Metabolic Networks and Pathways: Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.Molecular Sequence Annotation: The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.Gene Ontology: Sets of structured vocabularies used for describing and categorizing genes, and gene products by their molecular function, involvement in biological processes, and cellular location. These vocabularies and their associations to genes and gene products (Gene Ontology annotations) are generated and curated by the Gene Ontology Consortium.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.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.Transcriptome: The pattern of GENE EXPRESSION at the level of genetic transcription in a specific organism or under specific circumstances in specific cells.Software: Sequential operating programs and data which instruct the functioning of a digital computer.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.Genes, pol: DNA sequences that form the coding region for retroviral enzymes including reverse transcriptase, protease, and endonuclease/integrase. "pol" is short for polymerase, the enzyme class of reverse transcriptase.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.alpha-Linolenic Acid: A fatty acid that is found in plants and involved in the formation of prostaglandins.Plant Oils: Oils derived from plants or plant products.Fatty Liver: Lipid infiltration of the hepatic parenchymal cells resulting in a yellow-colored liver. The abnormal lipid accumulation is usually in the form of TRIGLYCERIDES, either as a single large droplet or multiple small droplets. Fatty liver is caused by an imbalance in the metabolism of FATTY ACIDS.DiglyceridesLiver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Diacylglycerol Kinase: An enzyme of the transferase class that uses ATP to catalyze the phosphorylation of diacylglycerol to a phosphatidate. EC 2.7.1.107.Vault Ribonucleoprotein Particles: Large cytoplasmic ribonucleoprotein particles that have an eight-fold symmetry with a central pore and petal-like structure giving the appearance of an octagonal dome. (The Dictionary of Cell Biology, Lackie and Dow, 2nd ed.)Diabetes Mellitus: A heterogeneous group of disorders characterized by HYPERGLYCEMIA and GLUCOSE INTOLERANCE.Diabetes Mellitus, Type 2: A subclass of DIABETES MELLITUS that is not INSULIN-responsive or dependent (NIDDM). It is characterized initially by INSULIN RESISTANCE and HYPERINSULINEMIA; and eventually by GLUCOSE INTOLERANCE; HYPERGLYCEMIA; and overt diabetes. Type II diabetes mellitus is no longer considered a disease exclusively found in adults. Patients seldom develop KETOSIS but often exhibit OBESITY.Enoyl-CoA Hydratase: An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Fatty Acids: Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.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.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)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.WingDrosophila melanogaster: A species of fruit fly much used in genetics because of the large size of its chromosomes.Odonata: An order of insects comprising three suborders: Anisoptera, Zygoptera, and Anisozygoptera. They consist of dragonflies and damselflies.Drosophila: A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.Drosophila Proteins: Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.Quantitative Trait Loci: Genetic loci associated with a QUANTITATIVE TRAIT.Genitalia, Male: The male reproductive organs. They are divided into the external organs (PENIS; SCROTUM;and URETHRA) and the internal organs (TESTIS; EPIDIDYMIS; VAS DEFERENS; SEMINAL VESICLES; EJACULATORY DUCTS; PROSTATE; and BULBOURETHRAL GLANDS).Genetic Variation: Genotypic differences observed among individuals in a population.Territoriality: Behavior in defense of an area against another individual or individuals primarily of the same species.Genes, Insect: The functional hereditary units of INSECTS.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.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).Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.Genomics: The systematic study of the complete DNA sequences (GENOME) of organisms.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.Acyltransferases: Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Barth Syndrome: Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.Tripterygium: A plant genus of the family CELASTRACEAE that is a source of triterpenoids and diterpene epoxides such as triptolide.Medication Adherence: Voluntary cooperation of the patient in taking drugs or medicine as prescribed. This includes timing, dosage, and frequency.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.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Aneugens: Agents which affect CELL DIVISION and the MITOTIC SPINDLE APPARATUS resulting in the loss or gain of whole CHROMOSOMES, thereby inducing an ANEUPLOIDY.Attentional Blink: Temporary visual deficit or impaired visual processing occurring in a rapid serial visual presentation task. After a person identifies the first of two visual targets, the ability to detect the second target is impaired for the next few hundred milliseconds. This phenomenon is called attentional blink.Williams Syndrome: A disorder caused by hemizygous microdeletion of about 28 genes on chromosome 7q11.23, including the ELASTIN gene. Clinical manifestations include SUPRAVALVULAR AORTIC STENOSIS; MENTAL RETARDATION; elfin facies; impaired visuospatial constructive abilities; and transient HYPERCALCEMIA in infancy. The condition affects both sexes, with onset at birth or in early infancy.Cholestasis, Intrahepatic: Impairment of bile flow due to injury to the HEPATOCYTES; BILE CANALICULI; or the intrahepatic bile ducts (BILE DUCTS, INTRAHEPATIC).MississippiDrugs, Chinese Herbal: Chinese herbal or plant extracts which are used as drugs to treat diseases or promote general well-being. The concept does not include synthesized compounds manufactured in China.Receptor-Interacting Protein Serine-Threonine Kinase 2: A RIP serine-theonine kinase that contains a C-terminal caspase activation and recruitment domain. It can signal by associating with other CARD-signaling adaptor proteins and INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.Retroelements: Elements that are transcribed into RNA, reverse-transcribed into DNA and then inserted into a new site in the genome. Long terminal repeats (LTRs) similar to those from retroviruses are contained in retrotransposons and retrovirus-like elements. Retroposons, such as LONG INTERSPERSED NUCLEOTIDE ELEMENTS and SHORT INTERSPERSED NUCLEOTIDE ELEMENTS do not contain LTRs.Nobel PrizeGenetic Drift: The fluctuation of the ALLELE FREQUENCY from one generation to the next.History, 19th Century: Time period from 1801 through 1900 of the common era.
(1/166) Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver.

The specific activities and substrate specificities of 3-oxoacyl-CoA thiolase A (thiolase A) purified from normal rat liver peroxisomes and 3-oxoacyl-CoA thiolase B (thiolase B) isolated from livers of rats treated with the peroxisome proliferator clofibrate were virtually identical. The enzymes could be distinguished by their N-terminal amino acid sequences, their isoelectric points and their stability, the latter being higher for thiolase A. Contrary to thiolase B, which showed a marked cold lability in the presence of KCl by dissociating into monomers with poor activity, thiolase A retained its full activity and its homodimeric structure under these conditions.  (+info)

(2/166) Expression and intracellular processing of the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts.

Although the sterol carrier protein 2 (SCP-2) gene encodes for two proteins, almost nothing is known of the function and potential processing of the larger transcript corresponding to the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase (SCP-x), in intact cells. L-cell fibroblasts transfected with cDNA encoding for the 58 kDa SCP-x protein had a 4.5-fold increase in SCP-x mRNA transcript levels. Western blot analysis showed SCP-x protein expression reached 0.011% of total protein, representing a 4.1-fold increase over basal levels. Surprisingly, the 13.2 kDa SCP-2 protein also increased 2-fold in the transfected cells. This was consistent with part of the 58 kDa SCP-x being proteolytically processed to 13.2 kDa SCP-2 as there was no evidence of an mRNA transcript corresponding to a 13.2/15.2 kDa gene product in the transfected L-cell clones. Confocal immunofluorescence microscopy of transfected L-cells showed that SCP-x/SCP-2 co-localized in highest concentration with catalase in peroxisomes, but significant amounts appeared extra-peroxisomal. Overexpression of SCP-x significantly altered cholesterol uptake and metabolism. Uptake of exogenous [3H]cholesterol and total cholesterol mass were increased 1.9- and 1.4-fold, respectively, in SCP-x expressors. Although cholesterol ester mass was unaltered, incorporation of exogenous [3H]cholesterol and [3H]oleic acid into cholesteryl esters increased 2.3- and 2.5-fold, respectively. These results from intact cells suggest the 13.2 kDa SCP-2 can arise from the larger SCP-2 gene product and indicate a role for the 58 kDa SCP-x protein in cholesterol uptake and intracellular cycling.  (+info)

(3/166) Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC.

The activities of beta-oxidation enzymes were measured in extracts of glucose- and triolein-grown cells of Aspergillus niger. Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity was detected. HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that beta-oxidation was limited to one cycle. Octanoyl-CoA accumulated as the decanoyl-CoA was oxidized. Beta-oxidation enzymes in isolated mitochondrial fractions were also studied. The results are discussed in the context of methyl ketone production by fungi.  (+info)

(4/166) Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain.

The fibroblast growth factor (FGF) family is composed of polypeptides with sequence identity which signal through transmembrane tyrosine kinase receptors. We report here the purification from bovine brain microsomes of an FGF-2-binding complex composed of three proteins of apparent molecular masses 150 kDa, 79 kDa and 46 kDa. Only the 150 kDa and 79 kDa proteins bound FGF-2 in cross-linking and ligand-blotting experiments. Binding of FGF-2 to p79 is enhanced in the presence of calcium. Peptide sequences allowed the identification of p150 and the cloning of the cDNAs encoding p79 and p46. The deduced amino acid sequence of p79 reveals high similarity to those of gastrin-binding protein and mitochondrial enoyl-CoA hydratase/hydroxyacyl-CoA dehydrogenase. p46 is similar to mitochondrial ketoacyl-CoA thiolase. Stable transfection of FR3T3 rat fibroblast cells with p79 cDNA analysed by electron microscopy following immunolabelling of ultra-thin cryosections revealed a localization of p79 in the secretory pathway, mainly in the endoplasmic reticulum and the Golgi region, where it is specifically associated with the molecular chaperone calnexin. In vivo a protein similar to the Golgi protein MG-160 forms a complex with FGF-2 and p79.  (+info)

(5/166) Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate.

We examined the expression and localization of type-II 3-oxoacyl-CoA thiolase in the nematode Caenorhabditis elegans. Type-II thiolase acts on 3-oxoacyl-CoA esters with a methyl group at the alpha carbon, whereas conventional thiolases do not. Mammalian type-II thiolase, which is also termed sterol carrier protein x (SCPx) or SCP2/3-oxoacyl-CoA thiolase, is located in the peroxisomes and involved in phytanic acid degradation and most probably in bile acid synthesis. The nematode enzyme lacks the SCP2 domain, which carries the peroxisomal-targeting signal, but produces bile acids in a cell-free system. Northern and Western blot analyses demonstrated that C. elegans expressed type-II thiolase throughout its life cycle, especially during the larval stages, and that the expression was significantly enhanced by the addition of clofibrate at 5 mM or more to the culture medium. Whole-mount in situ hybridization and immunostaining of L4 larvae revealed that the enzyme was mainly expressed in intestinal cells, which are multifunctional like many of the cell types in C. elegans. Subcellular fractionation and indirect immunoelectron microscopy of the nematode detected the enzyme in the matrix of peroxisomes. These results indicate the fundamental homology between mammalian SCPx and the nematode enzyme regardless of whether the SCP2 part is fused, suggesting their common physiological roles.  (+info)

(6/166) Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. Strain HR199.

The gene loci fcs, encoding feruloyl coenzyme A (feruloyl-CoA) synthetase, ech, encoding enoyl-CoA hydratase/aldolase, and aat, encoding beta-ketothiolase, which are involved in the catabolism of ferulic acid and eugenol in Pseudomonas sp. strain HR199 (DSM7063), were localized on a DNA region covered by two EcoRI fragments (E230 and E94), which were recently cloned from a Pseudomonas sp. strain HR199 genomic library in the cosmid pVK100. The nucleotide sequences of parts of fragments E230 and E94 were determined, revealing the arrangement of the aforementioned genes. To confirm the function of the structural genes fcs and ech, they were cloned and expressed in Escherichia coli. Recombinant strains harboring both genes were able to transform ferulic acid to vanillin. The feruloyl-CoA synthetase and enoyl-CoA hydratase/aldolase activities of the fcs and ech gene products, respectively, were confirmed by photometric assays and by high-pressure liquid chromatography analysis. To prove the essential involvement of the fcs, ech, and aat genes in the catabolism of ferulic acid and eugenol in Pseudomonas sp. strain HR199, these genes were inactivated separately by the insertion of omega elements. The corresponding mutants Pseudomonas sp. strain HRfcsOmegaGm and Pseudomonas sp. strain HRechOmegaKm were not able to grow on ferulic acid or on eugenol, whereas the mutant Pseudomonas sp. strain HRaatOmegaKm exhibited a ferulic acid- and eugenol-positive phenotype like the wild type. In conclusion, the degradation pathway of eugenol via ferulic acid and the necessity of the activation of ferulic acid to the corresponding CoA ester was confirmed. The aat gene product was shown not to be involved in this catabolism, thus excluding a beta-oxidation analogous degradation pathway for ferulic acid. Moreover, the function of the ech gene product as an enoyl-CoA hydratase/aldolase suggests that ferulic acid degradation in Pseudomonas sp. strain HR199 proceeds via a similar pathway to that recently described for Pseudomonas fluorescens AN103.  (+info)

(7/166) Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway.

Organelle biogenesis and turnover are necessary to maintain biochemical processes that are appropriate to the needs of the eukaryotic cell. Specific degradation of organelles in response to changing environmental cues is one aspect of achieving proper metabolic function. For example, the yeast Saccharomyces cerevisiae adjusts the level of peroxisomes in response to differing nutritional sources. When cells are grown on oleic acid as the sole carbon source, peroxisome biogenesis is induced. Conversely, a subsequent shift to glucose-rich or nitrogen-limiting conditions results in peroxisome degradation. The degradation process, pexophagy, requires the activity of vacuolar hydrolases. In addition, peroxisome degradation is specific. Analyses of cellular marker proteins indicate that peroxisome degradation under these conditions occurs more rapidly and to a greater extent than mitochondrial, Golgi, or cytosolic protein delivery to the vacuole by the non-selective autophagy pathway. To elucidate the molecular mechanism of selective peroxisome degradation, we examined pexophagy in mutants that are defective in autophagy (apg) and the selective targeting of aminopeptidase I to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway. Inhibition of peroxisome degradation in cvt and apg mutants indicates that these pathways overlap and that peroxisomes are delivered to the vacuole by a mechanism that utilizes protein components of the Cvt/autophagy pathways.  (+info)

(8/166) Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of beta oxidation of the intermediate benzylsuccinate.

The pathway of anaerobic toluene oxidation to benzoyl coenzyme A (benzoyl-CoA) consists of an initial reaction catalyzed by benzylsuccinate synthase, a glycyl radical enzyme adding the methyl group of toluene to the double bond of a fumarate cosubstrate, and a subsequent beta-oxidation pathway of benzylsuccinate. Benzylsuccinate synthase has been studied in some detail, whereas the enzymes participating in beta oxidation of benzylsuccinate are unknown. We have investigated these enzymes by analyzing substrate-induced proteins in toluene-grown cells. Toluene-induced proteins were identified and N-terminally sequenced. Nine of these proteins are encoded by an 8.5-kb operon consisting of bbs (beta-oxidation of benzylsuccinate) genes whose products are apparently involved in the beta-oxidation pathway of benzylsuccinate. Two of the genes, bbsE and bbsF, code for the subunits of a succinyl-CoA:benzylsuccinate CoA-transferase whose activity was previously detected in toluene-grown Thauera aromatica. The bbsG gene codes for a specific benzylsuccinyl-CoA dehydrogenase, as confirmed by overexpression of the gene in Escherichia coli and detection of enzyme activity. The further enzymes of the pathway are probably encoded by bbsH (enoyl-CoA hydratase), bbsCD (3-hydroxyacyl-CoA dehydrogenase), and bbsB (3-oxoacyl-CoA thiolase). The operon contains two additional genes, bbsA and bbsI, for which no obvious function could be derived. The bbs operon is expressed only in toluene-grown cells and is regulated at the transcriptional level. Promoter mapping revealed a transcription start site upstream of the bbsA gene. This represents the first known promoter site in Thauera spp.  (+info)

*  ACAA1
Acetyl-Coenzyme A acyltransferase 1 is an acetyl-CoA C-acyltransferase enzyme. This gene encodes an enzyme operative in the ... 3-Ketoacyl-CoA thiolase, peroxisomal also known as acetyl-Coenzyme A acyltransferase 1 is an enzyme that in humans is encoded ... acetyl-Coenzyme A acyltransferase 1". Bout A, Hoovers JM, Bakker E, Mannens MM, Geurts van Kessel A, Westerveld A, Tager JM, ... 1995). "Refined localization of human peroxisomal 3-oxoacyl-CoA thiolase (ACAA) to 3p22". Hum. Hered. 45 (2): 75-9. doi:10.1159 ...
*  ACAA2
Acetyl-Coenzyme A acyltransferase 2 is an acetyl-CoA C-acyltransferase enzyme. The ACAA2 gene encodes a 41.9 kDa protein that ... 3-Ketoacyl-CoA thiolase, mitochondrial also known as acetyl-Coenzyme A acyltransferase 2 is an enzyme that in humans is encoded ... Cao W, Liu N, Tang S, Bao L, Shen L, Yuan H, Zhao X, Lu H (Jun 2008). "Acetyl-Coenzyme A acyltransferase 2 attenuates the ... acetyl-Coenzyme A acyltransferase 2". Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, ...
*  Pseudotropine acyltransferase
... acyl-CoA transferase, tigloyl-CoA:pseudotropine acyltransferase, acetyl-CoA:pseudotropine acyltransferase, pseudotropine ... and 3β-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases". FEBS ... This enzyme catalyses the following chemical reaction acyl-CoA + pseudotropine ⇌ {\displaystyle \rightleftharpoons } CoA + O- ... "Tigloyl-CoA:pseudotropine acyltransferase - an enzyme of tropane alkaloid biosynthesis". Phytochemistry. 39: 315-322. doi: ...
*  Tropine acyltransferase
... (EC 2.3.1.185, tropine:acyl-CoA transferase, acetyl-CoA:tropan-3-ol acyltransferase, tropine ... and 3β-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases". FEBS ... This enzyme catalyses the following chemical reaction acyl-CoA + tropine ⇌ {\displaystyle \rightleftharpoons } CoA + O- ... Tropine acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...
*  Liang Tong
His lab focuses on enzymes involved in fatty acid metabolism, including Acetyl-CoA carboxylase, carnitine acyltransferase, AMP- ...
*  Beta-ketoacyl-(acyl-carrier-protein) synthase III
The systematic name of this enzyme class is acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase. Other names in common ... CoA + CO2 Thus, the two substrates of this enzyme are acetyl-CoA and malonyl-[acyl-carrier-protein], whereas its 3 products are ... CoA, malonyl CoA, degraded CoA). Specific inhibitors developed using rational design have recently been reported. In 2005, the ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + malonyl-[acyl carrier protein] ⇌ {\displaystyle \ ...
*  ACAT1 mRNA
Human acetyl-coA cholesterol acyltransferase (ACAT1) gene produces a chimeric mRNA through the interchromosomal processing of ... Cholesterol Acyltransferase 1 (acat1) Sequences Located in Two Different Chromosomes (7 and 1) Are Required to Produce a Novel ...
*  SCP2
... and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx". DNA Cell Biol. 10 (9): 695-8. doi:10.1089 ... Non-specific lipid-transfer protein also known as sterol carrier protein 2 (SCP-2) or propanoyl-CoA C-acyltransferase is a ...
*  HADHB
Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ... which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. The encoded protein can also bind ... Middleton B (1994). "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase ... The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another ...
*  acyl-carrier-protein) S-acetyltransferase
"Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the ... CoA + acetyl-[acyl-carrier-protein] Thus, the two substrates of this enzyme are acetyl-CoA and acyl carrier protein, whereas ... Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, Acetyl CoA:ACP transacylase, [acyl- ... The systematic name of this enzyme class is acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. ...
*  BAHD acyltransferase
Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J 14: 297- ... The BAHD acyltransferases are a super family of enzymes found primarily in plants, algae and bacteria. They are CoA-dependent ... a benzoyl/hydroxycinnamoyl-CoA acyltransferase identified in Gentiana triflora and is believed to be involved in the synthesis ... also a benzoyl/hydroxycinnamoyl-CoA acyltransferase identified in carnation (Dianthus caryophyllus). It is thought to be ...
*  Acetyl-CoA C-acetyltransferase
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... 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 ...
*  Acetyl-CoA C-myristoyltransferase
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... CoA Thus, the two substrates of this enzyme are myristoyl-CoA and acetyl-CoA, whereas its two products are 3-oxopalmitoyl-CoA ... an acetyl-CoA C-myristoyltransferase (EC 2.3.1.155) is an enzyme that catalyzes the chemical reaction myristoyl-CoA + acetyl- ... The systematic name of this enzyme class is myristoyl-CoA:acetyl-CoA C-myristoyltransferase. Miyazawa S, Furuta S, Osumi T, ...
*  List of EC numbers (EC 2)
... anthocyanin 5-aromatic acyltransferase EC 2.3.1.154: propionyl-CoA C2-trimethyltridecanoyltransferase EC 2.3.1.155: acetyl-CoA ... glycerol-3-phosphate O-acyltransferase EC 2.3.1.16: acetyl-CoA C-acyltransferase EC 2.3.1.17: aspartate N-acetyltransferase EC ... succinyl-CoA:(R)-benzylsuccinate CoA-transferase EC 2.8.3.16: formyl-CoA transferase EC 2.8.3.17: cinnamoyl-CoA:phenyllactate ... acetyl-CoA-benzylalcohol acetyltransferase EC 2.3.1.225: protein S-acyltransferase EC 2.3.1.226: carboxymethylproline synthase ...
*  End-plate potential
Acetylcholine is synthesized in the cytoplasm of the neuron from choline and acetyl-CoA. Choline acyltransferase is the enzyme ...
*  List of MeSH codes (D08)
... acetyl-CoA C-acyltransferase MeSH D08.811.913.050.134 --- acetyltransferases MeSH D08.811.913.050.134.029 --- acyl-carrier ... acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 --- palmitoyl-coa hydrolase MeSH D08.811.277.352.897.850 --- ubiquitin ... 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 ...
*  Phosphate acetyltransferase
CoA + acetyl phosphate The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... 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 ...
*  Thiolase
... and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx". DNA Cell Biol. 10 (9): 695-8. doi:10.1089 ... preferentially catalyze the degradation of 3-ketoacyl-CoA to form acetyl-CoA and a shortened acyl-CoA species, but are also ... In the second step, the addition of CoA (in the degradative reaction) or acetyl-CoA (in the biosynthetic reaction) to the acyl- ... Thiolases, also known as acetyl-coenzyme A acetyltransferases (ACAT), are enzymes which convert two units of acetyl-CoA to ...
*  Monoterpenol O-acetyltransferase
CoA + a monoterpenol acetate ester Thus, the two substrates of this enzyme are acetyl-CoA and monoterpenol, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... 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 ...
*  Arylamine N-acetyltransferase
CoA + an N-acetylarylamine Thus, the two substrates of this enzyme are acetyl-CoA and arylamine, whereas its two products are ... CoA and N-acetylarylamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... 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 ...
*  Peptide alpha-N-acetyltransferase
CoA Thus, the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nalpha-acetylpeptide and ... CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than ... 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 ...
*  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, ... specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class ... 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 ...
*  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 ... and O-acetyl-L-serine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the ... The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, ...
*  D-tryptophan N-acetyltransferase
N-acetyl-D-tryptophan Thus, the two substrates of this enzyme are acetyl-CoA and D-tryptophan, whereas its two products are CoA ... and N-acetyl-D-tryptophan. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + D-tryptophan ⇌ {\displaystyle \rightleftharpoons } CoA + ... The systematic name of this enzyme class is acetyl-CoA:D-tryptophan N-acetyltransferase. Other names in common use include D- ...
*  Phenylalanine N-acetyltransferase
CoA + N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl- ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ...
*  HGSNAT
... "acetyl-CoA:heparan-α-D-glucosaminide N-acetyltransferase" and "acetyl-CoA:alpha-glucosaminide N-acetyltransferase") is an ... In enzymology, this enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other ... acetyl-CoA + heparan sulfate α-D-glucosaminide ⇌ {\displaystyle \rightleftharpoons } CoA + heparan sulfate N-acetyl-α-D- ... Klein U, Kresse H, von Figura K (1978). "Sanfilippo syndrome type C: deficiency of acetyl-CoA:alpha-glucosaminide N- ...
The genome of the basal agaricomycete Xanthophyllomyces dendrorhous provides insights into the organization of its acetyl-CoA...  The genome of the basal agaricomycete Xanthophyllomyces dendrorhous provides insights into the organization of its acetyl-CoA...
Further InterPro domain analyses of the PKS-like gene predicted a beta-ketoacyl synthase (KS) domain, an acyl transferase (AT) ... CoA-related pathways. The two major acetyl-Co A derived biosynthesis pathways in X. dendrorhous are terpenoid and fatty acid ... Another important group of compounds originating from acetyl-CoA are the fatty acids. In the X. dendrorhous genome, the genes ... The synthesis starts with the acetyl CoA carboxylase and the acyl carrier protein (Table 3). The following reactions, the ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/s12864-015-1380-0
ACAA2 Gene - GeneCards | THIM Protein | THIM Antibody  ACAA2 Gene - GeneCards | THIM Protein | THIM Antibody
Acetyl-CoA Acyltransferase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... acetyl-CoA acyltransferase 2,mitochondrial-3-oxoacyl-coenzyme A,thiolase,concluding the step of fatty acid beta oxidation * ... Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. *THIM_HUMAN,P42765. UniProtKB/Swiss-Prot Function: Abolishes BNIP3-mediated ... ACAA2 (Acetyl-CoA Acyltransferase 2) is a Protein Coding gene. Diseases associated with ACAA2 include Ketothiolase Deficiency. ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?gene=ACAA2
Nucleic Acid-Based Theranostics for Tackling Alzheimers Disease  Nucleic Acid-Based Theranostics for Tackling Alzheimer's Disease
Acetyl-CoA acyl transferase. Acetyl-CoA acyl transferase has a role in lipid metabolism that has been implicated in the ... Murphy et al. [139] inhibited Acetyl-CoA acyl transferase using an artificial miRNA to reduce Aβ plaque burden and improve ... Antisense inhibition at the β-secretase-site of β-amyloid precursor protein reduces cerebral amyloid and acetyl cholinesterase ...
more infohttp://www.thno.org/v07p3933.htm
fadI - 3-ketoacyl-CoA thiolase - Shewanella baltica (strain OS185) - fadI gene & protein  fadI - 3-ketoacyl-CoA thiolase - Shewanella baltica (strain OS185) - fadI gene & protein
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ... Acetyl-CoA acyltransferaseUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ... Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.UniRule annotation. ,p>Manual validated information which has been generated by the ... Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ...
more infohttps://www.uniprot.org/uniprot/A6WQ26
fadI - 3-ketoacyl-CoA thiolase - Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) - fadI gene & protein  fadI - 3-ketoacyl-CoA thiolase - Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) - fadI gene & protein
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ... Acetyl-CoA acyltransferaseUniRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ... Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.UniRule annotation. ,p>Manual validated information which has been generated by the ... Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ...
more infohttps://www.uniprot.org/uniprot/A6TC20
CPT1a-Dependent Long-Chain Fatty Acid Oxidation Contributes to Maintaining Glucagon Secretion from Pancreatic Islets.  CPT1a-Dependent Long-Chain Fatty Acid Oxidation Contributes to Maintaining Glucagon Secretion from Pancreatic Islets.
Acetyl-coa C-acyltransferase. Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and ... 3-hydroxyacyl Coa Dehydrogenases. Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in ... Acyl-coa Dehydrogenase, Long-chain. A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a ... the CoA ester of a fatty acid two carbons shorter is formed. ...
more infohttps://www.bioportfolio.com/resources/pmarticle/2069128/CPT1a-Dependent-Long-Chain-Fatty-Acid-Oxidation-Contributes-to-Maintaining-Glucagon-Secretion.html
SWISSPROT: Q2IN02 ANADE  SWISSPROT: Q2IN02 ANADE
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006631; P:fatty acid metabolic process ... DR CDD; cd00751; thiolase; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI. DR InterPro; ... KW Acyltransferase {ECO:0000256,RuleBase:RU003557, KW ECO:0000313,EMBL:ABC80183.1}; KW Complete proteome {ECO:0000313,Proteomes ... DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313,EMBL:ABC80183.1}; DE EC=2.3.1.16 {ECO:0000313,EMBL:ABC80183.1}; GN ...
more infohttp://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-ac?query=ABC80183&db=SWISSPROT&ident=ACNUC7421
KEGG BRITE: KEGG Orthology (KO) - Sphingobium sp. SYK-6  KEGG BRITE: KEGG Orthology (KO) - Sphingobium sp. SYK-6
24630 acetyl-CoA acetyltransferase SLG_21370 acetyl-CoA acyltransferase SLG_24730 acetyl-CoA acetyltransferase SLG_31440 acetyl ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K11103 dctA; aerobic ... citryl-CoA lyase [EC:4.1.3.34] K01644 citE; citrate lyase subunit beta / citryl-CoA lyase [EC:4.1.3.34] K00990 glnD; [protein- ...
more infohttp://www.genome.jp/kegg-bin/get_htext?ssy00001+SLG_28000
KEGG PATHWAY: pol00630  KEGG PATHWAY: pol00630
Acetyl-CoA C-acyltransferase [KO:K00626] [EC:2.3.1.9]. Bpro_4187 Acetyl-CoA C-acetyltransferase [KO:K00626] [EC:2.3.1.9] ... Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases. ...
more infohttp://www.genome.jp/dbget-bin/www_bget?pathway+pol00630
Transcriptomic effects of di-(2-ethylhexyl)-phthalate in Syrian hamster embryo cells: an important role of early cytoskeleton...  Transcriptomic effects of di-(2-ethylhexyl)-phthalate in Syrian hamster embryo cells: an important role of early cytoskeleton...
On the other hand, three genes (Actin β, Lipoprotein lipase, and Acetyl-Coenzyme A acyltransferase 1a) and 5 gene isoforms ( ... Bell DR, Elcombe CR: Induction of Acyl-Coa oxidase and Cytochrome-P450iva1 Rna in rat primary hepatocyte culture by peroxisome ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-12-524
Supplementation with alpha-linolenic acid-rich diacylglycerol suppresses fatty liver formation accompanied by an up-regulation...  Supplementation with alpha-linolenic acid-rich diacylglycerol suppresses fatty liver formation accompanied by an up-regulation...
EC 1.1.1.35/3-Hydroxyacyl CoA Dehydrogenases; EC 2.3.1.16/Acetyl-CoA C-Acyltransferase; EC 4.2.1.17/Enoyl-CoA Hydratase; EC 5.1 ... 3-Hydroxyacyl CoA Dehydrogenases / antagonists & inhibitors. Acetyl-CoA C-Acyltransferase / antagonists & inhibitors. Animals. ... and acyl-CoA oxidase (ACO) and medium-chain acyl-CoA dehydrogenase (MCAD) mRNA levels. By contrast, no significant changes were ... Enoyl-CoA Hydratase / antagonists & inhibitors. Fatty Liver / blood, metabolism, prevention & control*. Liver / drug effects, ...
more infohttp://www.biomedsearch.com/nih/Supplementation-with-alpha-linolenic-acid/15863369.html
ACAA2 - PCR Primer Pair - Probe | PrimePCR | Bio-Rad  ACAA2 - PCR Primer Pair - Probe | PrimePCR | Bio-Rad
Acetyl-CoA acyltransferase 2. Aliases:. Not Available. RefSeq:. Not Available. Ensembl:. ENSCAFG00000019019 ...
more infohttp://www.bio-rad.com/en-us/prime-pcr-assays/assay/qcfacip0001299-primepcr-probe-assay-acaa2-dog
CAIRO LIVER DEVELOPMENT DN  CAIRO LIVER DEVELOPMENT DN
acetyl-CoA acyltransferase 2. 1428326_s_at. 10247. HRSP12. heat-responsive protein 12. ...
more infohttp://software.broadinstitute.org/gsea/msigdb/cards/CAIRO_LIVER_DEVELOPMENT_DN.html
Fatty acid oxidation complex, alpha subunit, mitochondrial (IPR012803) | InterPro | EMBL-EBI  Fatty acid oxidation complex, alpha subunit, mitochondrial (IPR012803) | InterPro | EMBL-EBI
The beta subunit has acetyl-CoA C-acyltransferase (EC:2.3.1.16) activity. ... Subunit activities include: enoyl-CoA hydratase (EC:4.2.1.17) and 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35). Some ... GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity GO:0004300 enoyl-CoA hydratase activity ... Enoyl-CoA hydratase/isomerase (IPR001753) *Fatty acid oxidation complex, alpha subunit, mitochondrial (IPR012803) ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR012803
Abetalipoproteinemia disease: Malacards - Research Articles, Drugs, Genes, Clinical Trials  Abetalipoproteinemia disease: Malacards - Research Articles, Drugs, Genes, Clinical Trials
phosphatidylcholine-sterol O-acyltransferase activator activity. GO:0060228 9.48. APOA1 APOE 12. acetyl-CoA C-acyltransferase ... enoyl-CoA hydratase activity. GO:0004300 9.52. HADHA HADHB 9. 3-hydroxyacyl-CoA dehydrogenase activity. GO:0003857 9.51. HADHA ... Hydroxyacyl-CoA Dehydrogenase Trifunctional Multienzyme Complex Subunit Alpha. Protein Coding. 20.33. Novoseek inferred 51 ... Hydroxyacyl-CoA Dehydrogenase Trifunctional Multienzyme Complex Subunit Beta. Protein Coding. 19.16. Novoseek inferred 51 ...
more infohttp://www.malacards.org/card/abetalipoproteinemia
anti-Acetyl-CoA Acyltransferase 2 (ACAA2) Antikörper</span>  anti-Acetyl-CoA Acyltransferase 2 (ACAA2) Antikörper</span>
... mitochondrial acetyl-Coenzyme A acyltransferase 2 , acetyl-coenzyme A acyltransferase 2 , acetyl-CoA acyltransferase ... anti-Acetyl-CoA Acyltransferase 2 Antikörper (ACAA2). Auf www.antikoerper-online.de finden Sie aktuell 58 Acetyl-CoA ... acetyl-CoA acyltransferase 2 (acaa2) Antikörper * acetyl-Coenzyme A acyltransferase 2 (mitochondrial 3-oxoacyl-Coenzyme A ... Human Acetyl-CoA Acyltransferase 2 (ACAA2) Interaktionspartner * ACAA2 is a functional BNIP3 (zeige BNIP3 Antikörper) binding ...
more infohttp://www.antikoerper-online.de/monocarboxylic-acid-catabolic-process-pathway-92/acaa2-antibody-6895/
Recombinant Human ACAA2 293 Cell Lysate ACAA2-9118HCL - Creative BioMart  Recombinant Human ACAA2 293 Cell Lysate ACAA2-9118HCL - Creative BioMart
ACAA2; acetyl-CoA acyltransferase 2; acetyl Coenzyme A acyltransferase 2; 3-ketoacyl-CoA thiolase, mitochondrial; DSAEC; ... acetyl-CoA C-acyltransferase activity; protein binding; transferase activity, transferring acyl groups other than amino-acyl ... acetyl-Coenzyme A acyltransferase 2; mitochondrial 3-oxoacyl-CoA thiolase; mitochondrial 3-oxoacyl-Coenzyme A thiolase; ... Antigen standard for acetyl-Coenzyme A acyltransferase 2 (ACAA2), nuclear gene encoding mitochondrial protein is a lysate ...
more infohttps://www.creativebiomart.net/description_410762_318.htm
Many P-Element Insertions Affect Wing Shape in Drosophila melanogaster | Genetics  Many P-Element Insertions Affect Wing Shape in Drosophila melanogaster | Genetics
yip2 codes for an acetyl-CoA C-acyltransferase, which is found in the mitochondrion. Srp54 codes for a protein that includes an ...
more infohttp://www.genetics.org/content/169/3/1461