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.Carnitine Acyltransferases: Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.1-Acylglycerophosphocholine O-Acyltransferase: An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.Glycerol-3-Phosphate O-Acyltransferase: An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.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.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.Acylation: The addition of an organic acid radical into a molecule.Acyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.1-Acylglycerol-3-Phosphate O-Acyltransferase: An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. This enzyme has alpha, beta, gamma, delta and epsilon subunits.Lipoylation: Covalent attachment of LIPIDS and FATTY ACIDS to other compounds and PROTEINS.Glycerophosphates: Any salt or ester of glycerophosphoric acid.Steroid Metabolism, Inborn Errors: Errors in metabolic processing of STEROIDS resulting from inborn genetic mutations that are inherited or acquired in utero.EstersLipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.TartronatesSubstrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Carnitine O-Palmitoyltransferase: An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.Waxes: A plastic substance deposited by insects or obtained from plants. Waxes are esters of various fatty acids with higher, usually monohydric alcohols. The wax of pharmacy is principally yellow wax (beeswax), the material of which honeycomb is made. It consists chiefly of cerotic acid and myricin and is used in making ointments, cerates, etc. (Dorland, 27th ed)Acyl Carrier Protein: Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system.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.Microsomes: Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Sterol 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.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.Glycerophospholipids: Derivatives of phosphatidic acid in which the hydrophobic regions are composed of two fatty acids and a polar alcohol is joined to the C-3 position of glycerol through a phosphodiester bond. They are named according to their polar head groups, such as phosphatidylcholine and phosphatidylethanolamine.Coumaric Acids: Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.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)Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.TriglyceridesPalmitic Acids: A group of 16-carbon fatty acids that contain no double bonds.Phosphatidic Acids: Fatty acid derivatives of glycerophosphates. They are composed of glycerol bound in ester linkage with 1 mole of phosphoric acid at the terminal 3-hydroxyl group and with 2 moles of fatty acids at the other two hydroxyl groups.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.Palmitic Acid: A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Esterification: The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes.Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.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.Lysophospholipids: Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.Mitochondria, Liver: Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Kinetics: The rate dynamics in chemical or physical systems.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.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.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Lipids: A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)Bacterial Proteins: Proteins found in any species of bacterium.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.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.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

Modified peptidoglycan transpeptidase activity in a carbenicillin-resistant mutant of Pseudomonas aeruginosa 18s. (1/3185)

A carbenicillin-resistant mutant of Pseudomonas aeruginosa 18s was found to possess peptidoglycan transpeptidase activity significantly more resistant to inhibition by benzyl penicillin, ampicillin, carbenicillin, and cephaloridine than that of the parent strain. The mutant was more resistant than the parent strain to all of the beta-lactam antibiotics tested, and 50% inhibition values for these compounds against membrane-bound model transpeptidase activity paralleled this increase. The resistance of the mutant to kanamycin, streptomycin, and chloramphenicol was unchanged.  (+info)

Patterns of evolutionary rate variation among genes of the anthocyanin biosynthetic pathway. (2/3185)

The anthocyanin biosynthetic pathway is responsible for the production of anthocyanin pigments in plant tissues and shares a number of enzymes with other biochemical pathways. The six core structural genes of this pathway have been cloned and characterized in two taxonomically diverse plant species (maize and snapdragon). We have recently cloned these genes for a third species, the common morning glory, Ipomoea purpurea. This additional information provides an opportunity to examine patterns of evolution among genes within a single biochemical pathway. We report here that upstream genes in the anthocyanin pathway have evolved substantially more slowly than downstream genes and suggest that this difference in evolutionary rates may be explained by upstream genes being more constrained because they participate in several different biochemical pathways. In addition, regulatory genes associated with the anthocyanin pathway tend to evolve more rapidly than the structural genes they regulate, suggesting that adaptive evolution of flower color may be mediated more by regulatory than by structural genes. Finally, for individual anthocyanin genes, we found an absence of rate heterogeneity among three major angiosperm lineages. This rate constancy contrasts with an accelerated rate of evolution of three CHS-like genes in the Ipomoea lineage, indicating that these three genes have diverged without coordinated adjustment by other pathway genes.  (+info)

Analysis of 4-phosphopantetheinylation of polyhydroxybutyrate synthase from Ralstonia eutropha: generation of beta-alanine auxotrophic Tn5 mutants and cloning of the panD gene region. (3/3185)

The postulated posttranslational modification of the polyhydroxybutyrate (PHA) synthase from Ralstonia eutropha by 4-phosphopantetheine was investigated. Four beta-alanine auxotrophic Tn5-induced mutants of R. eutropha HF39 were isolated, and two insertions were mapped in an open reading frame with strong similarity to the panD gene from Escherichia coli, encoding L-aspartate-1-decarboxylase (EC 4.1.1.15), whereas two other insertions were mapped in an open reading frame (ORF) with strong similarity to the NAD(P)+ transhydrogenase (EC 1.6.1.1) alpha 1 subunit, encoded by the pntAA gene from Escherichia coli. The panD gene was cloned by complementation of the panD mutant of R. eutropha Q20. DNA sequencing of the panD gene region (3,312 bp) revealed an ORF of 365 bp, encoding a protein with 63 and 67% amino acid sequence similarity to PanD from E. coli and Bacillus subtilis, respectively. Subcloning of only this ORF into vectors pBBR1MCS-3 and pBluescript KS- led to complementation of the panD mutants of R. eutropha and E. coli SJ16, respectively. panD-encoded L-aspartate-1-decarboxylase was further confirmed by an enzymatic assay. Upstream of panD, an ORF with strong similarity to pntAA from E. coli, encoding NAD(P)+ transhydrogenase subunit alpha 1 was found; downstream of panD, two ORFs with strong similarity to pntAB and pntB, encoding subunits alpha 2 and beta of the NAD(P)+ transhydrogenase, respectively, were identified. Thus, a hitherto undetermined organization of pan and pnt genes was found in R. eutropha. Labeling experiments using one of the R. eutropha panD mutants and [2-14C]beta-alanine provided no evidence that R. eutropha PHA synthase is covalently modified by posttranslational attachment of 4-phosphopantetheine, nor did the E. coli panD mutant exhibit detectable labeling of functional PHA synthase from R. eutropha.  (+info)

Redundant systems of phosphatidic acid biosynthesis via acylation of glycerol-3-phosphate or dihydroxyacetone phosphate in the yeast Saccharomyces cerevisiae. (4/3185)

In the yeast Saccharomyces cerevisiae lipid particles harbor two acyltransferases, Gat1p and Slc1p, which catalyze subsequent steps of acylation required for the formation of phosphatidic acid. Both enzymes are also components of the endoplasmic reticulum, but this compartment contains additional acyltransferase(s) involved in the biosynthesis of phosphatidic acid (K. Athenstaedt and G. Daum, J. Bacteriol. 179:7611-7616, 1997). Using the gat1 mutant strain TTA1, we show here that Gat1p present in both subcellular fractions accepts glycerol-3-phosphate and dihydroxyacetone phosphate as a substrate. Similarly, the additional acyltransferase(s) present in the endoplasmic reticulum can acylate both precursors. In contrast, yeast mitochondria harbor an enzyme(s) that significantly prefers dihydroxyacetone phosphate as a substrate for acylation, suggesting that at least one additional independent acyltransferase is present in this organelle. Surprisingly, enzymatic activity of 1-acyldihydroxyacetone phosphate reductase, which is required for the conversion of 1-acyldihydroxyacetone phosphate to 1-acylglycerol-3-phosphate (lysophosphatidic acid), is detectable only in lipid particles and the endoplasmic reticulum and not in mitochondria. In vivo labeling of wild-type cells with [2-3H, U-14C]glycerol revealed that both glycerol-3-phosphate and dihydroxyacetone phosphate can be incorporated as a backbone of glycerolipids. In the gat1 mutant and the 1-acylglycerol-3-phosphate acyltransferase slc1 mutant, the dihydroxyacetone phosphate pathway of phosphatidic acid biosynthesis is slightly preferred as compared to the wild type. Thus, mutations of the major acyltransferases Gat1p and Slc1p lead to an increased contribution of mitochondrial acyltransferase(s) to glycerolipid synthesis due to their substrate preference for dihydroxyacetone phosphate.  (+info)

Purification and characterization of phospholipase B from Kluyveromyces lactis, and cloning of phospholipase B gene. (5/3185)

Phospholipase B (PLB) from the yeast Kluyveromyces lactis was purified to homogeneity from culture medium. The enzyme was highly glycosylated with apparent molecular mass of 160-250 kDa, and had two pH optima, at pH 2.0 and pH 7.5. At acidic pH the enzyme hydrolyzed all phospholipid substrates tested here without metal ion. On the other hand, at alkaline pH the enzyme showed substrate specificity for phosphatidylcholine and lysophosphatidylcholine and required Ca2+, Fe3+, or Al3+ for the activity. The alkaline activity was increased more than 20-fold in the presence of Al3+ compared to that in the presence of Ca2+. cDNA sequence of PLB (KlPLB) was analyzed by a combination of several PCR procedures. KlPLB encoded a protein consist of 640 amino acids and the deduced amino acid sequence showed 66.7% similarity with the T. delbrueckii PLB. The amino acid sequence contained the lipase consensus sequence (G-X-S-X-G) and the catalytic aspartic acid motif. Replacement of Arg-112 or Asp-406 with alanine caused loss of the enzymatic activity at both pH. These results suggested that PLB activity are dependent on a catalytic mechanism similar to that of cytosolic phospholipase A2.  (+info)

Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. (6/3185)

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

Epidermal growth factor regulates fatty acid uptake and metabolism in Caco-2 cells. (7/3185)

Epidermal growth factor (EGF) has been reported to stimulate carbohydrate, amino acid, and electrolyte transport in the small intestine, but its effects on lipid transport are poorly documented. This study aimed to investigate EGF effects on fatty acid uptake and esterification in a human enterocyte cell line (Caco-2). EGF inhibited cell uptake of [14C]palmitate and markedly reduced its incorporation into triglycerides. In contrast, the incorporation in phospholipids was enhanced. To elucidate the mechanisms involved, key steps of lipid synthesis were investigated. The amount of intestinal fatty acid-binding protein (I-FABP), which is thought to be important for fatty acid absorption, and the activity of diacylglycerol acyltransferase (DGAT), an enzyme at the branch point of diacylglycerol utilization, were reduced. EGF effects on DGAT and on palmitate esterification occurred at 2-10 ng/ml, whereas effects on I-FABP and palmitate uptake occurred only at 10 ng/ml. This suggests that EGF inhibited palmitate uptake by reducing the I-FABP level and shifted its utilization from triglycerides to phospholipids by inhibiting DGAT. This increase in phospholipid synthesis might play a role in the restoration of enterocyte absorption function after intestinal mucosa injury.  (+info)

Role of ArgR in activation of the ast operon, encoding enzymes of the arginine succinyltransferase pathway in Salmonella typhimurium. (8/3185)

The ast operon, encoding enzymes of the arginine succinyltransferase (AST) pathway, was cloned from Salmonella typhimurium, and the nucleotide sequence for the upstream flanking region was determined. The control region contains several regulatory consensus sequences, including binding sites for NtrC, cyclic AMP receptor protein (CRP), and ArgR. The results of DNase I footprintings and gel retardation experiments confirm binding of these regulatory proteins to the identified sites. Exogenous arginine induced AST under nitrogen-limiting conditions, and this induction was abolished in an argR derivative. AST was also induced under carbon starvation conditions; this induction required functional CRP as well as functional ArgR. The combined data are consistent with the hypothesis that binding of one or more ArgR molecules to a region between the upstream binding sites for NtrC and CRP and two putative promoters plays a pivotal role in modulating expression of the ast operon in response to nitrogen or carbon limitation.  (+info)

*Sterol O-acyltransferase

... (also called Acyl-CoA cholesterol acyltransferase, Acyl-CoA cholesterin acyltransferase[citation ... Acyl-CoA cholesterol acyl transferase EC 2.3.1.26, more simply referred to as ACAT, also known as sterol O-acyltransferase ( ... sterol acyltransferase) different from the yeast and mammalian acyl-CoA:sterol acyltransferases". The Journal of Biological ... In yeast, acyl-CoA:sterol acyltransferase (ASAT) is functionally equivalent to ACAT. Although studies in vitro and in yeast ...

*Arginine N-succinyltransferase

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

*AGPAT2

"Entrez Gene: AGPAT2 1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acid acyltransferase, beta)". Human AGPAT2 ... 1-acyl-sn-glycerol-3-phosphate acyltransferase beta is an enzyme that in humans is encoded by the AGPAT2 gene. This gene ... Aguado B, Campbell RD (Feb 1998). "Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene ... "Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3". The Journal of ...

*GPAM

Glycerol-3-phosphate acyltransferase 1, mitochondrial is an enzyme that in humans is encoded by the GPAM gene. Glycerol-3- ... "Entrez Gene: GPAM glycerol-3-phosphate acyltransferase, mitochondrial". Skorve J, Ruyter B, Rustan AC, et al. (1990). "Effect ... Igal RA, Wang S, Gonzalez-Baró M, Coleman RA (2001). "Mitochondrial glycerol phosphate acyltransferase directs the ... Thomas PD, Poznansky MJ (1990). "Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase. ...

*Carnitine palmitoyltransferase II deficiency

In addition to similarities shared by the acyltransferases, CPT II also contains a distinct insertion of 30 residues in the ... CPT II shares structural elements with other members of the carnitine acyltransferase protein family. The crystal structure of ... 1993). "Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a ... is fully conserved in all members of the carnitine acyltransferase family and has been localized to the enzyme active site, ...

*Phosphatidylcholine-sterol O-acyltransferase

... lecithin-cholesterol acyltransferase), lecithin:cholesterol acyltransferase, and lysolecithin acyltransferase. This enzyme ... Other names in common use include lecithin---cholesterol acyltransferase, phospholipid---cholesterol acyltransferase, LCAT ( ... In enzymology, a phosphatidylcholine---sterol O-acyltransferase (EC 2.3.1.43) is an enzyme that catalyzes the chemical reaction ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

*Acyltransferase

Glyceronephosphate O-acyltransferase Lecithin-cholesterol acyltransferase Long-chain-alcohol O-fatty-acyltransferase ... Acyltransferase is a type of transferase enzyme that acts upon acyl groups. Examples include: ... Acetyltransferase Acyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...

*Palmitoyl acyltransferase

... is a group of enzymes that transfer palmityl group to -SH group on cysteine on a protein. This ... The palmitoyl acyltransferase was isolated and identified in 1999. The catalytic domain of the protein has aspartate-histidine- ... Draper, J. M.; Smith, C. D. (2009). "Palmitoyl acyltransferase assays and inhibitors (Review)". Molecular Membrane Biology. 26 ...

*Diglyceride acyltransferase

... (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis". Proceedings of the National Academy of Sciences of ... The protein is homologous to other membrane-bound O-acyltransferases. There are two isozymes of DGAT encoded by the genes DGAT1 ... diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption". The Journal of ...

*Phospholipid acyltransferase

This family contains acyltransferases involved in phospholipid biosynthesis and proteins of unknown function. This family also ... 1-acyl-sn-glycerol-3-phosphate acyltransferase InterPro: IPR004552 AGPAT1; AGPAT2; AGPAT3; AGPAT4; AGPAT5; AGPAT6; AGPAT7; ... AYTL1; AYTL2; GNPAT; GPAM; GPAT3; LYCAT; TAZ; TMEM68; Neuwald AF (1997). "Barth syndrome may be due to an acyltransferase ...

*Monolysocardiolipin acyltransferase

... (MLCL AT-1) is a mitochondrial acyltransferase that facilitates the remodeling of ... However, acyltransferase activities involved in the reacylation of MLCL had not been identified or characterized in any ... In 2003, the same lab purified and characterized an MLCL acyltransferase in pig liver mitochondria, and by comparing this ... Danos, Maria; Taylor, William A.; Hatch, Grant M. (2008). "Mitochondrial monolysocardiolipin acyltransferase is elevated in the ...

*Pseudotropine acyltransferase

... (EC 2.3.1.186, pseudotropine:acyl-CoA transferase, tigloyl-CoA:pseudotropine acyltransferase, ... Pseudotropine acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... pseudotropine O-acyltransferase. This enzyme catalyses the following chemical reaction acyl-CoA + pseudotropine ⇌ {\ ... pseudotropine acyltransferase - an enzyme of tropane alkaloid biosynthesis". Phytochemistry. 39: 315-322. doi:10.1016/0031-9422 ...

*BAHD acyltransferase

The BAHD acyltransferases are a super family of enzymes found primarily in plants, algae and bacteria. They are CoA-dependent ... 1998). In plants, BAHD acyltransferases are often involved in the production of phenolic secondary metabolites, for example in ... Acyltransferases in plants: a good time to be BAHD. Curr Opin Plant Biol 9: 331-340. DOI: 10.1016/j.pbi.2006.03.016 Stewart, ... The Pun1 gene for pungency in pepper encodes a putative acyltransferase. Plant J 42: 675-688. DOI: 10.1111/j.1365-313X. ...

*Lysolecithin acyltransferase

... may refer to: 1-acylglycerophosphocholine O-acyltransferase, an enzyme Phosphatidylcholine-sterol ...

*Tropine acyltransferase

... (EC 2.3.1.185, tropine:acyl-CoA transferase, acetyl-CoA:tropan-3-ol acyltransferase, tropine ... Tropine acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... and 3β-acetoxytropanes by Datura stramonium transformed root cultures involves two acetyl-CoA-dependent acyltransferases". FEBS ... acetyltransferase, tropine tigloyltransferase, TAT) is an enzyme with systematic name acyl-CoA:tropine O-acyltransferase. This ...

*Lysocardiolipin acyltransferase 1

"The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic ... Lysocardiolipin acyltransferase 1 is a protein that in humans is encoded by the LCLAT1 gene. GRCh38: Ensembl release 89: ... Lysocardiolipin acyltransferase 1". Retrieved 2018-01-18. Zhao Y, Chen YQ, Li S, Konrad RJ, Cao G (2009). " ...

*Ghrelin O-acyltransferase

... also known as membrane bound O-acyltransferase domain containing 4 is an enzyme that in humans is ... Heppner KM, Tong J, Kirchner H, Nass R, Tschöp MH (February 2011). "The ghrelin O-acyltransferase-ghrelin system: a novel ... Lim CT, Kola B, Grossman A, Korbonits M (2011). "The expression of ghrelin O-acyltransferase (GOAT) in human tissues". ... It is homologous to other membrane-bound O-acyltransferases. GRCh38: Ensembl release 89: ENSG00000177669 - Ensembl, May 2017 ...

*Lecithin retinol acyltransferase

... is an enzyme that in humans is encoded by the LRAT gene. Lecithin retinol acyltransferase is a ... "Entrez Gene: LRAT lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase)". Brown, Gordon; Beatriz ... Jahng WJ, Xue L, Rando RR (2004). "Lecithin retinol acyltransferase is a founder member of a novel family of enzymes". ... Andreola F, Giandomenico V, Spero R, De Luca LM (2001). "Expression of a smaller lecithin:retinol acyl transferase transcript ...

*Galactolipid O-acyltransferase

... mono-beta-D-galactosyldiacylgly cerol acyltransferase. This enzyme is also called galactolipid:galactolipid acyltransferase. ... In enzymology, a galactolipid O-acyltransferase (EC 2.3.1.134) is an enzyme that catalyzes the chemical reaction 2 mono-beta-D- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Dorne A-J; Douce R (1986). "Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer ...

*Dolichol O-acyltransferase

In enzymology, a dolichol O-acyltransferase (EC 2.3.1.123) is an enzyme that catalyzes the chemical reaction palmitoyl-CoA + ... This enzyme is also called acyl-CoA:dolichol acyltransferase. Tollbom O, Valtersson C, Chojnacki T, Dallner G (1988). " ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

*Galactosylacylglycerol O-acyltransferase

In enzymology, a galactosylacylglycerol O-acyltransferase (EC 2.3.1.141) is an enzyme that catalyzes the chemical reaction acyl ... The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:D-galactosylacylglycerol O-acyltransferase. Other names ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Chen HH, Wickrema A, Jaworski JG (1988). "Acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol acyltransferase from the ...

*Ecdysone O-acyltransferase

Other names in common use include acyl-CoA:ecdysone acyltransferase, and fatty acyl-CoA:ecdysone acyltransferase. Slinger AJ; ... In enzymology, an ecdysone O-acyltransferase (EC 2.3.1.139) is an enzyme that catalyzes the chemical reaction palmitoyl-CoA + ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Isaac RE (1988). "Acyl-CoA-ecdysone acyltransferase activity from the ovary of P americana". Insect Biochem. 18 (8): 779-784. ...

*Glyceronephosphate O-acyltransferase

glycerone-phosphate O-acyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ... Glyceronephosphate O-acyltransferase is an enzyme associated with Rhizomelic chondrodysplasia punctata type 2. GNPAT is located ...

*Phospholipid:diacylglycerol acyltransferase

The systematic name of this enzyme class is phospholipid:1,2-diacyl-sn-glycerol O-acyltransferase. This enzyme is also called ... In enzymology, a phospholipid:diacylglycerol acyltransferase (EC 2.3.1.158) is an enzyme that catalyzes the chemical reaction ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and ...

*Glutamine N-acyltransferase

The systematic name of this enzyme class is acyl-CoA:L-glutamine N-acyltransferase. Webster LT, Siddiqui UA, Lucas SV, Strong ... In enzymology, a glutamine N-acyltransferase (EC 2.3.1.68) is an enzyme that catalyzes the chemical reaction acyl-CoA + L- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... JM, Mieyal JJ (1976). "Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in ...
Glutathione S-transferase (GST) isoenzymes of human pancreas were purified, characterized and evaluated for their possible role in the metabolism of ethanol. Human pancreas has at least two GST isoenzymes belonging to the Alpha class (pI 8.8 and 8.1), one belonging to the Mu class (pI 6.4) and one belonging to the Pi class (pI 4.9). During the purification of GSTs from pancreas as well as from heart, liver, lung, brain and muscle, the fatty acid ethyl ester synthase (FAEES) activity was monitored in order to evaluate the role of GSTs in metabolism of ethanol, as suggested in earlier studies. Both t.l.c. and h.p.l.c. were used to identify ethyl oleate in reaction mixtures to monitor FAEES activity. During the purification of GSTs with the use of affinity chromatography on GSH linked to epoxy-activated Sepharose 6B, FAEES and GST activities from each of these tissues segregated independently. Purified GST isoenzymes from these tissues did not exhibit any FAEES activity. Antibodies raised against ...
Shop Acyl-coenzyme A amino acid N-acyltransferase ELISA Kit, Recombinant Protein and Acyl-coenzyme A amino acid N-acyltransferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Lecithin retinol acyltransferase (LRAT) is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester. This reaction is essential for the retinoid cycle in retinal photopigmentation and to metabolize vitamin A in the liver. Mutations in the LRAT gene have been associated with early-onset severe retinal dystrophy. LRAT is also known as phosphatidylcholine--retinol O-acyltransferase, LCA14, AI449251, and 1300010A18Rik.. ...
Lecithin retinol acyltransferase (LRAT) is a microsomal enzyme that catalyzes the esterification of all-trans-retinol into all-trans-retinyl ester. This reaction is essential for the retinoid cycle in retinal photopigmentation and to metabolize vitamin A in the liver. Mutations in the LRAT gene have been associated with early-onset severe retinal dystrophy. LRAT is also known as phosphatidylcholine--retinol O-acyltransferase, LCA14, AI449251, and 1300010A18Rik.. ...
A novel location of the bile-acid-conjugating enzyme bile acid-CoA:amino acid N-acyltransferase (BAT) has been discovered in the cytosolic fraction of rat kidney. Both taurine and glycine were utilized as substrates. Formation of bile acid N-acyl amidates was verified by h.p.l.c. by comparison with authentic standards and by specific hydrolysis using cholylglycine hydrolase. Immunoblot analysis using a human liver anti-BAT polyclonal antibody indicated that rat kidney BAT has the same molecular mass as rat liver BAT. These findings suggest that the kidney has a role in bile acid metabolism and physiology.. ...
This study has demonstrated the importance of NOME in mediating acute pancreatic toxicity and inflammation induced by alcohol, damage arising primarily from Ca2+-dependent mitochondrial dysfunction in PACs. Many theories have been proposed to explain the detrimental effects of alcohol in AP,22 ,23 including direct actions on Ca2+-release mechanisms,24 OME-sensitised mitochondrial dysfunction25 and formation of toxic FAEEs.26 The association between alcohol and fat in pancreatic damage is particularly intriguing; diets rich in corn oil and alcohol induce chronic pancreatic injury in rats.24 Epidemiological studies suggest that high fat diets may be linked to development of acute and chronic alcoholic pancreatitis,27 while hypertriglyceridaemia is an independent risk factor for both.28 The present data highlight the importance of NOME in mediating acute PAC damage leading to AP. It is likely that under conditions of OME inhibition, available alcohol and fatty acid from triglyceride hydrolysis are ...
Glycylpeptide N-tetradecanoyltransferase 1 also known as myristoyl-CoA:protein N-myristoyltransferase 1 (NMT-1) is an enzyme that in humans is encoded by the NMT1 gene. GRCh38: Ensembl release 89: ENSG00000136448 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000020936 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Duronio RJ, Reed SI, Gordon JI (May 1992). "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae". Proc Natl Acad Sci U S A. 89 (9): 4129-33. doi:10.1073/pnas.89.9.4129. PMC 525646 . PMID 1570339. "Entrez Gene: NMT1 N-myristoyltransferase 1". Rajala RV, Datla RS, Moyana TN, et al. (2000). "N-myristoyltransferase". Mol. Cell. Biochem. 204 (1-2): 135-55. doi:10.1023/A:1007012622030. PMID 10718634. Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580-5. doi:10.1093/embo-reports/kve141. PMC 1083955 . ...
A combination of site-directed and random mutagenesis generated sequence variants of a plastidial lysophosphatidic acid acyltransferase. Alanine substitutions of residues present within two conserved motifs including the putative catalytic histidine resulted in a loss of acyltransferase activity assessed as complementation competance. Substitutions at five sites within the central core resulted in reduced or loss of activity. Truncation mutants reveal that sequences in the C-terminal moiety are essential for function.. ...
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This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2012 ...
Using 5-rapid amplification of cDNA ends, we have identified an extended 5-end of mRNA coding for human myristoyl-CoA:protein N-myristoyltransferase (NMT). PCR using primers based on this new 5-sequence and reverse primers within the currently accepted coding sequence of the enzyme resulted in the identification of a novel splice variant of NMT. In vitro translation of these cDNAs resulted in the production of proteins with apparent molecular masses of 63 kDa and 48 kDa. Immunoprecipitation of NMT from human cell lines and immunoblotting of a range of rat tissues has identified proteins with molecular masses corresponding to those derived from these cDNAs, and provided evidence that their relative abundance differs among tissues. Our results provide evidence that this enzyme exists in different forms resulting from alternative splicing of the mRNA ...
GPI transamidase component PIG-T is an enzyme that in humans is encoded by the PIGT gene. This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. PIGT has been shown to interact with PIGK and GPAA1. GRCh38: Ensembl release 89: ENSG00000124155 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000017721 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Vainauskas S, Menon AK (Apr 2005). "Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex". J Biol Chem. 280 (16): 16402-9. doi:10.1074/jbc.M414253200. PMID 15713669. "Entrez Gene: ...
Proteins that have a GPI glycolipid modification are acknowledged to be key in the lifecycle of Plasmodium; for example the involvement of the GPI-anchored MSP1 on merozoites in erythrocyte invasion. The enzyme that transfers the preformed GPI to the proteins such as MSP1 is named GPI:protein transamidase, however, studying this enzyme biochemically has been arduous, due to the following hurdles. Firstly, the GPI:protein transamidase functions as a subunit in multidomain complex, some components of which maybe membrane associated, and there are no reports of functional recombinant reconstitution of this complex. Secondly, there are no convenient and sensitive transamidase assays available that are amenable to medium/high throughput studies, even though large small molecule cysteine peptidase inhibitor libraries exist and can be used to studying this enzyme.. Any input/thoughts on how to overcome the aforementioned obstacles in studying the Plasmodium GPI:protein transamidase would be most ...
Home » N-hydroxyarylamine o-acetyltransferase. N-hydroxyarylamine O-acetyltransferase (Science: enzyme) May be an aspect or arylamine acetyltransferase (EC 2.3.1.5) Registry number: EC 2.3.1.118 Synonym: n,o-arylhydroxamic acid acyltransferase, ahxa acyltransferase, arylhydroxamic acid acyltransferase, n-ohaa acetyltransferase, arylhydroxylamine o-acetyltransferase, arylhydroxamate n,o-acetyltransferase, acetyl-coA n-hydroxyarylamine n-acetyltransferase ...
Complete information for BAAT gene (Protein Coding), Bile Acid-CoA:Amino Acid N-Acyltransferase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
BioAssay record AID 144067 submitted by ChEMBL: Tested for Inhibitory concentration against human N-myristoyltransferase (NMT) in radiochemical HPLC end point assay with peptide GNAASARR-NH2 and [3H]myristoyl-CoA radioligand at 1 uM; ND=Not determined.
Colon cancer is one of the most common malignant diseases and a major cause of mortality in the Western world. Metastasis to lymph nodes and other gastrointestinal organs, especially to the liver and lungs, is most common and occurs in up to 25% of cancer patients when initially diagnosed. The majority of colon cancers develop from noncancerous adenomatous polyps on the lining of the colon which grow over the years to become cancerous. If detected early, the surgical resections of the growth, often in combination with chemotherapy, significantly increases life expectancy. We have shown that the enzyme N-myristoyltransferase (NMT) which carries out lipid modification of several proteins (including many of those involved in oncogenesis) is expressed at higher levels in cancerous tissues from the colon. We have also shown that in peripheral blood mononuclear cells (PBMC) and bone marrow (BM) cells collected from colon cancer patients and from azoxymethane-induced rats the expression and localization of NMT
Site-directed mutagenesis of rodent liver bile acid CoA: amino acid N-acyltransferase (BAT) - this project involves a combination of molecular biology, enzymology and protein mass ...
BAAT - Rabbit polyclonal antibody to BAT (bile acid Coenzyme A: amino acid N-acyltransferase (glycine N-choloyltransferase)) available from OriGene
Creative Biostructure now can provide advanced custom Mempro™ CoA-dependent acyltransferases production using virus-like particles for both academic and industry applications.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
lipoyltransferase II: transfers lipoyl group from lipoyl-AMP to the specific lysine residue of lipoate-dependent enzymes; isolated from bovine liver; amino acid sequence in first source; GenBank AB006441
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This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in lysine
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BY MARY L. CHANG. Diglyceride acyltransferase, known to lipidologists as DGAT, gets a lot of attention in the April issue of the Journal of Lipid Research, where its the focus of an article by researchers at Columbia University and AstraZeneca and a related commentary. ...
Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. In contrast to DGAT2 it is not essential for survival. May be involved in VLDL (very low density lipoprotein) assembly. In liver, plays a role in esterifying exogenous fatty acids to glycerol. Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders. ...
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Complete information for MOGAT1 gene (Protein Coding), Monoacylglycerol O-Acyltransferase 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glut
MOGAT2山羊多克隆抗体(ab106247)可与人样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
A RUGALMAS FOGLALKOZTATÁS ELTERJESZTÉSE A SZÉCHENYI 2020 PROGRAM TÁMOGATÁSÁVAL 11 KONZORCIUM EGYÜTTMŰKÖDÉSÉBEN. 2,007 milliárd forint európai uniós támogatás segítségével valósul meg a rugalmas foglalkoztatás elterjesztését célzó Széchenyi 2020 pályázat GINOP 5.3.1., „A" komponense. A pályázat célkitűzése, hogy a konvergencia régiókban működő kis- illetve közepes vállalatok (kkv-k) szakmailag magas szintű, száz százalékosan finanszírozott átvilágítási, tanácsadói és fejlesztői szolgáltatást vehessenek igénybe munkaszervezésük rugalmasabbá tételéhez. A Széchenyi 2020 Program keretében 2014-ben jelent meg „A rugalmas foglalkoztatás elterjesztése a konvergencia régiókban" című pályázat, melynek „A munkáltatói átvilágítást végző szervezetek kiválasztása és az átvilágítás lefolytatása" elnevezésű „A" komponense a szervezeti kultúra fejlesztésének és a munka-magánélet összhangjának támogatását ...
[SWF]http://www3.chem.nagoya-u.ac.jp/wordpress/wp-content/themes/landscape/content_images/faculty_molecular.swf,595,241[/SWF] 生体システムの中に見られる大小様々なビルディングブロック分子は、化学的な多様性があり、また、近年の合成化学やバイオテクノロ ...
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Genetic information processingProtein fateProtein modification and repairapolipoprotein N-acyltransferase (TIGR00546; EC 2.3.1.-; HMM-score: 15.1) ...
The Ca2+ ionophore 4-Br A23187 is effective in increasing [Ca2+]i and eliciting secretion when ICRAC is inhibited by SK&F 96365. Antigen (Ag) (1 μg/ml) sti
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Looking for online definition of GPI transamidase component PIG-S in the Medical Dictionary? GPI transamidase component PIG-S explanation free. What is GPI transamidase component PIG-S? Meaning of GPI transamidase component PIG-S medical term. What does GPI transamidase component PIG-S mean?
Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors (By similarity). Converts lysophosphatidylcholine to phosphatidycholine.
Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors ...
The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT (ScLPLAT) belongs to a distinct protein family that includes human MBOAT1, MBOAT2, MBOAT4, and several closely related proteins from other eukaryotes. We further show that two plant proteins within this family, the Arabidopsis proteins AtLPLAT1 and AtLPLAT2, possess lysophospholipid acyltransferase activities similar to ScLPLAT. We propose that other members of this protein family, which we refer to as the LPLAT family, also are likely to possess LPLAT activity. Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that it cannot efficiently use lysophosphatidic acid produced by acylation of glycerol-3-phosphate in vitro.. ...
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1C4T: Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase.
In response to salt water stress there is a marked increase in the plasma membranes of the epithelial secretory cells of the salt glands of domestic ducklings. In the present study, the fine-structural localization of the acyltransferases involved in synthesis of phospholipids has been investigated in this tissue during this increased biogenesis of plasma membranes. The specific activity of the acyltransferases of the salt gland rose in response to salt stress, and this preceded the rapid increase in weight and cellular differentiation. After the weight increase of the gland became established, the specific activity of the acyltransferases declined, but the total activity remained constant. Salt gland tissue fixed in a mixture of glutaraldehyde and formaldehyde retained 35% of the acyltransferase activity of unfixed tissue. Cytochemical studies of the localization of acyltransferase activity in fixed and unfixed salt gland showed reaction product associated only with the lamellar membranes of ...
BioAssay record AID 143943 submitted by ChEMBL: The compound was tested for the affinity against Candida albicans N-myristoyltransferase (NMT).
Falany, C.N., Johnson, M.R., Barnes, S. and Diasio, R.B. (1994). „Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase". J. Biol. Chem. 269: 19375-19379. PMID 8034703 ...
Acyltransferase which contributes to the regulation of free arachidonic acid (AA) in the cell through the remodeling of phospholipids. Mediates the conversion of lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Required for cortical lamination during brain development (By similarity).
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Triacylglycerol (TAG) is a major component of lipid storage in yeast. The acyl CoA: diacylgycerol acyltransferase (DGAT) that catalyzes the final and rate-limiting step in the production of TAG is rather interesting. Consequently, cloning and analysis of the gene-encoding TAG synthase, diacylglycerol acyltransferase gene (DGA1), of the oleaginous yeast Rhodosporidiobolus fluvialis DMKU-RK253 were undertaken. Analysis of the deduced amino acid sequence of DGA1 from R. fluvialis DMKU-RK253 (RfDGA1) showed similarity with the acyl-CoA:diacylglycerol acyltransferase 2 (DGAT2) from other organisms. The cDNA of RfDGA1 was cloned into the yeast expression vector pYES2 and heterologously overexpressed in Saccharomyces cerevisiae. One of the transformants showed a 1.6-fold increase in lipid content compared with the wild-type strain harbouring the pYES2 empty vector. Furthermore, DGA1 overexpression in R. fluvialis DMKU-RK253 resulted in a 2.5-fold increase in lipid content when compared with the wild-type
GenBank) dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (E2)(dihydrolipoamide succinyltransferase component of 2-oxoglutaratedehydrogenase complex ...
Objective HCV is intimately linked with the liver lipid metabolism, devoted to the efflux of triacylglycerols stored in lipid droplets (LDs) in the form of triacylglycerol-rich very-low-density lipoproteins (VLDLs): (i) the most infectious HCV particles are those of lowest density due to association with triacylglycerol-rich lipoproteins and (ii) HCV-infected patients frequently develop hepatic steatosis (increased triacylglycerol storage). The recent identification of lysophosphatidylcholine acyltransferase 1 (LPCAT1) as an LD phospholipid-remodelling enzyme prompted us to investigate its role in liver lipid metabolism and HCV infectious cycle. ...
Journal of Immunology Research is a peer-reviewed, Open Access journal that provides a platform for scientists and clinicians working in different areas of immunology and therapy. The journal publishes research articles, review articles, as well as clinical studies related to classical immunology, molecular immunology, clinical immunology, cancer immunology, transplantation immunology, immune pathology, immunodeficiency, autoimmune diseases, immune disorders, and immunotherapy.
Transgenic technology has become an important technique for crop genetic improvement. The application of well-characterized promoters is essential for developing a vector system for efficient genetic transformation. Therefore, isolation and functional validation of more alternative constitutive promoters to the CaMV35S promoter is highly desirable. In this study, a 2093-bp sequence upstream of the translation initiation codon ATG of AtSCPL30 was isolated as the full-length promoter (PD1). To characterize the AtSCPL30 promoter (PD1) and eight 5′ deleted fragments (PD2-PD9) of different lengths were fused with GUS to produce the promoter::GUS plasmids and were translocated into Nicotiana benthamiana. PD1-PD9 could confer strong and constitutive expression of transgenes in almost all tissues and development stages in Nicotiana benthamiana transgenic plants. Additionally, PD2-PD7 drove transgene expression consistently over twofold higher than the well-used CaMV35S promoter under normal and stress
phosphatidylethanolamine, N-acylphosphatidylethanolamine, N-monomethylphosphatidylethanolamine, N,N-dimethylphosphatidylethanolamine, phosphatidylethanol, lysophosphatidylethanolamine - structure, occurrence, biochemistry and analysis, N-acyl-phosphatidylethanolamine
Metabolic & Genetic Information Center Inborn erros of metabolism LIPOYLTRANSFERASE 2 DEFICIENCY (LIPT2D) NELABA NELABA ENCEPHALOPATHY, NEONATAL SEVERE, WITH LACTIC ACIDOSIS AND BRAIN ABNORMALITIES
Sigma-Aldrich offers abstracts and full-text articles by [James R Petrie, Thomas Vanhercke, Pushkar Shrestha, Anna El Tahchy, Adam White, Xue-Rong Zhou, Qing Liu, Maged P Mansour, Peter D Nichols, Surinder P Singh].
Amazon SWF metrics are available starting today in all AWS regions. Amazon SWF is a background job, task coordination and state management service for cloud and on-premise applications. It provides features that let you build and run reliable background jobs and other applications that need to track and manage state. With Amazon SWF, you can stop writing complex glue-code and state machinery and invest more in the business logic that makes your applications unique. Amazon SWF metrics give you latency information to tell you how long steps in your workflows are taking and give you counts for key state changes in those workflows. Now, in addition to using CPU metrics to scale your worker fleets with Amazon Auto Scaling, you can use information about how long your workflow steps are taking to determine if your workers are falling behind and automatically add or reduce computing capacity. This helps you make sure your workflow applications can efficiently keep up with demand from your end-users. For ...
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Palmitoyl acyl transferase (PAT); Palmitoylating enzyme; zDHHC proteins Protein palmitoylation is the first discovered and the most common lipid modification. This posttranslational change involves...
RPH629Hu01, MGAT2; DGAT2L5; DC5; 2-Acylglycerol O-Acyltransferase 2; Diacylglycerol O-acyltransferase candidate 5; Diacylglycerol acyltransferase 2-like protein 5 | Products for research use only!
1IIC: Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis.
View Zdhhc17/Zdhhc17 FVB.129P2-Zdhhc17: phenotypes, images, diseases, and references.
Sigma-Aldrich offers abstracts and full-text articles by [Zhiqiang Li, Hui Jiang, Tingbo Ding, Caixia Lou, Hai H Bui, Ming-Shang Kuo, Xian-Cheng Jiang].
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GPI Transamidase Subunit; Involved In Attachment Of Glycosylphosphatidylinositol (GPI) Anchors To Proteins; May Have A Role In Recognition Of The Attachment Signal Or Of The Lipid Portion Of GPI
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The lung (adjectival form: pulmonary) is the essential respiration organ in many air-breathing animals, including most tetrapods, a few fish and a few snails. In mammals and the more complex life forms, the two lungs are located near the backbone on either side of the heart. Their principal function is to transport oxygen from the atmosphere into the bloodstream, and to release carbon dioxide from the bloodstream into the atmosphere. This exchange of gases is accomplished in the mosaic of specialized cells that form millions of tiny, exceptionally thin-walled air sacs called alveoli ...
A gene gun or a biolistic particle delivery system, originally designed for plant transformation, is a device for injecting cells with genetic information. The payload is an elemental particle of a heavy metal coated with plasmid DNA. This technique is often simply referred to as bioballistics or biolistics ...
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Fast delivery of ZDHHC3 knockout Human Cell Lines for the study of gene function. Created by CRISPR/Cas9 genome editing. Includes matched wildtype control.
Diacylglycerol acyltransferase (DGAT), an integral membrane protein of the endoplasmic reticulum, catalyses the final step in the sn-glycerol-3-phosphate pathway leading to triacylglycerol. Although DGAT has been cloned ...
Title: Polyketide bio-derivatization using thepromiscuous acyltransferase KirCIIAuthor: Musiol-Kroll, E.M., Zubeil, F., Schafhauser, T.,Hartner, T., Kulik, A., McArthur, J., Koryakina, I., Wohlleben, W., Grond, S.,Williams, G.J., Lee, S.Y., and Weber,
Title: Polyketide bio-derivatization using thepromiscuous acyltransferase KirCIIAuthor: Musiol-Kroll, E.M., Zubeil, F., Schafhauser, T.,Hartner, T., Kulik, A., McArthur, J., Koryakina, I., Wohlleben, W., Grond, S.,Williams, G.J., Lee, S.Y., and Weber,
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
MetabolismEnergy metabolismTCA cycledihydrolipoyllysine-residue succinyltransferase, E2 component of oxoglutarate dehydrogenase (succinyl-transferring) complex (TIGR01347; EC 2.3.1.61; HMM-score: 23.7) ...
Plasmid pUC-STS from Dr. Claudia Schmidt-dannerts lab contains the insert Stilbene synthase and is published in BMC Biotechnol. 2006 Mar 21;6:22. This plasmid is available through Addgene.
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AGPAT4; 1-acylglycerol-3-phosphate O-acyltransferase 4 (lysophosphatidic acid acyltransferase, delta); 1-acyl-sn-glycerol-3-phosphate acyltransferase delta; dJ473J16.2; LPAAT delta; 1 acyl sn glycerol 3 phosphate acyltransferase delta; 1 acylglycerol 3 phosphate O acyltransferase 4; 1 AGP acyltransferase 4; Lysophosphatidic acid acyltransferase delta; 1-AGPAT 4; 1-AGP acyltransferase 4; lysophosphatidic acid acyltransferase-delta (LPAAT-delta); 1-AGPAT4; LPAAT-delta; RP3-473J16.2; 1-AGPAT4, dJ473J16.2, LPAAT-delta, RP3-473J16.2; zgc:63605; wu:fc21c07; wu:fc25a07; fc21c07 ...
The second acylation reaction in glycerolipid biosynthesis is catalyzed by an sn-1-acylglycerol-3-phosphate acyltransferase. The enzyme of Limnanthes douglusii involved in triacylglycerol synthesis has an unusual specificity for very long chain acyl groups in both of its substrates, namely acyl-CoA and sn-1-acylglycerol-3-phosphate, and causes the enrichment of erucoyl groups in the sn-2 position of the seed oil of this plant species. We have isolated a cDNA clone encoding this embryo-specific, microsomal acyltransferase via heterologous complementation of an Escherichia coli mutant deficient in sn -1-acyl-glycerol-3-phosphate acyltransferase activity. The open reading frame of the cDNA insert encodes a protein with a length of 281 amino acids, with three predicted membrane-spanning domains and of about 31.7 kDa. The sequence exhibits substantial sequence similaritiy to the sn-1-acylglycerol-3-phosphate acyltransferase of E. coli. The corresponding transcript was detectable in developing embryos ...
We recently demonstrated that cotyledons of cotton (Gossypium hirsutum L.) seedlings synthesize N-acylphosphatidylethanolamine (NAPE), an unusual acylated derivative of phosphatidylethanolamine (PE), during postgerminative growth (K.D. Chapman and T.S. Moore [1993] Arch Biochem Biophys 301: 21-)33). Here, we report the discovery of an acyltransferase enzyme, fatty acid: diacylphosphatidylethanolamine N-acyltransferase (designated NAPE synthase), that synthesizes NAPE from PE and free fatty acids (FFA) in cottonseed microsomes. [14C]NAPE was synthesized from [14C]palmitic acid and endogenous PE in a time-, pH-, temperature-, and protein concentration-dependent manner. [14C]Palmitic acid was incorporated exclusively into the N-acyl position of NAPE. [14C]palmitoyl coenzyme A (CoA) and [14C]-dipalmitoyl phosphatidylcholine (PC) were poor acyl donors for the synthesis of NAPE (i.e. 200- and 3000-fold lower incorporation efficiency than palmitic acid, respectively). Synthesis of NAPE from ...
Chenodeoxycholoyl-CoA is bile acid Coenzyme A ester. In humans, bile acids conjugated with glycine and taurine are the major solutes in bile, and unconjugated bile acids are almost nondetectable in normal bile. Conjugated bile acids are less toxic and are more efficient promoters of intestinal absorption of dietary lipid than unconjugated bile acids. The synthesis of bile acid and amino acid conjugates in human liver is the result of two independent enzymatic reactions with a bile acid coenzyme A thioester intermediate formation of bile acid-CoA esters, considered the rate-limiting step in bile acid amidation and catalyzed by an ATP-dependent microsomal enzyme, bile acid-CoA synthetase (EC 6.2.1.7). In the second reaction, the thioester bond is cleaved, and an amide bond is formed between the bile acid and the amino acids glycine or taurine. The bile acid-CoA:amino acid N-acyltransferase (EC 2.3.1.65) catalyzes this reaction in the cytosol prior to secretion into bile. In human liver the ...
Looking for online definition of palmitoyltransferase ZDHHC2 in the Medical Dictionary? palmitoyltransferase ZDHHC2 explanation free. What is palmitoyltransferase ZDHHC2? Meaning of palmitoyltransferase ZDHHC2 medical term. What does palmitoyltransferase ZDHHC2 mean?
Article Saddle up, soybean seed pigments: argonaute5 in spatially regulated silencing of Chalcone Synthase genes. Most soybean seeds you see, whether in bins at the store, or in train cars as a commodity crop, have a yellow seed coat that may have on...
Over the past several decades, great efforts have been made to explore the molecular mechanism underlying tumorigenicity, invasion, and metastasis of HCC to identify biomarkers for prediction and to develop effective treatments. To our knowledge to date, there is evidence linking the CKAP4 gene to tumor growth in patients with bladder cancer and cervical carcinoma.[8, 9] Our recent work indicates that CKAP4 is a prognostic marker in patients with intrahepatic cholangiocellular carcinoma and is clinicopathologically associated with tumor progression and metastasis.[14] To our knowledge, systematic investigation of the prognostic significance of CKAP4 in HCC has not been reported to date, especially with long-term follow-up and a large number of patients.. In the current study, we observed that CKAP4 expression was upregulated in patients with HCC and the high level of CKAP4 correlated with a favorable prognosis. Analyzing the association between CKAP4 expression and pathological characteristics ...
N-acylphosphatidylethanolamine (NAPE) was recently shown to be synthesized in vitro in cottonseed microsomes by the direct N-acylation of phosphatidylethanolamine (PE) with unesterfied fatty acids (K.D. Chapman and T. S. Moore, 1993, Plant Physiol. 1
Agpat2 - Agpat2 (untagged ORF) - Rat 1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acid acyltransferase, beta) (Agpat2), (10 ug) available for purchase from OriGene - Your Gene Company.
en] The simplest model for the interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics involves the three following steps: (a) the formation of a reversible equimolar enzyme - antibiotic complex; (b) the irreversible transformation of this complex into a modified enzyme - antibiotic complex; and (c) the breakdown of this latter complex and the concomitant release of a regenerated enzyme and a modified antibiotic molecule. The dissociation constant for step 1 and the rate constants for steps 2 and 3 were measured with various beta-lactam antibiotics. With antibiotic such as benzylpenicillin, which behaves as a good substrate, steps 1 and 2 occur at enzymic velocities, whereas step 3 occurs at a very low velocity and hence is responsible for the low efficiency of the overall process ...
La retinolo O-acido grasso-aciltransferasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione: acil-CoA + retinolo ⇄ CoA + retinil estere Lenzima agisce sul palmitoil-CoA e su altri derivati acili grassi a lunga catena del CoA. Helgerud, P., Petersen, L.B. and Norum, K.R., Retinol esterification by microsomes from the mucosa of human small intestine. Evidence for acyl-Coenzyme A retinol acyltransferase activity, in J. Clin. Invest., vol. 71, 1983, pp. 747-753, Entrez PubMed 6826734. Ross, A.C., Retinol esterification by rat liver microsomes. Evidence for a fatty acyl coenzyme A: retinol acyltransferase, in J. Biol. Chem., vol. 257, 1982, pp. 2453-2459, Entrez PubMed 7061433 ...
1-MLCL(0:0/16:0/16:0/16:0) is a monolysocardiolipin (MLCL). Monolysocardiolipins have three fatty acid tails, instead of the usual two. 1-MLCL(0:0/16:0/16:0/16:0) contains one chain of at the C1 position, three chains of hexadecanoic acid at the C2, C3 and C4 positions. MLCL is present in eukaryotes as part of the metabolic cycle of mitochondrial lipids. Removal of one acyl chain from a cardiolipin results in generation of monolysocardiolipin (MLCL). MLCL has been used as an inter-mediate in the synthesis of spin-labeled CL to study the interaction of CL with mitochondrial enzymes. Because a role for MLCL has been suggested in apoptosis, this molecule has been used to study its interaction with various enzymes involved in lipid remodeling and apoptosis. There are two species of monolysocardiolipins, 1-MLCL which is missing a fatty acid in position R1 the and 2-MLCL which is missing a fatty acid in position R4 ...
Diacylglycerol acyltransferases (DGATs) catalyze the final and rate-limiting step of triacylglycerol (TAG) biosynthesis in eukaryotic organisms. Database search has identified at least 59 DGAT1 sequences from 48 organisms, but the expression of any DGAT1 as a full-length protein in E. coli had not been reported because DGAT1s are integral membrane proteins and difficult to express and purify. The objective of this study was to establish a procedure for expressing full-length DGAT1 in E. coli. An expression plasmid containing the open reading frame for tung tree (Vernicia fordii) DGAT1 fused to maltose binding protein and poly-histidine affinity tags was constructed and expressed in E. coli BL21(DE3). Immunoblotting showed that the recombinant DGAT1 (rDGAT1) was expressed, but mostly targeted to the membranes and insoluble fractions. Extensive degradation also occurred. Nonetheless, the fusion protein was partially purified from the soluble fraction by Ni-NTA and amylose resin affinity chromatography.
To identify DNA sequences of the Arabidopsis thaliana chalcone synthase gene (CHS) concerned with induction by UV-B and UV-A/blue light, AtCHS promoter constructions were assayed by transient expression in protoplasts prepared from two different lines of cultured A. thaliana cells. The protoplasts responded similarly to A. thaliana leaf tissue in light-dependent CHS transcript accumulation. The reporter enzyme beta-glucuronidase (GUS) was used to monitor light-responsive promoter activity. A 1972 bp promoter conferred UV-B and UV-A/blue light induction of GUS activity. Deletion to 164 bp resulted in reduced promoter strength but retention of responsiveness to UV-B and UV-A/blue light. Further deletion abolished transcriptional activity. The 164 bp promoter contains sequences closely resembling LRUPcCHS, (light-responsive unit of the Petroselinum crispum CHS promoter). This A. thaliana CHS promoter region, designated LRUAtCHS, was sufficient to confer UV-B and UV-A/blue light responsiveness to a ...
Forensic testing uses DNA sequences to identify an individual for legal purposes. Unlike the tests described above, forensic testing is not used to detect gene mutations associated with disease. This type of testing can identify crime or catastrophe victims, rule out or implicate a crime suspect, or establish biological relationships between people (for example, paternity). 42 Carnitine Palmitoyltransferase I Deficiency How Is Genetic Testing Done? Once a person decides to proceed with genetic testing, a medical geneticist, primary care doctor, specialist, or nurse practitioner can order the test. Unlike the tests described above, forensic testing is not used to detect gene mutations associated with disease. This type of testing can identify crime or catastrophe victims, rule out or implicate a crime suspect, or establish biological relationships between people (for example, paternity). 42 Carnitine Palmitoyltransferase I Deficiency How Is Genetic Testing Done? Once a person decides to proceed ...
A common active site of polyhydroxyalkanoate synthase from Bacillus cereus YB-4 is involved in polymerization and alcoholysis reactionsA common active site of polyhydroxyalkanoate synthase from Bacillus cereus YB-4 is involved in polymerization and alcoholysis reactions ...
Triacylglycerols (TAGs) and wax esters (WEs) are important neutral lipids which serve as energy reservoir in some plants and microorganisms. In recent years, these biologically produced neutral lipids have been regarded as potential alternative energy sources for biofuel production because of the increased interest on developing renewable and environmentally benign alternatives for fossil fuels. In bacteria, the final step in TAG and WE biosynthetic pathway is catalyzed by wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase (WS/DGAT). This bifunctional WS/DGAT enzyme is also a key enzyme in biotechnological production of liquid WE via engineering of plants and microorganisms. To date, knowledge about this class of biologically and biotechnologically important enzymes is mainly from biochemical characterization of WS/DGATs from Arabidopsis, jojoba and some bacteria that can synthesize both TAGs and WEs intracellularly, whereas little is known about WS/DGATs from eukaryotic
Carnitine palmitoyltransferase II deficiency (CPTII), lethal neonatal form is a rare genetic condition. It is a fatty acid oxidation disorder, which means the body cant use fats to make energy. The heart and muscles rely on fats for energy, and during times of fasting (like when we sleep), the liver and many other organs also use fats. Symptoms of this disorder begin within a few hours to a few days after birth and include seizures, trouble breathing, a weakened and enlarged heart (cardiomyopathy) and an irregular heartbeat (arrhythmia). The disease quickly progresses and can result in kidney, liver, or respiratory (breathing) failure.. CPTII is caused by a mutation (change) to the CPT2 gene. This gene provides the code to make the protein, carnitine palmitoyltransferase II (CPII). Normally, fats are broken down in our cells into their smaller parts or fatty acids. Fatty acids are then moved into the mitochondria (the part of cell where energy is made) using carnitine. Once inside the ...
Contents: Occurrence and importance of ether lipids in brain.- Introduction.- Classification of ether lipids found in brain.- Physicochemical properties of ether lipids.- Fecapentaenes, the novel plasmalogens.- Other ether lipid found in mammalian tissues.- Lipid metabolism in ether lipid-deficient mice.- Conclusion.- Biosynthesis of plasmalogens in brain.- General considerations and distribution of plasmalogens in brain.- Biosynthesis of plasmalogens.- Dihydroxyacetone phosphate acyltransferase.- Alkyl-dihydroxyacetone phosphate synthase.- Acyl/alkyl dihydroxyacetone phosphate reductase 2.2.4. Alkyl-GP acyltransferase.- Alkylacyl-GP phosphohydrolase.- CDP-ethanomamine: diacylglycerol ethanolaminephosphotransferase.- Plasmalogen synthesizing enzymes during brain development.- Topology and distribution of plasmalogen and plasmalogen synthesizing enzymes.- Plasmalogens in lipid rafts.- Plasmalogens in the nucleus.- Factors affecting plasmalogen biosynthesis in brain.- Conclusion.- Catabolism of ...
TY - JOUR. T1 - Interaction of malonyl-CoA and related compounds with mitochondria from different rat tissues. Relationship between ligand binding and inhibition of carnitine palmitoyltransferase I.. AU - Mills, S. E.. AU - Foster, D. W.. AU - McGarry, J. D.. PY - 1983/7/15. Y1 - 1983/7/15. N2 - The sensitivity of carnitine palmitoyltransferase I (CPT I; EC 2.3.1.21) to inhibition by malonyl-CoA and related compounds was examined in isolated mitochondria from liver, heart and skeletal muscle of the rat. In all three tissues the same order of inhibitory potency emerged: malonyl-CoA much greater than succinyl-CoA greater than methylmalonyl-CoA much greater than propionyl-CoA greater than acetyl-CoA. For any given agent, suppression of CPT I activity was much greater in skeletal muscle than in liver, with the heart enzyme having intermediate sensitivity. With skeletal-muscle mitochondria a high-affinity binding site for [14C]malonyl-CoA was readily demonstrable (Kd approx. 25 nM). The ability of ...

Lpcat4 - Lysophospholipid acyltransferase LPCAT4 - Mus musculus (Mouse) - Lpcat4 gene & proteinLpcat4 - Lysophospholipid acyltransferase LPCAT4 - Mus musculus (Mouse) - Lpcat4 gene & protein

In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase ... Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; ... 1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n6). 1-alkenylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.121 ... Lysophospholipid acyltransferase LPCAT4Add BLAST. 524. Amino acid modifications. Feature key. Position(s). DescriptionActions. ...
more infohttp://www.uniprot.org/uniprot/Q6NVG1

A family of eukaryotic lysophospholipid acyltransferases with broad specificityA family of eukaryotic lysophospholipid acyltransferases with broad specificity

Finally, we show that ScLPLAT differs from the specific lysophosphatidic acid acyltransferase that is encoded by SLC1 in that ... Ale1, lysophospholipid acyltransferase, LPLAT, MBOAT protein, phospholipid remodeling, Slc1, yeast, arabidopsis National ... The budding yeast ALE1 gene encodes a lysophospholipid acyltransferase (LPLAT) with broad specificity. We show that yeast LPLAT ... possess lysophospholipid acyltransferase activities similar to ScLPLAT. We propose that other members of this protein family, ...
more infohttp://uu.diva-portal.org/smash/record.jsf?pid=diva2:208527

Human Metabolome Database: Showing Protein 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (HMDBP11598)Human Metabolome Database: Showing Protein 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (HMDBP11598)

Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. May regulate the cellular storage of ... Showing Protein 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (HMDBP11598). IdentificationBiological propertiesGene ... gi,31542303,ref,NP_057090.2, 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 [Homo sapiens] ...
more infohttp://www.hmdb.ca/proteins/HMDBP11598

A Plant Acyltransferase Involved in Triacylglycerol Biosynthesis Complements an Escherichia Coli sn-1-acylglycerol-3-phosphate...A Plant Acyltransferase Involved in Triacylglycerol Biosynthesis Complements an Escherichia Coli sn-1-acylglycerol-3-phosphate...

... acylglycerol-3-phosphate acyltransferase activity which showed properties different from those of the bacterial acyltransferase ... A Plant Acyltransferase Involved in Triacylglycerol Biosynthesis Complements an Escherichia Coli sn-1-acylglycerol-3-phosphate ... The sequence exhibits substantial sequence similaritiy to the sn-1-acylglycerol-3-phosphate acyltransferase of E. coli. The ... Bin Yu, Setsuko Wakao, Jilian Fan, Christoph Benning, Loss of Plastidic Lysophosphatidic Acid Acyltransferase Causes Embryo- ...
more infohttp://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1995.806zz.x/abstract

Lysophosphatidylcholine acyltransferase 1 is downregulated by hepatitis C virus: impact on production of lipo-viro-particles |...Lysophosphatidylcholine acyltransferase 1 is downregulated by hepatitis C virus: impact on production of lipo-viro-particles |...

Lysophosphatidylcholine acyltransferase 1 is downregulated by hepatitis C virus: impact on production of lipo-viro-particles ... Lysophosphatidylcholine acyltransferase 1 is downregulated by hepatitis C virus: impact on production of lipo-viro-particles ... The recent identification of lysophosphatidylcholine acyltransferase 1 (LPCAT1) as an LD phospholipid-remodelling enzyme ...
more infohttp://gut.bmj.com/content/early/2016/08/31/gutjnl-2016-311508

Lysophosphatidylcholine Acyltransferase 1 (LPCAT1) Specifically Interacts with Phospholipid Transfer Protein StarD10 to...Lysophosphatidylcholine Acyltransferase 1 (LPCAT1) Specifically Interacts with Phospholipid Transfer Protein StarD10 to...

lyso-PC acyltransferase 1. ER. endoplasmic reticulum. LB. lamellar body. START. steroidogenic acute regulatory protein-related ... 5B). Because amino acids 79-271 of LPCAT1 contains the acyltransferase domain spanning amino acids 114-239, a construct ... Soupene E., Fyrst H., Kuypers F. A. (2008) Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes. Proc. Natl. Acad ... Lysophosphatidylcholine Acyltransferase 1 (LPCAT1) Specifically Interacts with Phospholipid Transfer Protein StarD10 to ...
more infohttp://pubmedcentralcanada.ca/pmcc/articles/PMC4513115/

agpat4, 1-acylglycerol-3-phosphate O-acyltransferase 4 - Creative Biogeneagpat4, 1-acylglycerol-3-phosphate O-acyltransferase 4 - Creative Biogene

1 AGP acyltransferase 4; Lysophosphatidic acid acyltransferase delta; 1-AGPAT 4; 1-AGP acyltransferase 4; lysophosphatidic acid ... AGPAT4; 1-acylglycerol-3-phosphate O-acyltransferase 4 (lysophosphatidic acid acyltransferase, delta); 1-acyl-sn-glycerol-3- ... phosphate acyltransferase delta; dJ473J16.2; LPAAT delta; 1 acyl sn glycerol 3 phosphate acyltransferase delta; 1 acylglycerol ... This gene encodes a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. This integral membrane protein converts ...
more infohttps://www.creative-biogene.com/symbolsearch_agpat4.html

Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse...Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse...

Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse reactions ... Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine (PC ... View full text: Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward ... [email protected]: Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and ...
more infohttp://nparc.nrc-cnrc.gc.ca/eng/view/object/?id=4673c77e-e816-4d49-adc9-511e33e07af1

Mice deleted for GPAT3 have reduced GPAT activity in white adipose tissue and altered energy and cholesterol homeostasis in...Mice deleted for GPAT3 have reduced GPAT activity in white adipose tissue and altered energy and cholesterol homeostasis in...

Identification of a novel sn-glycerol-3-phosphate acyltransferase isoform, GPAT4, as the enzyme deficient in Agpat6−/− mice. J ... Glycerol-3-phosphate acyltransferases: rate limiting enzymes of triacylglycerol biosynthesis. Biochim Biophys Acta 1791: 501- ... 1A). This strategy deletes the majority of the acyltransferase domain of GPAT3 and introduces a frame-shift mutation after aa ... GPAT, acyl-CoA:glycerol-3-phosphate acyltransferase. A: strategy for generating Gpat3 knockout (KO) mice. Part of the murine ...
more infohttp://ajpendo.physiology.org/content/306/10/E1176.long

Dr Wondwossen Abate Woldie - University of PlymouthDr Wondwossen Abate Woldie - University of Plymouth

4. Alrammah H, Abate, W., Avent, N.,Jackson, S. K. (2015) Overexpression of lysophosphatidylcholine acyltransferase 2 (LPCAT2) ... S.K. Jackson, W. Abate and A.J. Tonks (2008) Lysophospholipid acyltransferases: Novel potential regulators of theinflammatory ... 1. Abate W andJackson SK (2015). Lysophosphatidylcholine Acyltransferase (LPCAT)- 2 Co-localises withTLR4 and Regulates ...
more infohttps://www.plymouth.ac.uk/staff/wondwossen-abate-woldie

Wax ester biosynthetic pathway by Daolin Cheng"Wax ester biosynthetic pathway" by Daolin Cheng

Two of them exist in plans; the jojoba-like wax synthase (WS), and the bifunctional wax synthase/diacylglycerol acyl ...
more infohttps://lib.dr.iastate.edu/etd/13529/

Acyltransferase - WikipediaAcyltransferase - Wikipedia

Glyceronephosphate O-acyltransferase Lecithin-cholesterol acyltransferase Long-chain-alcohol O-fatty-acyltransferase ... Acyltransferase is a type of transferase enzyme that acts upon acyl groups. Examples include: ... Acetyltransferase Acyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and ...
more infohttps://en.wikipedia.org/wiki/Acyltransferase

Palmitoyl acyltransferase - WikipediaPalmitoyl acyltransferase - Wikipedia

Palmitoyl acyltransferase is a group of enzymes that transfer palmityl group to -SH group on cysteine on a protein. This ... The palmitoyl acyltransferase was isolated and identified in 1999. The catalytic domain of the protein has aspartate-histidine- ... Draper, J. M.; Smith, C. D. (2009). "Palmitoyl acyltransferase assays and inhibitors (Review)". Molecular Membrane Biology. 26 ...
more infohttps://en.wikipedia.org/wiki/Palmitoyl_acyltransferase

Diglyceride acyltransferase - WikipediaDiglyceride acyltransferase - Wikipedia

Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... cholesterol acyltransferase-related enzymes". The Journal of Biological Chemistry. 273 (41): 26765-71. doi:10.1074/jbc.273.41. ... a second mammalian diacylglycerol acyltransferase, and related family members". The Journal of Biological Chemistry. 276 (42): ... "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the ...
more infohttps://en.wikipedia.org/wiki/Diglyceride_acyltransferase

Lecithin cholesterol acyltransferase deficiency - WikipediaLecithin cholesterol acyltransferase deficiency - Wikipedia

Lecithin cholesterol acyltransferase deficiency (LCAT deficiency) is a disorder of lipoprotein metabolism. The disease has two ... Lecithin cholesterol acyltransferase catalyzes the formation of cholesterol esters in lipoproteins. Symptoms of the familial ... "Lecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential Diagnosis". 2016-08-08. Kuivenhoven, J. A ... "Lecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential Diagnosis". 2016-08-08. Reference, ...
more infohttps://en.wikipedia.org/wiki/Lecithin_cholesterol_acyltransferase_deficiency

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase - WikipediaUDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase - Wikipedia

... glucosamine N-acyltransferase, acyltransferase LpxD, acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase, firA (gene), lpxD ... UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC 2.3.1.191, UDP-3-O-acyl-glucosamine N-acyltransferase, UDP-3-O-(R ... Buetow, L.; Smith, T.K.; Dawson, A.; Fyffe, S.; Hunter, W.N. (2007). "Structure and reactivity of LpxD, the N-acyltransferase ... Bartling, C.M.; Raetz, C.R. (2008). "Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis ...
more infohttps://en.wikipedia.org/wiki/UDP-3-O-(3-hydroxymyristoyl)glucosamine_N-acyltransferase

Diglyceride acyltransferase - WikipediaDiglyceride acyltransferase - Wikipedia

Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... cholesterol acyltransferase-related enzymes". The Journal of Biological Chemistry. 273 (41): 26765-71. doi:10.1074/jbc.273.41. ... a second mammalian diacylglycerol acyltransferase, and related family members". The Journal of Biological Chemistry. 276 (42): ... "Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the ...
more infohttps://en.m.wikipedia.org/wiki/Dgat1

Dihydroxyacetone phosphate acyltransferase definition | Drugs.comDihydroxyacetone phosphate acyltransferase definition | Drugs.com

Definition of dihydroxyacetone phosphate acyltransferase. Provided by Stedmans medical dictionary and Drugs.com. Includes ... dihydroxyacetone phosphate acyltransferase. Definition: an enzyme that catalyzes an important step in plasmalogen biosynthesis ...
more infohttps://www.drugs.com/dict/dihydroxyacetone-phosphate-acyltransferase.html

MULTISPECIES: lauroyl acyltransferase [Leptospira] - Protein - NCBIMULTISPECIES: lauroyl acyltransferase [Leptospira] - Protein - NCBI

MULTISPECIES: lauroyl acyltransferase [Leptospira] MULTISPECIES: lauroyl acyltransferase [Leptospira]. gi,488619399,ref,WP_ ...
more infohttps://www.ncbi.nlm.nih.gov/protein/WP_002556247

Acyltransferase, C-terminal domain (IPR032098) | InterPro | EMBL-EBIAcyltransferase, C-terminal domain (IPR032098) | InterPro | EMBL-EBI

The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic ... lysophosphatidylglycerol acyltransferase 1, and lysocardiolipin acyltransferase 1, which has both lysophosphatidylinositol and ... including 1-acyl-sn-glycerol-3-phosphate acyltransferase (also known as lysophosphatidic acid acyltransferase), acyl-CoA: ... This domain is found at the C terminus of several lysophospholipid acyltransferases, ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR032098

Acyltransferases - TransferasesAcyltransferases - Transferases

To place an order online, simply browse to the product you are interested in and click on the Add to Cart button. To complete this process, you will need to confirm the size and quantity of the products that you require. To complete an order you will need to register using our simple online registration process. We do not share your contact details with any third parties.. When you are ready to check out simply enter your PO number to complete the ordering process. Please ensure that you send us a copy of your PO by fax or email afterwards. We will then liaise with you or your purchasing department to confirm the order.. ...
more infohttp://www.adooq.com/acyltransferases.html

1-acylglycerol-3-phosphate acyltransferase definition | Drugs.com1-acylglycerol-3-phosphate acyltransferase definition | Drugs.com

Definition of 1-acylglycerol-3-phosphate acyltransferase. Provided by Stedmans medical dictionary and Drugs.com. Includes ... See: lysophosphatidic acid acyltransferase. Further information. Always consult your healthcare provider to ensure the ...
more infohttps://www.drugs.com/dict/1-acylglycerol-3-phosphate-acyltransferase.html

Lecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential DiagnosisLecithin-Cholesterol Acyltransferase Deficiency: Overview, Presentation, Differential Diagnosis

The two familial forms of lecithin-cholesterol acyltransferase (LCAT) deficiency are termed familial LCAT deficiency (complete ... encoded search term (Lecithin-Cholesterol Acyltransferase Deficiency) and Lecithin-Cholesterol Acyltransferase Deficiency What ... Lecithin-Cholesterol Acyltransferase Deficiency. Updated: Aug 08, 2016 * Author: Catherine Anastasopoulou, MD, PhD, FACE; Chief ... Lecithin-cholesterol acyltransferase (LCAT) is a lipoprotein-associated enzyme which plays a large role in the esterification ...
more infohttps://emedicine.medscape.com/article/122958-overview

Acyl transferase/acyl hydrolase/lysophospholipase (IPR016035) | InterPro | EMBL-EBIAcyl transferase/acyl hydrolase/lysophospholipase (IPR016035) | InterPro | EMBL-EBI

Acyl transferase/acyl hydrolase/lysophospholipase (IPR016035). Short name: Acyl_Trfase/lysoPLipase Description. This ... This domain can be found in acyl transferases such as bacterial malonyl-CoA ACP transacylase (FabD) and the homologous domain ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR016035
  • In this work, we present the structure of the bacterial LPLAT protein LpxM, and we describe a high-throughput, label-free mass spectrometric assay to characterize acyltransferase enzymatic activity. (pnas.org)
  • This work enables the interrogation of other bacterial acyltransferases' structure-mechanism relationships, and the assay described herein provides a foundation for quantitatively characterizing the enzymology of any number of clinically relevant LPLAT proteins. (pnas.org)
  • Glycerol 3-phosphate, derived primarily from glycolysis or gluconeogenesis, is esterified at the sn -1 carbon position by glycerol 3-phosphate acyltransferases producing lysophosphatidate (1-acylglycerol 3-phosphate). (aocs.org)