trapped: the enzyme tetramer is acetylated at Cys89 and has a CoA molecule bound in each of its active-site pockets. CONCLUSIONS: The shape of the substrate-binding pocket reveals the basis for the short-chain substrate specificity of the enzyme. The active-site architecture, and in particular the position of the covalently attached acetyl group, allow a more detailed reaction mechanism to be proposed in which Cys378 is involved in both steps of the reaction. The structure also suggests an important role for the thioester oxygen atom of the acetylated enzyme in catalysis.  (+info)

(7/222) Aberrant oxidation of the cholesterol side chain in bile acid synthesis of sterol carrier protein-2/sterol carrier protein-x knockout mice.

Peroxisomal beta-oxidation plays an important role in the metabolism of a wide range of substrates, including various fatty acids and the steroid side chain in bile acid synthesis. Two distinct thiolases have been implicated to function in peroxisomal beta-oxidation: the long known 41-kDa beta-ketothiolase identified by Hashimoto and co-workers (Hijikata, M., Ishii, N., Kagamiyama, H., Osumi, T., and Hashimoto, T. (1987) J. Biol. Chem. 262, 8151-8158) and the recently discovered 60-kDa SCPx thiolase, that consists of an N-terminal domain with beta-ketothiolase activity and a C-terminal moiety of sterol carrier protein-2 (SCP2, a lipid carrier or transfer protein). Recently, gene targeting of the SCP2/SCPx gene has shown in mice that the SCPx beta-ketothiolase is involved in peroxisomal beta-oxidation of 2-methyl-branched chain fatty acids like pristanic acid. In our present work we have investigated bile acid synthesis in the SCP2/SCPx knockout mice. Specific inhibition of beta-oxidation at the thiolytic cleavage step in bile acid synthesis is supported by our finding of pronounced accumulation in bile and serum from the knockout mice of 3alpha,7alpha, 12alpha-trihydroxy-27-nor-5beta-cholestane-24-one (which is a known bile alcohol derivative of the cholic acid synthetic intermediate 3alpha,7alpha,12alpha-trihydroxy-24-keto-cholestano yl-coenzyme A). Moreover, these mice have elevated concentrations of bile acids with shortened side chains (i.e. 23-norcholic acid and 23-norchenodeoxycholic acid), which may be produced via alpha- rather than beta-oxidation. Our results demonstrate that the SCPx thiolase is critical for beta-oxidation of the steroid side chain in conversion of cholesterol into bile acids.  (+info)

(8/222) Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method.

Sterol carrier protein X (SCPx) plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. To investigate whether patients with an unresolved defect in peroxisomal beta-oxidation are deficient for SCPx, we developed a novel and specific assay to measure the activity of SCPx in both liver and fibroblast homogenates. The substrate used in the assay, 3alpha, 7alpha,12alpha-trihydroxy-24-keto-5beta-cholestanoy l-CoA (24-keto-THC-CoA), is produced by preincubating the enoyl-CoA of the bile acid intermediate THCA with a lysate from the yeast Saccharomyces cerevisiae expressing human D-bifunctional protein. After the preincubation period, liver or fibroblast homogenate is added plus CoASH, and the production of choloyl-CoA is determined by HPLC. The specificity of the assay was demonstrated by the finding of a full deficiency in fibroblasts from an SCPx knock-out mouse. In addition to SCPx activity measurements in fibroblasts from patients with a defect in peroxisomal beta-oxidation of unresolved etiology, we studied the stability and activity of SCPx in fibroblasts from patients with Zellweger syndrome, which lack functional peroxisomes. We found that SCPx is not only stable in the cytosol, but displays a higher activity in fibroblasts from patients with Zellweger syndrome than in control fibroblasts. Furthermore, in all patients studied with a defect in peroxisomal beta-oxidation of unknown origin, SCPx was found to be normally active, indicating that human SCPx deficiency remains to be identified.  (+info)

*  Acetyl-CoA C-acetyltransferase
CoA + acetoacetyl-CoA Hence, this enzyme has one substrate, acetyl-CoA, and two products, CoA and acetoacetyl-CoA. Acetyl-CoA C ... acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, and thiolase II. This enzyme ... In enzymology, an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) is an enzyme that catalyzes the chemical reaction 2 acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include ...
*  SGSH
... acetyl CoA:alpha-glucosaminide acetyltransferase (type C; MIM 252930); and N-acetylglucosamine 6-sulfatase (type D; MIM 252940 ...
*  Alkylglycerophosphate 2-O-acetyltransferase
CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate Thus, the two substrates of this enzyme are acetyl-CoA and 1-alkyl-sn-glycero-3- ... 1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase. This enzyme is also called alkyllyso-GP:acetyl-CoA acetyltransferase. ... Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen". J. Biol. Chem. 261 ( ... The systematic name of this enzyme class is acetyl-CoA: ... whereas its two products are CoA and 1-alkyl-2-acetyl-sn- ...
*  Phosphate acetyltransferase
CoA + acetyl phosphate The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl ... In enzymology, a phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:phosphate acetyltransferase. Other names in common use include ...
*  Monoterpenol O-acetyltransferase
In enzymology, a monoterpenol O-acetyltransferase (EC 2.3.1.69) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:monoterpenol O-acetyltransferase. This enzyme is also called menthol ... the two substrates of this enzyme are acetyl-CoA and monoterpenol, whereas its two products are CoA and monoterpenol acetate ... a monoterpenol ⇌ {\displaystyle \rightleftharpoons } CoA + a monoterpenol acetate ester Thus, ...
*  Arylamine N-acetyltransferase
4-aminobiphenyl N-acetyltransferase, acetyl CoA-arylamine N-acetyltransferase, 2-naphthylamine N-acetyltransferase, arylamine ... In enzymology, an arylamine N-acetyltransferase (EC 2.3.1.5) is an enzyme that catalyzes the chemical reaction acetyl-CoA + an ... The systematic name of this enzyme class is acetyl-CoA:arylamine N-acetyltransferase. Other names in common use include ... N-acetyltransferase, p-aminosalicylate N-acetyltransferase, serotonin acetyltransferase, and serotonin N-acetyltransferase. As ...
*  Imidazole N-acetyltransferase
CoA + N-acetylimidazole Thus, the two substrates of this enzyme are acetyl-CoA and imidazole, whereas its two products are CoA ... In enzymology, an imidazole N-acetyltransferase (EC 2.3.1.2) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:imidazole N-acetyltransferase. Other names in common use include ... imidazole acetylase, and imidazole acetyltransferase. Kinsky SC (1960). "Assay, purification, and properties of imidazole ...
*  Alcohol O-acetyltransferase
CoA + an acetyl ester Thus, the two substrates of this enzyme are acetyl-CoA and alcohol, whereas its two products are CoA and ... In enzymology, an alcohol O-acetyltransferase (EC 2.3.1.84) is an enzyme that catalyzes the chemical reaction acetyl-CoA + an ... The systematic name of this enzyme class is acetyl-CoA:alcohol O-acetyltransferase. This enzyme is also called alcohol ... Yoshioka K; Hashimoto N (1981). "Ester formation by alcohol acetyltransferase from brewers' yeast". Agric. Biol. Chem. 45: 2183 ...
*  Formate C-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:formate C-acetyltransferase. Other names in common use include pyruvate ... The coenzyme-A radical then picks up the acetyl group from Cys418 to generate acetyl-CoA, leaving behind a Cys418 radical. ... it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows: ... Activated pyruvate formate lyase allows formation of acetyl-CoA, a small molecule important in the production of energy, when ...
*  Peptide alpha-N-acetyltransferase
Nalpha-acetyltransferase, amino-terminal amino acid-acetylating enzyme, and acetyl-CoA:peptide alpha-N-acetyltransferase. As of ... In enzymology, a peptide alpha-N-acetyltransferase (EC 2.3.1.88) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:peptide Nalpha-acetyltransferase. Other names in common use include beta ... the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nalpha-acetylpeptide and CoA. This ...
*  Maltose O-acetyltransferase
CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose Thus, the two substrates of this enzyme are acetyl-CoA and maltose, ... The systematic name of this enzyme class is acetyl-CoA:maltose O-acetyltransferase. Other names in common use include maltose ... In enzymology, a maltose O-acetyltransferase (EC 2.3.1.79) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... whereas its two products are CoA and [[6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose]]. This enzyme belongs to the family ...
*  Cortisol O-acetyltransferase
CoA + cortisol 21-acetate Thus, the two substrates of this enzyme are acetyl-CoA and cortisol, whereas its two products are CoA ... The systematic name of this enzyme class is acetyl-CoA:cortisol O-acetyltransferase. Other names in common use include cortisol ... In enzymology, a cortisol O-acetyltransferase (EC 2.3.1.27) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... corticosteroid acetyltransferase, and corticosteroid-21-O-acetyltransferase. Thomas PJ (1968). "Cortisol acetyltransferase from ...
*  Phenylalanine N-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl- ... CoA + N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... CoA-L-phenylalanine alpha-N-acetyltransferase. This enzyme participates in phenylalanine metabolism. Leuzinger W, Baker AL, ...
*  Serine O-acetyltransferase
CoA + O-acetyl-L-serine Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA ... The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, ... In enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the ...
*  Polysialic-acid O-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:polysialic-acid O-acetyltransferase. Other names in common use include ... CoA + polysialic acid acetylated on O-7 or O-9 Thus, the two substrates of this enzyme are acetyl-CoA and alpha-2,8-linked ... In enzymology, a polysialic-acid O-acetyltransferase (EC 2.3.1.136) is an enzyme that catalyzes the chemical reaction acetyl- ... Higa HH, Varki A (1988). "Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1-positive Escherichia coli. The enzyme ...
*  D-tryptophan N-acetyltransferase
Other names in common use include D-tryptophan acetyltransferase, and acetyl-CoA-D-tryptophan-alpha-N-acetyltransferase. Zenk ... N-acetyl-D-tryptophan Thus, the two substrates of this enzyme are acetyl-CoA and D-tryptophan, whereas its two products are CoA ... In enzymology, a D-tryptophan N-acetyltransferase (EC 2.3.1.34) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:D-tryptophan N-acetyltransferase. ...
*  Thioethanolamine S-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:2-aminoethanethiol S-acetyltransferase. Other names in common use ... include thioltransacetylase B, thioethanolamine acetyltransferase, and acetyl-CoA:thioethanolamine S-acetyltransferase. BRADY ... CoA + S-(2-aminoethyl)thioacetate Thus, the two substrates of this enzyme are acetyl-CoA and 2-aminoethanethiol, whereas its ... In enzymology, a thioethanolamine S-acetyltransferase (EC 2.3.1.11) is an enzyme that catalyzes the chemical reaction acetyl- ...
*  Histidine N-acetyltransferase
N-acetyl-L-histidine Thus, the two substrates of this enzyme are acetyl-CoA and L-histidine, whereas its two products are CoA ... In enzymology, a histidine N-acetyltransferase (EC 2.3.1.33) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-histidine N-acetyltransferase. Other names in common use include ... Baslow MH (1966). "N -acetyl-L-histidine synthetase activity from the brain of the killifish". Brain Res. 3 (2): 210-3. doi: ...
*  Aspartate N-acetyltransferase
N-acetyl-L-aspartate Thus, the two substrates of this enzyme are acetyl-CoA and L-aspartate, whereas its two products are CoA ... In enzymology, an aspartate N-acetyltransferase (EC 2.3.1.17) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-aspartate N-acetyltransferase. Other names in common use include ... aspartate acetyltransferase, and L-aspartate N-acetyltransferase. Goldstein FB (1959). "Biosynthesis of N-acetyl-L-aspartic ...
*  Glucosamine N-acetyltransferase
CoA + N-acetyl-D-glucosamine Thus, the two substrates of this enzyme are acetyl-CoA and D-glucosamine, whereas its two products ... In enzymology, a glucosamine N-acetyltransferase (EC 2.3.1.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + D- ... The systematic name of this enzyme class is acetyl-CoA:D-glucosamine N-acetyltransferase. Other names in common use include ... are CoA and N-acetyl-D-glucosamine. This enzyme belongs to the family of transferases, specifically those acyltransferases ...
*  Hydrogen-sulfide S-acetyltransferase
CoA + thioacetate Thus, the two substrates of this enzyme are acetyl-CoA and hydrogen sulfide, whereas its two products are CoA ... The systematic name of this enzyme class is acetyl-CoA:hydrogen-sulfide S-acetyltransferase. This enzyme is also called ... In enzymology, a hydrogen-sulfide S-acetyltransferase (EC 2.3.1.10) is an enzyme that catalyzes the chemical reaction acetyl- ... hydrogen-sulfide acetyltransferase. BRADY RO, STADTMAN ER (1954). "Enzymatic thioltransacetylation". J. Biol. Chem. 211 (2): ...
*  Salutaridinol 7-O-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:salutaridinol 7-O-acetyltransferase. This enzyme participates in ... CoA + 7-O-acetylsalutaridinol Thus, the two substrates of this enzyme are acetyl-CoA and salutaridinol, whereas its two ... In enzymology, a salutaridinol 7-O-acetyltransferase (EC 2.3.1.150) is an enzyme that catalyzes the chemical reaction acetyl- ... doi:10.1016/S0040-4039(00)76696-2. Lenz R, Zenk MH (1995). "Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from papaver ...
*  N-hydroxyarylamine O-acetyltransferase
The systematic name of this enzyme class is acetyl-CoA:N-hydroxyarylamine O-acetyltransferase. Other names in common use ... CoA + an N-acetoxyarylamine Thus, the two substrates of this enzyme are acetyl-CoA and N-hydroxyarylamine, whereas its two ... In enzymology, a N-hydroxyarylamine O-acetyltransferase (EC 2.3.1.118) is an enzyme that catalyzes the chemical reaction acetyl ... include arylhydroxamate N,O-acetyltransferase, arylamine N-acetyltransferase, and N-hydroxy-2-aminofluorene-O-acetyltransferase ...
*  Leucine N-acetyltransferase
CoA + N-acetyl-L-leucine Thus, the two substrates of this enzyme are acetyl-CoA and L-leucine, whereas its two products are CoA ... In enzymology, a leucine N-acetyltransferase (EC 2.3.1.66) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine ... Isolation and properties of an enzyme synthesizing acetyl-L-leucine". J. Antibiot. 33 (8): 857-862. doi:10.7164/antibiotics. ...
*  HGSNAT
... "acetyl-CoA:heparan-α-D-glucosaminide N-acetyltransferase" and "acetyl-CoA:alpha-glucosaminide N-acetyltransferase") is an ... acetyl-CoA + heparan sulfate α-D-glucosaminide ⇌ {\displaystyle \rightleftharpoons } CoA + heparan sulfate N-acetyl-α-D- ... Pohlmann R, Klein U, Fromme HG, von Figura K (1981). "Localisation of acetyl-CoA: alpha-glucosaminide N-acetyltransferase in ... deficiency of acetyl-CoA:alpha-glucosaminide N-acetyltransferase in skin fibroblasts". Proc. Natl. Acad. Sci. U.S.A. 75 (10): ...
*  ACAT2
... acetyl-Coenzyme A acetyltransferase 2) gene Acetyl-Coenzyme A acetyltransferase 2 is an acetyl-CoA C-acetyltransferase enzyme. ... Acetyl-CoA acetyltransferase, cytosolic, also known as cytosolic acetoacetyl-CoA thiolase, is an enzyme that in humans is ... acetyl-Coenzyme A acetyltransferase 2". Human ACAT2 genome location and ACAT2 gene details page in the UCSC Genome Browser. ... He X, Lu Y, Saha N, Yang H, Heng CK (Dec 2005). "Acyl-CoA: cholesterol acyltransferase-2 gene polymorphisms and their ...
phaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & protein  phaA - Acetyl-CoA acetyltransferase - Zoogloea ramigera - phaA gene & protein
2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation. ,p>Manual validated information which has been generated by ... mevalonate from acetyl-CoA.. Proteins known to be involved in the 3 steps of the subpathway in this organism are:. *Acetyl-CoA ... sp,P07097,THIL_ZOORA Acetyl-CoA acetyltransferase OS=Zoogloea ramigera GN=phaA PE=1 SV=4 ... mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis. ...
more infohttp://www.uniprot.org/uniprot/P07097
Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...  Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast,...
keywords = "3-ketoacyl-CoA thiolase, Acetoacetyl-CoA thiolase, Candida tropicalis, Cytosol, Mevalonate, Peroxisome", ... Ueda M, Kanayama N, Tanaka A. Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane- ... Ueda, M, Kanayama, N & Tanaka, A 2000, 'Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n- ... Ueda, M., Kanayama, N., & Tanaka, A. (2000). Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes ...
more infohttps://okayama.pure.elsevier.com/en/publications/genetic-evaluation-of-peroxisomal-and-cytosolic-acetoacetyl-coa-t
Choline acetyltransferase activity in rat heart after transplantation. - Semantic Scholar  Choline acetyltransferase activity in rat heart after transplantation. - Semantic Scholar
Acetyl-CoA + Choline in equilibrium Acetylcholine + CoA. To demonstrate the neuronal relationship of this enzyme, CAT activity ... Choline acetyltransferase activity decreased 98% in the right atrium of the transplanted denervated hearts, 94% in the SA node ... Choline acetyltransferase (CAT) catalyzes the biosynthesis of acetylcholine according to the chemical equation: ... Choline acetyltransferase (CAT) catalyzes the biosynthesis of acetylcholine according to the chemical equation: Acetyl-CoA + ...
more infohttps://www.semanticscholar.org/paper/Choline-acetyltransferase-activity-in-rat-heart-af-Lund-Schmid/3cdbfe4895f564edc24ab28d022c98c0c1a78aae
Acetyl-CoA:N-acetyltransferase | definition of acetyl-CoA:N-acetyltransferase by Medical dictionary  Acetyl-CoA:N-acetyltransferase | definition of acetyl-CoA:N-acetyltransferase by Medical dictionary
What is acetyl-CoA:N-acetyltransferase? Meaning of acetyl-CoA:N-acetyltransferase medical term. What does acetyl-CoA:N- ... N-acetyltransferase in the Medical Dictionary? acetyl-CoA:N-acetyltransferase explanation free. ... redirected from acetyl-CoA:N-acetyltransferase) a·ce·tyl-CoA a·ce·tyl·trans·fer·ase. an acetyltransferase forming acetoacetyl- ... Acetyl-CoA:N-acetyltransferase , definition of acetyl-CoA:N-acetyltransferase by Medical dictionary https://medical-dictionary. ...
more infohttps://medical-dictionary.thefreedictionary.com/acetyl-CoA%3AN-acetyltransferase
Acetyl-CoA C-acetyltransferase - Wikipedia  Acetyl-CoA C-acetyltransferase - Wikipedia
CoA + acetoacetyl-CoA Hence, this enzyme has one substrate, acetyl-CoA, and two products, CoA and acetoacetyl-CoA. Acetyl-CoA C ... acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, and thiolase II. This enzyme ... In enzymology, an acetyl-CoA C-acetyltransferase (EC 2.3.1.9) is an enzyme that catalyzes the chemical reaction 2 acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include ...
more infohttps://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase
Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D | Disease page | IUPHAR/BPS Guide to PHARMACOLOGY  Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D | Disease page | IUPHAR/BPS Guide to PHARMACOLOGY
Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D disease page. Quantitative data and detailed annnotation of the targets of ... Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D. GtoPdb Disease Summaries. This section gives an overview of the disease, and ... No ligand related data available for Acetyl-CoA acetyltransferase-2 deficiency; ACAT2D ...
more infohttp://guidetopharmacology.org/GRAC/DiseaseDisplayForward?diseaseId=20
ACAT1 elisa kit | Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP 659033.1  ACAT1 elisa kit | Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP 659033.1
Mouse Acetyl-CoA acetyltransferase ELISA Kit-NP_659033.1 (MBS285428) product datasheet at MyBioSource, ELISA Kits ... Biological Process: acetyl-CoA biosynthetic process; acetyl-CoA catabolic process; coenzyme A biosynthetic process; coenzyme A ... Molecular Function: acetyl-CoA C-acetyltransferase activity; carbon-carbon lyase activity; catalytic activity; coenzyme binding ... 1. Data show that microRNA miR-467b regulates the acetyl-CoA acetyltransferase 1 (ACAT1) expression via targeting ACAT1 3' ...
more infohttps://www.mybiosource.com/acat1-mouse-elisa-kits/acetyl-coa-acetyltransferase/285428
Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...  Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat...
In addition, the enzyme preferred acetyl-CoA to palmitoyl-CoA or oleoyl-CoA as substrate. ... acetyl-CoA acetyltransferase from rat spleen. J Gomez-Cambronero, S Velasco, M Sanchez-Crespo, F Vivanco, J M Mato ... The enzyme 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine: acetyl-CoA acetyltransferase (EC 2.3.1.67) was purified from rat ... Partial purification and characterization of 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine:acetyl-CoA acetyltransferase from rat ...
more infohttp://www.biochemj.org/content/237/2/439
Acetyl CoA-deacetylcephalosporin C acetyltransferase: Definition with Acetyl CoA-deacetylcephalosporin C acetyltransferase...  Acetyl CoA-deacetylcephalosporin C acetyltransferase: Definition with Acetyl CoA-deacetylcephalosporin C acetyltransferase...
Definition of Acetyl CoA-deacetylcephalosporin C acetyltransferase with photos and pictures, translations, sample usage, and ... acetyl-CoA c-acyltransferase. acetyl-CoA carboxylase. acetyl-CoA deacylase. acetyl-CoA hydrolase. acetyl-CoA ligase. acetyl-CoA ... Lexicographical Neighbors of Acetyl CoA-deacetylcephalosporin C Acetyltransferase. acetyl-CoA acylase. acetyl-CoA ... acetyl CoA carboxylase phosphatase. acetyl chloride. acetyl group. acetyl methylcarbinol. acetyl phosphate. acetyl radical. ...
more infohttp://www.lexic.us/definition-of/acetyl_CoA-deacetylcephalosporin_C_acetyltransferase
Antibody Database - Reagents for the antigen ACAT1 / acetyl-CoA acetyltransferase 1 stained with Alkaline Phosphatase (AP)  Antibody Database - Reagents for the antigen 'ACAT1 / acetyl-CoA acetyltransferase 1' stained with 'Alkaline Phosphatase (AP)'
... acetyl-CoA acetyltransferase 1' stained with 'Alkaline Phosphatase (AP)' in the Antibody Database ... acetyl-CoA acetyltransferase 1 Alkaline Phosphatase (AP) Antibodies. Antibodies in the Chromocyte database for ACAT1 / acetyl- ...
more infohttps://www.chromocyte.com/Antibody-Database/Antigen/ACAT1---acetyl-CoA-acetyltransferase-1_3626/Alkaline-Phosphatase--AP-_240
Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac...  Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac...
Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ... Cytosolic Carnitine Acetyltransferase as a Source of Cytosolic Acetyl-CoA: A Possible Mechanism for Regulation of Cardiac ...
more infohttp://www.biochemj.org/content/early/2018/02/07/BCJ20170823
Atomic resolution structure of human alpha-tubulin acetyltransferase
   bound to acetyl-CoA :: MPG.PuRe
				  Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA :: MPG.PuRe
Atomic resolution structure of human alpha-tubulin acetyltransferase,br/, bound to acetyl-CoA ... Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA ... human alpha-tubulin acetyltransferase bound to acetyl-CoA. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES ... we present the structure of the human alpha-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at ...
more infohttp://pubman.mpdl.mpg.de/pubman/faces/viewItemOverviewPage.jsp?itemId=escidoc:1609330
Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. -  Test catalog - Centro de...  Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. - Test catalog - Centro de...
Acetyl-CoA:alpha-glucosaminide N-acetyltransferase 50 - 171. nmol/h/mg prot.. ... Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts.. Fee code: 16025 ... Home > Test catalog > Acetyl-CoA:alpha-glucosaminide N-acetyltransferase (Sanfilippo syndrome type C), fibroblasts. ...
more infohttp://cdb.hospitalclinic.org/en_catalogo-cdb/248578081/acetyl-coaalpha-glucosaminide-n-acetyltransferase-sanfilippo-syndrome-type-c-fibroblasts
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...
... acetyl Coenzyme A hydrolysis by human arylamine N-acetyltransferase Type 1/murine arylamine N-acetyltransferase Type 2, open up ... no acetyl Coenzyme A hydrolysis was found when murine arylamine N-acetyltransferase Type 1 or recombinant bacterial arylamine N ... revealing that the disappearance of acetyl CH3 from acetyl Coenzyme A occurred concomitantly with the appearance of a CH3 peak ... Furthermore, in silico docking of folate within the active site of human arylamine N-acetyltransferase Type 1 suggests that ...
more infohttps://pharm.ox.ac.uk/publications/465131
ACAT1 Gene - GeneCards | THIL Protein | THIL Antibody  ACAT1 Gene - GeneCards | THIL Protein | THIL Antibody
Acetyl-CoA Acetyltransferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... ACAT1 (Acetyl-CoA Acetyltransferase 1) is a Protein Coding gene. Diseases associated with ACAT1 include Alpha-Methylacetoacetic ... 2 acetyl-CoA = CoA + acetoacetyl-CoA. *THIL_HUMAN,P24752. UniProtKB/Swiss-Prot EnzymeRegulation: Activated by potassium ions, ... a mitochondrially localized enzyme that catalyzes the reversible formation of acetoacetyl-CoA from two molecules of acetyl-CoA ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=ACAT1&keywords=hsa-mir-1260b
Center for Structural Genomics of Infectious Diseases - Deposits  Center for Structural Genomics of Infectious Diseases - Deposits
Crystal structure of the Bacillus anthracis acetyl-CoA acetyltransferase. (tree view). Edit deposit information. CSGID target. ...
more infohttps://csgid.org/deposits/view/3SS6
Zeitschrift für Naturforschung C  Zeitschrift für Naturforschung C
Acetyl-CoA:4-Hydroxybutinylbithiophene O-Acetyltransferase Isoenzymes from Tagetes patula Seedlings. Metschulat, Gernot / ...
more infohttps://www.degruyter.com/view/j/znc.1987.42.issue-7-8/issue-files/znc.1987.42.issue-7-8.xml
Integrated metabolome and transcriptome analysis of Magnolia champaca identifies biosynthetic pathways for floral volatile...  Integrated metabolome and transcriptome analysis of Magnolia champaca identifies biosynthetic pathways for floral volatile...
... acetyl-CoA acetyltransferase; HMGS, hydroxymethylglutaryl-CoA synthase; HMGR, hydroxymethylglutaryl-CoA reductase; MVK, ... 4-coumaroyl-CoA ligase; CCoAOMT, caffeoyl-CoA 3-O-methyltransferase; CCR, cinnamoyl-CoA reductase; CAD, cinnamyl alcohol ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/28615048
Treesearch - scientific articles written or published by the U.S. Forest Service  Treesearch - scientific articles written or published by the U.S. Forest Service
acetoacetyl-CoA, acetyl-CoA acetyltransferase, b-oxidation, ectomycorrhizae, Laccaria bicolor, Pinus resinosa, symbiosis ... Symbiosis-regulated expression of an acetyl-CoA acetyltransferase gene in the ectomycorrhizal fungus Laccaria bicolor. The ...
more infohttps://www.fs.usda.gov/treesearch/search?keywords=%22symbiosis%22
  • Here, we present the structure of the human alpha-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 angstrom resolution. (mpg.de)
  • Proton nuclear magnetic resonance spectroscopy allowed chemical modifications occurring during the catalytic reaction to be analysed in real time, revealing that the disappearance of acetyl CH3 from acetyl Coenzyme A occurred concomitantly with the appearance of a CH3 peak corresponding to that of free acetate and suggesting that folate is not acetylated during the reaction. (ox.ac.uk)
  • The evidence presented in this paper adds to our growing understanding of the endogenous roles of human arylamine N-acetyltransferase Type 1 and its mouse homologue and expands the catalytic repertoire of these enzymes, demonstrating that they are by no means just xenobiotic metabolising enzymes but probably also play an important role in cellular metabolism. (ox.ac.uk)
  • However, activated immune or cancer cells can also export citrate to the cytosol, where it is converted back to acetyl-coenzyme A (acetyl-CoA) by ATP citrate lyase. (frontiersin.org)
  • View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA , the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis . (uniprot.org)
  • Cyclohexa-1,5-diene-1-carbonyl-coenzyme A (CoA) hydratases of Geobacter metallireducens and Syntrophus aciditrophicus: Evidence for a common benzoyl-CoA degradation pathway in facultative and strict anaerobes. (genome.jp)
  • These data, together with the characterisation of a naphthoquinone inhibitor of folate-dependent acetyl Coenzyme A hydrolysis by human arylamine N-acetyltransferase Type 1/murine arylamine N-acetyltransferase Type 2, open up a range of future avenues of exploration, both for elucidating the developmental role of these enzymes and for improving chemotherapeutic approaches to pathological conditions including estrogen receptor-positive breast cancer. (ox.ac.uk)
  • Compared with other lysine acetyltransferases of known structure, alpha-tubulin acetyltransferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active site and putative alpha-tubulin binding site. (mpg.de)
  • Its key biosynthetic enzymes are lyso-PAF acetyltransferases (lyso-PAF-AT), responsible for PAF synthesis through the remodeling route and a specific CDP-choline:1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase (PAF-CPT), responsible for its de novo biosynthesis. (chemweb.com)
  • The de novo pathway utilizes 1-alkyl-2-acetyl- sn -glycerol and CDP-choline as substrates of a DTT-insensitive phosphocholine transferase (PAF-PCT). (springer.com)
  • Here, we describe experiments demonstrating that human arylamine N-acetyltransferase Type 1 and its murine homologue (Type 2) can also catalyse the direct hydrolysis of acetyl Coenzyme A in the presence of folate. (ox.ac.uk)
  • Furthermore, in silico docking of folate within the active site of human arylamine N-acetyltransferase Type 1 suggests that folate may bind at the enzyme's active site, and facilitate acetyl Coenzyme A hydrolysis. (ox.ac.uk)