Acyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Glucosephosphate Dehydrogenase Deficiency: A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.Lipid Metabolism, Inborn Errors: Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.Genes, Recessive: Genes that influence the PHENOTYPE only in the homozygous state.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Pedigree: The record of descent or ancestry, particularly of a particular condition or trait, indicating individual family members, their relationships, and their status with respect to the trait or condition.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.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Palmitoyl-CoA Hydrolase: Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.Thiolester HydrolasesAcyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.Thermogenesis: The generation of heat in order to maintain body temperature. The uncoupled oxidation of fatty acids contained within brown adipose tissue and SHIVERING are examples of thermogenesis in MAMMALS.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)Coenzyme ACoenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Acetyl-CoA Hydrolase: An enzyme that catalyzes reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids. EC 3.1.2.1.Fatty Acids, Nonesterified: FATTY ACIDS found in the plasma that are complexed with SERUM ALBUMIN for transport. These fatty acids are not in glycerol ester form.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.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.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Software: Sequential operating programs and data which instruct the functioning of a digital computer.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.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.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.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Patient Advocacy: Promotion and protection of the rights of patients, frequently through a legal process.ArchivesNuclear Magnetic Resonance, Biomolecular: NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Nitrogen Isotopes: Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.Bacteriophage Pf1: A species of filamentous Pseudomonas phage in the genus INOVIRUS, family INOVIRIDAE.Liquid Crystals: Materials in intermediate state between solid and liquid.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Dictionaries, MedicalSterol O-Acyltransferase: An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.Phosphatidylcholine-Sterol O-Acyltransferase: An enzyme secreted from the liver into the plasma of many mammalian species. It catalyzes the esterification of the hydroxyl group of lipoprotein cholesterol by the transfer of a fatty acid from the C-2 position of lecithin. In familial lecithin:cholesterol acyltransferase deficiency disease, the absence of the enzyme results in an excess of unesterified cholesterol in plasma. EC 2.3.1.43.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.Lecithin Acyltransferase Deficiency: An autosomal recessively inherited disorder caused by mutation of LECITHIN CHOLESTEROL ACYLTRANSFERASE that facilitates the esterification of lipoprotein cholesterol and subsequent removal from peripheral tissues to the liver. This defect results in low HDL-cholesterol level in blood and accumulation of free cholesterol in tissue leading to a triad of CORNEAL OPACITY, hemolytic anemia (ANEMIA, HEMOLYTIC), and PROTEINURIA.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.Cholesterol Esters: Fatty acid esters of cholesterol which constitute about two-thirds of the cholesterol in the plasma. The accumulation of cholesterol esters in the arterial intima is a characteristic feature of atherosclerosis.Dictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Diacylglycerol O-Acyltransferase: An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.Bile Acids and Salts: Steroid acids and salts. The primary bile acids are derived from cholesterol in the liver and usually conjugated with glycine or taurine. The secondary bile acids are further modified by bacteria in the intestine. They play an important role in the digestion and absorption of fat. They have also been used pharmacologically, especially in the treatment of gallstones.Sphingosine N-Acyltransferase: An enzyme that catalyzes the acyltransferase of SPHINGOSINE to N-acylsphingosine using acyl-COENZYME A as donor and COENZYME A as acceptor. The enzyme is mainly localized in the MITOCHONDRIA.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Glycocholic Acid: The glycine conjugate of CHOLIC ACID. It acts as a detergent to solubilize fats for absorption and is itself absorbed.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).Penicillium chrysogenum: A mitosporic fungal species used in the production of penicillin.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.Ketocholesterols: Cholesterol substituted in any position by a keto moiety. The 7-keto isomer inhibits 3-hydroxy-3-methylglutaryl-CoA reductase activity and inhibits cholesterol uptake in the coronary arteries and aorta in vitro.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).Cholesterol Oxidase: An enzyme that catalyzes the oxidation of cholesterol in the presence of molecular oxygen to 4-cholesten-3-one and hydrogen peroxide. The enzyme is not specific for cholesterol, but will also oxidize other 3-hydroxysteroids. EC 1.1.3.6.Kainic Acid: (2S-(2 alpha,3 beta,4 beta))-2-Carboxy-4-(1-methylethenyl)-3-pyrrolidineacetic acid. Ascaricide obtained from the red alga Digenea simplex. It is a potent excitatory amino acid agonist at some types of excitatory amino acid receptors and has been used to discriminate among receptor types. Like many excitatory amino acid agonists it can cause neurotoxicity and has been used experimentally for that purpose.Hydroxycholesterols: Cholesterol which is substituted by a hydroxy group in any position.Hippocampus: A curved elevation of GRAY MATTER extending the entire length of the floor of the TEMPORAL HORN of the LATERAL VENTRICLE (see also TEMPORAL LOBE). The hippocampus proper, subiculum, and DENTATE GYRUS constitute the hippocampal formation. Sometimes authors include the ENTORHINAL CORTEX in the hippocampal formation.Holothuria: A genus of large SEA CUCUMBERS in the family Holothuriidae possessing thick body walls, a warty body surface, and microscopic ossicles.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
(1/1356) Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis.

In nonribosomal biosynthesis of peptide antibiotics by multimodular synthetases, amino acid monomers are activated by the adenylation domains of the synthetase and loaded onto the adjacent carrier protein domains as thioesters, then the formation of peptide bonds and translocation of the growing chain are effected by the synthetase's condensation domains. Whether the condensation domains have any editing function has been unknown. Synthesis of aminoacyl-coenzyme A (CoA) molecules and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the adenylation domain editing function to be bypassed. This method was used to demonstrate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor residue (D-phenylalanine) and higher selectivity at the acceptor residue (L-proline) in the formation of the chain-initiating D-Phe-L-Pro dipeptidyl-enzyme intermediate.  (+info)

(2/1356) 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)

(3/1356) Inositol acylation of glycosylphosphatidylinositols in the pathogenic fungus Cryptococcus neoformans and the model yeast Saccharomyces cerevisiae.

Cryptococcus neoformans, an opportunistic fungus responsible for life-threatening infection in immunocompromised patients, is able to synthesize glycosylphosphatidylinositol (GPI) structures. Radiolabelling experiments in vitro with the use of a cryptococcal cell-free system showed that the pathway begins as in other eukaryotes, with the addition of N-acetylglucosamine to phosphatidylinositol, followed by deacetylation of the sugar residue. The third step, acylation of the inositol ring, seemed to involve a fatty acid other than palmitate, in contrast with previous findings in Saccharomyces cerevisiae and mammalian GPI pathways. A systematic study of inositol acylation in C. neoformans and S. cerevisiae showed that both organisms used a variety of fatty acids in this step; these were transferred directly from acyl-CoA to inositol without modification. However, the specificity of fatty acid utilization was quite distinct in the two fungi, with the pathogen being substantially more restrictive. In mammalian cells fatty acids added exogenously as acyl-CoAs are not transferred directly to inositol. These results suggest significant differences in the GPI biosynthetic pathway between mammalian and C. neoformans cells that could represent targets for anti-cryptococcal therapy.  (+info)

(4/1356) Delta3,5,7,Delta2,4,6-trienoyl-CoA isomerase, a novel enzyme that functions in the beta-oxidation of polyunsaturated fatty acids with conjugated double bonds.

The mitochondrial metabolism of unsaturated fatty acids with conjugated double bonds at odd-numbered positions, e.g. 9-cis, 11-trans-octadecadienoic acid, was investigated. These fatty acids are substrates of beta-oxidation in isolated rat liver mitochondria and hence are expected to yield 5,7-dienoyl-CoA intermediates. 5, 7-Decadienoyl-CoA was used to study the degradation of these intermediates. After introduction of a 2-trans-double bond by acyl-CoA dehydrogenase or acyl-CoA oxidase, the resultant 2,5, 7-decatrienoyl-CoA can either continue its pass through the beta-oxidation cycle or be converted by Delta3,Delta2-enoyl-CoA isomerase to 3,5,7-decatrienoyl-CoA. The latter compound was isomerized by a novel enzyme, named Delta3,5,7,Delta2,4, 6-trienoyl-CoA isomerase, to 2,4,6-decatrienoyl-CoA, which is a substrate of 2,4-dienoyl-CoA reductase (Wang, H.-Y. and Schulz, H. (1989) Biochem. J. 264, 47-52) and hence can be completely degraded via beta-oxidation. Delta3,5,7,Delta2,4,6-Trienoyl-CoA isomerase was purified from pig heart to apparent homogeneity and found to be a component enzyme of Delta3,5,Delta2,4-dienoyl-CoA isomerase. Although the direct beta-oxidation of 2,5,7-decatrienoyl-CoA seems to be the major pathway, the degradation via 2,4,6-trienoyl-CoA makes a significant contribution to the total beta-oxidation of this intermediate.  (+info)

(5/1356) Carbon-13 nuclear magnetic resonance study of metabolism of propionate by Escherichia coli.

We have evaluated the use of [1,2-13C2]propionate for the analysis of propionic acid metabolism, based on the ability to distinguish between the methylcitrate and methylmalonate pathways. Studies using propionate-adapted Escherichia coli MG1655 cells were performed. Preservation of the 13C-13C-12C carbon skeleton in labeled alanine and alanine-containing peptides involved in cell wall recycling is indicative of the direct formation of pyruvate from propionate via the methylcitrate cycle, the enzymes of which have recently been demonstrated in E. coli. Additionally, formation of 13C-labeled formate from pyruvate by the action of pyruvate-formate lyase is also consistent with the labeling of pyruvate C-1. Carboxylation of the labeled pyruvate leads to formation of [1,2-13C2]oxaloacetate and to multiply labeled glutamate and succinate isotopomers, also consistent with the flux through the methylcitrate pathway, followed by the tricarboxylic acid (TCA) cycle. Additional labeling of TCA intermediates arises due to the formation of [1-13C]acetyl coenzyme A from the labeled pyruvate, formed via pyruvate-formate lyase. Labeling patterns in trehalose and glycine are also interpreted in terms of the above pathways. The information derived from the [1, 2-13C2]propionate label is contrasted with information which can be derived from singly or triply labeled propionate and shown to be more useful for distinguishing the different propionate utilization pathways via nuclear magnetic resonance analysis.  (+info)

(6/1356) Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35.

A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia coli to yield an active enzyme. The purified enzyme had a pH optimum of approximately 8.0, Km values of 0.49 mM for pimelic acid, 0.18 mM for CoA and 0.72 mM for ATP, a subunit Mr of approximately 80000 as determined by SDS/PAGE, and was found to be a tetramer by gel-filtration chromatography. The specific activity of the purified enzyme was 77.3 units/mg of protein. The enzyme was not absolutely specific for pimelic acid. The relative activity for adipic acid (C6) was 72% and for azaleic acid (C9) was 18% of that for pimelic acid (C7). The N-terminal amino acid was blocked to amino acid sequencing, but controlled proteolysis resulted in three peptide fragments for which amino acid sequences were obtained. An oligonucleotide gene probe corresponding to one of the amino acid sequences was synthesized and used to isolate the gene (pauA, pimelic acid-utilizing A) coding for pimeloyl-CoA synthetase. The pauA gene, which codes for a protein with a theoretical Mr of 74643, was then sequenced. The deduced amino acid sequence of the enzyme showed similarity to hypothetical proteins from Archaeoglobus fulgidus, Methanococcus jannaschii, Pyrococcus horikoshii, E. coli and Streptomyces coelicolor, and some limited similarity to microbial succinyl-CoA synthetases. The similarity with the protein from A. fulgidus was especially strong, thus indicating a function for this unidentified protein. The pauA gene was cloned into E. coli, where it was expressed and resulted in an active enzyme.  (+info)

(7/1356) Short-chain acyl-CoA-dependent production of oxalate from oxaloacetate by Burkholderia glumae, a plant pathogen which causes grain rot and seedling rot of rice via the oxalate production.

In Burkholderia glumae (formerly named Pseudomonas glumae), isolated as the causal agent of grain rot and seedling rot of rice, oxalate was produced from oxaloacetate in the presence of short-chain acyl-CoA such as acetyl-CoA and propionyl-CoA. Upon purification, the enzyme responsible was separated into two fractions (tentatively named fractions II and III), both of which were required for the acyl-CoA-dependent production of oxalate. In conjugation with the oxalate production from oxaloacetate catalyzed by fractions II and III, acetyl-CoA used as the acyl-CoA substrate was consumed and equivalent amounts of CoASH and acetoacetate were formed. The isotope incorporation pattern indicated that the two carbon atoms of oxalate are both derived from oxaloacetate, and among the four carbon atoms of acetoacetate two are from oxaloacetate and two from acetyl-CoA. When the reaction was carried out with fraction II alone, a decrease in acetyl-CoA and an equivalent level of net utilization of oxaloacetate were observed without appreciable formation of CoASH, acetoacetate or oxalate. It appears that in the oxalate production from oxaloacetate and acetyl-CoA, fraction II catalyzes condensation of the two substrates to form an intermediate which is split into oxalate and acetoacetate by fraction III being accompanied by the release of CoASH.  (+info)

(8/1356) NIH shift in flavin-dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase.

The flavoprotein 2-aminobenzoyl-CoA monooxygenase/reductase from the eubacterium Azoarcus evansii catalyzes the dearomatization of 2-aminobenzoyl-CoA. The reaction consists in an O2-dependent monooxygenation at the benzene position 5, which is followed immediately by an NADH-dependent hydrogenation of the intermediate at the same catalytic locus. The reaction was studied by 1H, 2H, and 13C NMR spectroscopy of the products. The main product was characterized as 5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA by two-dimensional NMR spectroscopy. Thus, [5-2H]2-aminobenzoyl-CoA was converted into [6-2H]5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA, indicating a 5 --> 6 shift of the [5-2H] label. Label from NAD2H was transferred to the 3 position of the cyclic eneamine, whereas label from solvent D2O was incorporated into the 4 and the 6 positions of 5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA. The labeling pattern is compatible with the monooxygenation proceeding via what is formally an NIH shift, yielding 5-oxo-2-aminocyclohex-1, 3-diene-1-carboxyl-CoA as a protein-bound intermediate. It is suggested that this shift in flavin-dependent monooxygenation may have general validity.  (+info)

*  ACOT11
"Entrez Gene: ACOT11 acyl-CoA thioesterase 11". "Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)". Protein Data ... Acyl-coenzyme A thioesterase 11 also known as StAR-related lipid transfer protein 14 (STARD14) is an enzyme that in humans is ... Glick BS, Rothman JE (Mar 1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 ( ... Ogiwara H, Tanabe T, Nikawa J, Numa S (Aug 1978). "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme ...
*  Short-chain acyl-coenzyme A dehydrogenase deficiency
... (SCADD), also called ACADS deficiency and SCAD deficiency, is an autosomal ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ... Short-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". Molecular Genetics and Metabolism (Free full text). 95 (4): 195-200. doi ...
*  Medium-chain acyl-coenzyme A dehydrogenase deficiency
Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Wilcken, B.; Hammond, J.; Silink, M. (1994-05-01). "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase ... "Medium-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". PMID 20301597. Leydiker, K. B.; Neidich, J. A.; Lorey, F.; Barr, E. M ... Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ...
*  Very long-chain acyl-coenzyme A dehydrogenase deficiency
... (VLCADD) is a fatty-acid metabolism disorder which prevents the body ... Episodes of very long-chain acyl-coenzyme A dehydrogenase deficiency can be triggered by periods of fasting, illness, and ... pain cardiomyopathy Mutations in the ACADVL gene lead to inadequate levels of an enzyme called very long-chain acyl-coenzyme A ... https://rarediseases.org/rare-diseases/very-long-chain-acyl-coa-dehydrogenase-deficiency-lcad/. ...
*  Short-chain acyl-CoA dehydrogenase
... enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA ... Beinert, H.; Lardy, H.; Myrbäck, K. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D. The Enzymes. 7 (2nd ed.). New York ... short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, ACADS (gene ... Short-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...
*  SOAT2
2003). "Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro ... Lin S; Lu X; Chang CC; Chang TY (2004). "Human Acyl-Coenzyme A:Cholesterol Acyltransferase Expressed in Chinese Hamster Ovary ... 1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". J. Biol. ... 2004). "Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA: ...
*  ACADS
The ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency. The ACADS gene is approximately 13 kb in ... Jethva R, Bennett MJ, Vockley J (Dec 2008). "Short-chain acyl-coenzyme A dehydrogenase deficiency". Molecular Genetics and ... Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. This gene encodes a ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ...
*  2-acylglycerophosphocholine O-acyltransferase
Specificities of acyl coenzyme A:phospholipid acyltransferases". J. Biol. Chem. 240: 1905-1911. PMID 14299609. Van Den Bosch H ... The systematic name of this enzyme class is acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Other names in ... the two substrates of this enzyme are acyl-CoA and 2-acyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and ... is an enzyme that catalyzes the chemical reaction acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine ⇌ {\displaystyle \ ...
*  ACADVL
This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product ... "Very Long-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". 1993. PMID 20301763. GeneReviews/NCBI/NIH/UW entry on Very long- ... Mutations in the ACADVL are associated with very long-chain acyl-coenzyme A dehydrogenase deficiency. The protein encoded by ... ACADVL is linked with very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCADD), which has many symptoms, and typically ...
*  ACADM
... (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ... Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. More than 30 ACADM gene ... The acyl-coenzyme A dehydrogenase for medium-chain fatty acids (ACADM) enzyme is essential for converting these particular ... 1993). "Medium-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". PMID 20301597. Gregersen N, Andresen BS, Bross P, Winter V, ...
*  Retinol O-fatty-acyltransferase
Evidence for acyl-Coenzyme A retinol acyltransferase activity". J. Clin. Invest. 71 (3): 747-53. doi:10.1172/JCI110822. PMC ... Evidence for a fatty acyl coenzyme A: retinol acyltransferase". J. Biol. Chem. 257 (5): 2453-9. PMID 7061433. Molecular and ... In enzymology, a retinol O-fatty-acyltransferase (EC 2.3.1.76) is an enzyme that catalyzes the chemical reaction acyl-CoA + ... The systematic name of this enzyme class is acyl-CoA:retinol O-acyltransferase. Other names in common use include retinol ...
*  ACOX1
Peroxisomal acyl-coenzyme A oxidase 1 is an enzyme that in humans is encoded by the ACOX1 gene. The protein encoded by this ... "Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl". Human ACOX1 genome location and ACOX1 gene details page in the UCSC ... 1994). "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase". Biochem. Biophys. Res. ... 1996). "Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase ...
*  ACOX3
Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene. Acyl-Coenzyme A oxidase 3 also ... "Entrez Gene: ACOX3 acyl-Coenzyme A oxidase 3, pristanoyl". Human ACOX3 genome location and ACOX3 gene details page in the UCSC ... ACOX1 Acyl-CoA oxidase GRCh38: Ensembl release 89: ENSG00000087008 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and ...
*  ACOT7
Cytosolic acyl coenzyme A thioester hydrolase is an enzyme that in humans is encoded by the ACOT7 gene. This gene encodes a ... member of the acyl coenzyme family. The encoded protein hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain ... "Entrez Gene: ACOT7 acyl-CoA thioesterase 7". Human ACOT7 genome location and ACOT7 gene details page in the UCSC Genome Browser ... 2003). "Human brain acyl-CoA hydrolase isoforms encoded by a single gene". Biochem. Biophys. Res. Commun. 299 (1): 49-56. doi: ...
*  Propionate CoA-transferase
Stadtman ER (1952). "Acyl-coenzyme A synthesis by phosphotransacetylase and coenzyme A transphorase". Fed. Proc. 11: 291. ... Other names in common use include propionate coenzyme A-transferase, propionate-CoA:lactoyl-CoA transferase, propionyl CoA: ...
*  ACBD3
... acyl-Coenzyme A binding domain containing 3". Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y (November 2001 ...
*  ACAD9
"Entrez Gene: ACAD9 acyl-Coenzyme A dehydrogenase family, member 9". Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, ... Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T (Jun 1995). "Purification of human very-long-chain acyl-coenzyme A ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. The ACAD9 gene ... Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J (Sep 2005). "Human acyl-CoA ...
*  ACAD8
"Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8". Battaile KP, Nguyen TV, Vockley J, Kim JJ (2004). " ... The protein encoded by ACAD8 is a mitochondrial protein belongs to the acyl-CoA dehydrogenase family of enzymes, which function ... ACAD8 functions as a homotetramer and has an overall structure is similar to other acyl-CoA dehydrogenases. The functional ... and short-chain acyl-CoA dehydrogenases". The Journal of Biological Chemistry. 279 (16): 16526-34. doi:10.1074/jbc.M400034200. ...
*  ACOT1
Glick BS, Rothman JE (Mar 1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 ( ... Ogiwara H, Tanabe T, Nikawa J, Numa S (Aug 1978). "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ... Coenzyme A, and free fatty acids. Recent studies have shown that Acyl-CoA esters have many more functions than simply an energy ...
*  Acyl-CoA thioesterase 9
It is a member of the acyl-CoA thioesterase superfamily, which is a group of enzymes that hydrolyze Coenzyme A esters. There is ... Glick BS, Rothman JE (1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 (6110): ... Ogiwara H, Tanabe T, Nikawa J, Numa S (Aug 1978). "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ...
*  N-ethylmaleimide sensitive fusion protein
Glick BS, Rothman JE (1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 (6110): ...
*  Diglyceride acyltransferase
"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the ... "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". The Journal of ... Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... "Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis". ...
*  Inborn error of metabolism
Medium-chain acyl-coenzyme A dehydrogenase deficiency (often shortened to MCADD.) Disorders of porphyrin metabolism E.g., acute ...
*  Long-chain acyl-CoA dehydrogenase
... palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase ... Hauge, J.G.; Crane, F.L.; Beinert, H. (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III ... Hall, C.L.; Heijkenkjold, L.; Bartfai, T.; Ernster, L.; Kamin, H. (1976). "Acyl coenzyme A dehydrogenases and electron- ... Long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
*  Very-long-chain acyl-CoA dehydrogenase
I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". J. Biol. Chem. 267 (2): 1027-1033. PMID ... Very-long-chain acyl-CoA dehydrogenase (EC 1.3.8.9, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA: ... "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". ... Very-long-chain acyl-CoA dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...
*  Metabolism
The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, ... These coenzymes are therefore continuously made, consumed and then recycled. One central coenzyme is adenosine triphosphate ( ... This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to reduce their ... The electrons then flow through photosystem I and can then either be used to reduce the coenzyme NADP+, for use in the Calvin ...
*  Long-chain-alcohol O-fatty-acyltransferase
Stöveken, T; Kalscheuer R; Malkus U; Reichelt R; Steinbüchel A. (2005). "The wax ester synthase/acyl coenzyme A:diacylglycerol ... However, when using acetyl alcohol as the acyl acceptor, AWAT1 prefers saturated acyl groups, while AWAT2 shows activity with ... "Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol acyltransferase WSD1 required for stem wax ester ... The systematic name of this enzyme class is acyl-CoA:long-chain-alcohol O-acyltransferase. Other names in common use include ...
Acot13 - Acyl-coenzyme A thioesterase 13 - Mus musculus (Mouse) - Acot13 gene & protein  Acot13 - Acyl-coenzyme A thioesterase 13 - Mus musculus (Mouse) - Acot13 gene & protein
Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3- ... providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ...
more infohttp://www.uniprot.org/uniprot/Q9CQR4
Screening for medium chain acyl-CoA dehydrogenase deficiency using electrospray ionisation tandem mass spectrometry | Archives...  Screening for medium chain acyl-CoA dehydrogenase deficiency using electrospray ionisation tandem mass spectrometry | Archives...
1996) Ethylmalonic aciduria is associated with an amino acid variant of short chain acyl-coenzyme A dehydrogenase. Pediatr Res ... Free and acyl carnitines were detected and measured by setting the instrument to detect precursors of m/z (mass/charge ratio) ... 1988) The use of phenylpropionic acid as a loading test for medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis ... 1991) Prevalence of K329E mutation in medium-chain acyl-CoA dehydrogenase gene determined from Guthrie cards. Lancet 338:552- ...
more infohttp://adc.bmj.com/content/79/2/109
In vitro and in vivo consequences of variant medium-chain acyl-CoA dehydrogenase genotypes | Orphanet Journal of Rare Diseases ...  In vitro and in vivo consequences of variant medium-chain acyl-CoA dehydrogenase genotypes | Orphanet Journal of Rare Diseases ...
Fletcher JM, Pitt JJ: Fasting medium chain acyl-coenzyme A dehydrogenase-deficient children can make ketones. Metabolism. 2001 ... life-threatening disorders among which medium-chain acyl coenzyme A dehydrogenase (MCAD [E.C.1.3.99.3; OMIM 201450]) deficiency ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most common inherited disorder of the mitochondrial fatty acid ... Derks TG, Reijngoud DJ, Waterham HR, Gerver WJ, van den Berg MP, Sauer PJ, Smit GP: The natural history of medium-chain acyl ...
more infohttps://ojrd.biomedcentral.com/articles/10.1186/1750-1172-8-43
Acyl CoA dehydrogenase deficiency synonyms, acyl CoA dehydrogenase deficiency antonyms - FreeThesaurus.com  Acyl CoA dehydrogenase deficiency synonyms, acyl CoA dehydrogenase deficiency antonyms - FreeThesaurus.com
Antonyms for acyl CoA dehydrogenase deficiency. 1 synonym for acyl: acyl group. What are synonyms for acyl CoA dehydrogenase ... Synonyms for acyl CoA dehydrogenase deficiency in Free Thesaurus. ... acyl coenzyme A. *Acyl Coenzyme A Oxidase. *acyl coenzyme A:cholesterol acyltransferase ... acyl. (redirected from acyl CoA dehydrogenase deficiency). Also found in: Dictionary, Medical, Encyclopedia.. Related to acyl ...
more infohttps://www.freethesaurus.com/acyl+CoA+dehydrogenase+deficiency
Medium-chain acyl-coenzyme A dehydrogenase deficiency - Wikipedia  Medium-chain acyl-coenzyme A dehydrogenase deficiency - Wikipedia
Matern, D.; Rinaldo, P.; Pagon, R. A.; Bird, T. D.; Dolan, C. R.; Stephens, K.; Adam, M. P. (1993). "Medium-Chain Acyl-Coenzyme ... Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Redirected from Medium-chain acyl-CoA dehydrogenase deficiency). Medium-chain acyl-CoA dehydrogenase deficiency, often known as ... "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase deficiency". Archives of Disease in Childhood. 70 (5): ...
more infohttps://en.m.wikipedia.org/wiki/Medium-chain_acyl-CoA_dehydrogenase_deficiency
Medium-chain acyl-coenzyme A dehydrogenase deficiency  Medium-chain acyl-coenzyme A dehydrogenase deficiency
... (MCAD) ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD deficiency) *Short-chain acyl-coenzyme A dehydrogenase deficiency ( ... Very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCAD deficiency) *Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD). Classification & external resources ICD-9 277.85 ...
more infohttps://www.bionity.com/en/encyclopedia/Medium-chain_acyl-coenzyme_A_dehydrogenase_deficiency.html
Medium-chain acyl-coenzyme A dehydrogenase deficiency - SNPedia  Medium-chain acyl-coenzyme A dehydrogenase deficiency - SNPedia
Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ... Retrieved from "https://www.SNPedia.com/index.php?title=Medium-chain_acyl-coenzyme_A_dehydrogenase_deficiency&oldid=1202172" ...
more infohttps://www.snpedia.com/index.php/Medium-chain_acyl-coenzyme_A_dehydrogenase_deficiency
PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [A - Protein - NCBI  PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [A - Protein - NCBI
PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [Aquila chry... PREDICTED: acyl-coenzyme A thioesterase 9, ... PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [Aquila chrysaetos canadensis]. NCBI Reference Sequence: XP ...
more infohttps://www.ncbi.nlm.nih.gov/protein/XP_011578438.1
Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits | Biocompare.com  Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits | Biocompare.com
Compare Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody- ... Your search returned 24 Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA ELISA Kit across 1 supplier. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2-589797/ELISA_Kit/ELISA_Acyl-Coenzyme_A_Oxidase_1_Palmitoyl
RCSB PDB - Protein Feature View 









 - Acyl-coenzyme A synthetase ACSM2A, mitochondrial - Q08AH3 (ACS2A HUMAN)  RCSB PDB - Protein Feature View - Acyl-coenzyme A synthetase ACSM2A, mitochondrial - Q08AH3 (ACS2A HUMAN)
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttp://www.rcsb.org/pdb/protein/Q08AH3
Acox1 - Peroxisomal acyl-coenzyme A oxidase 1 - Mus musculus (Mouse) - Acox1 gene & protein  Acox1 - Peroxisomal acyl-coenzyme A oxidase 1 - Mus musculus (Mouse) - Acox1 gene & protein
Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs (By ... Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. ... Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. ... Peroxisomal acyl-coenzyme A oxidase 1Add BLAST. 661. Amino acid ... IPR029320 Acyl-CoA_ox_N. IPR006091 Acyl-CoA_Oxase/DH_cen-dom. IPR012258 Acyl-CoA_oxidase. IPR002655 Acyl-CoA_oxidase_C. ...
more infohttps://www.uniprot.org/uniprot/Q9R0H0
Acbd3 MGI Mouse Gene Detail - MGI:2181074 - acyl-Coenzyme A binding domain containing 3  Acbd3 MGI Mouse Gene Detail - MGI:2181074 - acyl-Coenzyme A binding domain containing 3
View mouse Acbd3 Chr1:180726043-180754204 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
more infohttp://www.informatics.jax.org/marker/MGI:2181074
A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts | SpringerLink  A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts | SpringerLink
1986) A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts. In: Freysz L ... A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts. ... Most cells undergo de novo synthesis of acyl chains. However, all tissues take up preformed long chain saturated, ...
more infohttps://link.springer.com/chapter/10.1007/978-1-4684-5212-9_57
ACOX3 (acyl-Coenzyme A oxidase 3, pristanoyl) - KOMP (Knockout Mouse Project)  ACOX3 (acyl-Coenzyme A oxidase 3, pristanoyl) - KOMP (Knockout Mouse Project)
acyl-Coenzyme A oxidase 3, pristanoyl. Synonyms: EST-s59, PCOX, pristanoyl-CoA oxidase. Gene nomenclature, locus information, ... OMIM: ACYL-CoA OXIDASE 3, PRISTANOYL; ACOX3*Gene Ontology: Acox3 *Mouse Phenome DB: Acox3 *UCSC: Chr.5:35,583,060-35,613,801(+) ...
more infohttps://www.komp.org/geneinfo.php?geneid=18145
Acadm - acyl-Coenzyme A dehydrogenase, medium chain | International Mouse Phenotyping Consortium  Acadm - acyl-Coenzyme A dehydrogenase, medium chain | International Mouse Phenotyping Consortium
Based on automated MP annotations supported by experiments on knockout mouse models. Click on icons to go to all Acadm data for that phenotype. ...
more infohttp://www.mousephenotype.org/data/genes/MGI:87867
RCSB PDB 









- 1NTI: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP Macromolecule Annotations...  RCSB PDB - 1NTI: RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP Macromolecule Annotations...
Subtle structural response to ligand binding revealed by residual dipolar coupling refined NMR structures of acyl coenzyme A ... Acyl-CoA binding protein-like Acyl-CoA binding protein Acyl-CoA binding protein Acyl-CoA binding protein Cow (Bos taurus) [ ... RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP. ...
more infohttp://www.rcsb.org/pdb/explore/derivedData.do?structureId=1NTI
Acyl-Coenzyme A:Cholesterol O-Transferase | definition of Acyl-Coenzyme A:Cholesterol O-Transferase by Medical dictionary  Acyl-Coenzyme A:Cholesterol O-Transferase | definition of Acyl-Coenzyme A:Cholesterol O-Transferase by Medical dictionary
Acyl-Coenzyme A:Cholesterol O-Transferase explanation free. What is Acyl-Coenzyme A:Cholesterol O-Transferase? Meaning of Acyl- ... Coenzyme A:Cholesterol O-Transferase medical term. What does Acyl-Coenzyme A:Cholesterol O-Transferase mean? ... Looking for online definition of Acyl-Coenzyme A:Cholesterol O-Transferase in the Medical Dictionary? ... Acyl-Coenzyme A:Cholesterol O-Transferase , definition of Acyl-Coenzyme A:Cholesterol O-Transferase by Medical dictionary https ...
more infohttps://medical-dictionary.thefreedictionary.com/Acyl-Coenzyme+A%3ACholesterol+O-Transferase
Acyl coenzyme A:cholesterol acyltransferase | definition of acyl coenzyme A:cholesterol acyltransferase by Medical dictionary  Acyl coenzyme A:cholesterol acyltransferase | definition of acyl coenzyme A:cholesterol acyltransferase by Medical dictionary
What is acyl coenzyme A:cholesterol acyltransferase? Meaning of acyl coenzyme A:cholesterol acyltransferase medical term. What ... Looking for online definition of acyl coenzyme A:cholesterol acyltransferase in the Medical Dictionary? acyl coenzyme A: ... Acyl coenzyme A:cholesterol acyltransferase , definition of acyl coenzyme A:cholesterol acyltransferase by Medical dictionary ... redirected from acyl coenzyme A:cholesterol acyltransferase) CES1. A gene on chromosome 16q22.2 that encodes a member of the ...
more infohttp://medical-dictionary.thefreedictionary.com/acyl+coenzyme+A%3Acholesterol+acyltransferase
Short-chain acyl-coenzyme A dehydrogenase deficiency - Wikipedia  Short-chain acyl-coenzyme A dehydrogenase deficiency - Wikipedia
Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD), also called ACADS deficiency and SCAD deficiency, is an autosomal ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ... Short-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". Molecular Genetics and Metabolism (Free full text). 95 (4): 195-200. doi ...
more infohttps://en.wikipedia.org/wiki/Short-chain_acyl-coenzyme_A_dehydrogenase_deficiency
  • We prepared a specific antiboty (DM10) against human acyl-conzyme A : cholesterol acyltransnferase (ACAT) and analyzed human tissues by immunohistochemical methods. (nii.ac.jp)
  • The fatty acids are broken down in stages by the successive removal of molecules of acetyl-coenzyme A, which contains 2 carbon atoms. (bionity.com)
  • Patients may also take daily doses of carnitine, which helps reduce toxic accumulation of fatty acids by forming acyl carnitines, which are excreted in the urine. (bionity.com)
  • Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. (uniprot.org)