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.Protein S: The vitamin K-dependent cofactor of activated PROTEIN C. Together with protein C, it inhibits the action of factors VIIIa and Va. A deficiency in protein S; (PROTEIN S DEFICIENCY); can lead to recurrent venous and arterial thrombosis.Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Fatty Acid Synthase, Type II: The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.3-Oxoacyl-(Acyl-Carrier-Protein) Synthase: An enzyme of long-chain fatty acid synthesis, that adds a two-carbon unit from malonyl-(acyl carrier protein) to another molecule of fatty acyl-(acyl carrier protein), giving a beta-ketoacyl-(acyl carrier protein) with the release of carbon dioxide. EC 2.3.1.41.Polyketide Synthases: Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.Acyl-Carrier Protein S-Malonyltransferase: This enzyme catalyzes the transacylation of malonate from MALONYL CoA to activated holo-ACP, to generate malonyl-(acyl-carrier protein), which is an elongation substrate in FATTY ACIDS biosynthesis. It is an essential enzyme in the biosynthesis of FATTY ACIDS in all BACTERIA.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.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Transferases (Other Substituted Phosphate Groups): A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.3-Oxoacyl-(Acyl-Carrier-Protein) Reductase: A 3-oxoacyl reductase that has specificity for ACYL CARRIER PROTEIN-derived FATTY ACIDS.Coenzyme AEscherichia 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.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.Pantothenic Acid: A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Protein S Deficiency: An autosomal dominant disorder showing decreased levels of plasma protein S antigen or activity, associated with venous thrombosis and pulmonary embolism. PROTEIN S is a vitamin K-dependent plasma protein that inhibits blood clotting by serving as a cofactor for activated PROTEIN C (also a vitamin K-dependent protein), and the clinical manifestations of its deficiency are virtually identical to those of protein C deficiency. Treatment with heparin for acute thrombotic processes is usually followed by maintenance administration of coumarin drugs for the prevention of recurrent thrombosis. (From Harrison's Principles of Internal Medicine, 12th ed, p1511; Wintrobe's Clinical Hematology, 9th ed, p1523)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.Enoyl-(Acyl-Carrier-Protein) Reductase (NADH): An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.Carbon-Sulfur Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. EC 6.2.Ribosomal Protein S6: A ribosomal protein that may play a role in controlling cell growth and proliferation. It is a major substrate of RIBOSOMAL PROTEIN S6 KINASES and plays a role in regulating the translation (TRANSLATION, GENETIC) of RNAs that contain an RNA 5' TERMINAL OLIGOPYRIMIDINE SEQUENCE.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)Acylation: The addition of an organic acid radical into a molecule.Thiolester HydrolasesMalonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.Bacterial Proteins: Proteins found in any species of bacterium.Triclosan: A diphenyl ether derivative used in cosmetics and toilet soaps as an antiseptic. It has some bacteriostatic and fungistatic action.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.Choline O-Acetyltransferase: An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC 2.3.1.6.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 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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Streptomyces: A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.Acetyl Coenzyme A: Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.Ribosomal Proteins: Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.Cerulenin: An epoxydodecadienamide isolated from several species, including ACREMONIUM, Acrocylindrum, and Helicoceras. It inhibits the biosynthesis of several lipids by interfering with enzyme function.Saccharopolyspora: A genus of gram-positive bacteria whose spores are round to oval and covered by a sheath.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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.Apoproteins: The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).Chloramphenicol O-Acetyltransferase: An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28.Kinetics: The rate dynamics in chemical or physical systems.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Anthraquinones: Compounds based on ANTHRACENES which contain two KETONES in any position. Substitutions can be in any position except on the ketone groups.Acyl-Carrier Protein S-Acetyltransferase: A enzyme that catalyzes the transfer of acetyl groups from ACETYL CoA to acyl-carrier protein to form COENZYME A and acetyl-acyl-carrier protein.Coriandrum: A plant genus of the family APIACEAE. The leaves are the source of cilantro and the seeds are the source of coriander, both of which are used in SPICES.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Thioctic Acid: An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.MalonatesMutation: 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.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Lipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)Naphthacenes: Polyacenes with four ortho-fused benzene rings in a straight linear arrangement. This group is best known for the subclass called TETRACYCLINES.p300-CBP Transcription Factors: A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.Peptide Synthases: Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Genes, Bacterial: The functional hereditary units of BACTERIA.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.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Protein C: A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation.Vibrio: A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle.Carrier State: The condition of harboring an infective organism without manifesting symptoms of infection. The organism must be readily transmissible to another susceptible host.Serine O-Acetyltransferase: An enzyme that catalyzes the conversion of L-SERINE to COENZYME A and O-acetyl-L-serine, using ACETYL-COA as a donor.Nuclear Magnetic Resonance, Biomolecular: NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Sulfhydryl Compounds: Compounds containing the -SH radical.N-Terminal Acetyltransferase A: An N-terminal acetyltransferase subtype that consists of the Naa10p catalytic subunit and the Naa15p auxiliary subunit. The structure of this enzyme is conserved between lower and higher eukaryotes. It has specificity for N-terminal SERINE; ALANINE; THREONINE; GLYCINE; VALINE; and CYSTINE residues and acts on nascent peptide chains after the removal of the initiator METHIONINE by METHIONYL AMINOPEPTIDASES.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Macrolides: A group of often glycosylated macrocyclic compounds formed by chain extension of multiple PROPIONATES cyclized into a large (typically 12, 14, or 16)-membered lactone. Macrolides belong to the POLYKETIDES class of natural products, and many members exhibit ANTIBIOTIC properties.Mycolic AcidsN-Terminal Acetyltransferase E: An N-terminal acetyltransferase subtype that consists of the Naa50p catalytic subunit, and the Naa10p and Naa15p auxiliary subunits. It has specificity for the N-terminal METHIONINE of peptides where the next amino acid in the chain is hydrophobic.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Complement Inactivator Proteins: Serum proteins that negatively regulate the cascade process of COMPLEMENT ACTIVATION. Uncontrolled complement activation and resulting cell lysis is potentially dangerous for the host. The complement system is tightly regulated by inactivators that accelerate the decay of intermediates and certain cell surface receptors.Polyketides: Natural compounds containing alternating carbonyl and methylene groups (beta-polyketones), bioenergenetically derived from repeated condensation of acetyl coenzyme A via malonyl coenzyme A, in a process similar to fatty acid synthesis.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.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).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.Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Molecular Weight: The sum of the weight of all the atoms in a molecule.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Ribosomal Protein S6 Kinases: A family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.Hydro-Lyases: Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Brassica: A plant genus of the family Cruciferae. It contains many species and cultivars used as food including cabbage, cauliflower, broccoli, Brussel sprouts, kale, collard greens, MUSTARD PLANT; (B. alba, B. junica, and B. nigra), turnips (BRASSICA NAPUS) and rapeseed (BRASSICA RAPA).Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Glycerophosphates: Any salt or ester of glycerophosphoric acid.EstersMass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.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.Chloroplasts: Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Acetyl-CoA C-Acetyltransferase: An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.Streptomyces coelicolor: A soil-dwelling actinomycete with a complex lifecycle involving mycelial growth and spore formation. It is involved in the production of a number of medically important ANTIBIOTICS.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.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.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.

Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. (1/8)

Polyketides are a class of natural products that exhibit a wide range of functional and structural diversity. They include antibiotics, immunosuppressants, antifungals, antihypercholesterolemics, and cytotoxins. Polyketide synthases (PKSs) use chemistry similar to fatty acid synthases (FASs), although building block variation and differing extents of reduction of the growing polyketide chain underlie their biosynthetic versatility. In contrast to the well studied sequential modular type I PKSs, less is known about how the iterative type I PKSs carry out and control chain initiation, elongation, folding, and cyclization during polyketide processing. Domain structure analysis of a group of related fungal, nonreducing PKSs has revealed well defined N-terminal domains longer than commonly seen for FASs and modular PKSs. Predicted structure of this domain disclosed a region similar to malonyl-CoA:acyl-carrier protein (ACP) transacylases (MATs). MATs play a key role transferring precursor CoA thioesters from solution onto FASs and PKSs for chain elongation. On the basis of site-directed mutagenesis, radiolabeling, and kinetics experiments carried out with individual domains of the norsolorinic acid PKS, we propose that the N-terminal domain is a starter unit:ACP transacylase (SAT domain) that selects a C(6) fatty acid from a dedicated yeast-like FAS and transfers this unit onto the PKS ACP, leading to the production of the aflatoxin precursor, norsolorinic acid. These findings could indicate a much broader role for SAT domains in starter unit selection among nonreducing iterative, fungal PKSs, and they provide a biochemical rationale for the classical acetyl "starter unit effect."  (+info)

De novo fatty acid synthesis mediated by acyl-carrier protein in Neurospora crassa mitochondria. (2/8)

The acyl-carrier protein (ACP) in Neurospora crassa mitochondria [Brody, S. & Mikolajczyk, S. (1988) Eur. J. Biochem. 173, 353-359] mediated a cerulenin-sensitive, de novo fatty acid synthesis independent of the fatty acid synthetase complex present in the cytoplasm. Incubation of mitochondria with [2-14C]malonate labeled only the ACP as indicated by autoradiography after SDS/PAGE. Under these in vitro conditions ATP was required for the initial acyl-ACP formation, but further elongation required either magnesium or the direct addition of NADPH. Labeled hexanoic (6:0) and caprylic (8:0) acids were detected as intermediates in the pathway, as well as hydroxymyristic acid. All of the intermediates, and the eventual product of the reaction, myristic acid (14:0), were released from the ACP by alkaline treatment. Pulse-chase experiments demonstrated the incorporation on to, and release of label from, the ACP. In vivo labeling of ACP with [2-14C]malonate was also detected and the label was in the form of hydroxymyristic acid. This newly discovered pathway is discussed from the standpoint of its possible role in providing acyl chains for mitochondrial lipids.  (+info)

Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. (3/8)

A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows the production of small amounts of homogeneous enzyme. The subunit Mr was estimated to be 29,000 and the native Mr was estimated to be 61,000, suggesting a homodimeric structure. The catalytic properties of the enzyme are consistent with a Bi Bi Ping Pong mechanism and the existence of an acetyl-enzyme intermediate in the catalytic cycle. The enzyme was inhibited by N-ethylmaleimide and more slowly by iodoacetamide in reactions protected by the substrate, acetyl-CoA. However, the enzyme was apparently only weakly inhibited by the thiol-specific reagent methyl methanethiosulphonate. The nature of the acetyl-enzyme intermediate is discussed in relationship to that found in other similar enzymes from E. coli, yeast and vertebrates.  (+info)

Effect of thiolactomycin on the individual enzymes of the fatty acid synthase system in Escherichia coli. (4/8)

Thiolactomycin, an antibiotic with the structure of (4S)-(2E,5E)-2,4,6-trimethyl-3-hydroxy-2,5,7-octatriene-4-++ +thiolide, selectively inhibits type II fatty acid synthases. The mode of the thiolactomycin action on the fatty acid synthase system of Escherichia coli was investigated. Of the six individual enzymes of the fatty acid synthase system, [acyl-carrier-protein] (ACP) acetyltransferase and 3-oxoacyl-ACP synthase were inhibited by thiolactomycin. On the other hand, the other enzymes were not affected by this antibiotic. The thiolactomycin inhibition of the fatty acid synthase system was reversible. As to ACP acetyltransferase, the inhibition was competitive with respect to ACP and uncompetitive with respect to acetyl-CoA. As to 3-oxoacyl-ACP synthase, the inhibition was competitive with respect to malonyl-ACP and noncompetitive with respect to acetyl-ACP. The thiolactomycin action on the fatty acid synthase system was compared with that of cerulenin.  (+info)

Characterization of the fatty acid synthetase system of Curtobacterium pusillum. (5/8)

Curtobacterium pusillum contains 11-cyclohexylundecanoic acid as a major component of cellular fatty acids. A trace amount of 13-cyclohexyltridecanoic acid is also present. Fatty acids other than omega-cyclohexyl fatty acids present are 13-methyltetradecanoic, 12-methyltetradecanoic, n-pentadecanoic, 14-methylpentadecanoic, 13-methylpentadecanoic, n-hexadecanoic, 15-methylhexadecanoic, 14-methylhexadecanoic, and n-heptadecanoic acids. The fatty acid synthetase system of this bacterium was studied. Various 14C-labeled precursors were added to the growth medium and the incorporation of radioactivity into cellular fatty acids was analyzed. Sodium [14C]acetate and [14C]glucose were incorporated into almost all species of cellular fatty acids, the incorporation into 11-cyclohexylundecanoic acid being predominant. [14C]Isoleucine was incorporated into 12-methyltetradecanoic and 14-methylhexadecanoic acids: [14C]leucine into 13-methyltetradecanoic and 15-methylhexadecanoic acids; and [14C]valine into 14-methylpentadecanoic acid. [14C]-Shikimic acid was incorporated almost exclusively into omega-cyclohexyl fatty acids. The fatty acid synthetase activity of the crude enzyme preparation of C. pusillum was reconstituted on the addition of acyl carrier protein. This synthetase system required NADPH and preferentially utilized cyclohexanecarbonyl-CoA as a primer. The system was also able to use branched- and straight-chain acyl-CoAs with 4 to 6 carbon atoms effectively as primers but was unable to use acetyl-CoA. However, if acetyl acyl carrier protein was used as the priming substrate, the system produced straight-chain fatty acids. The results imply that the specificity of the initial acyl-CoA:acyl carrier protein acyltransferase dictates the structure of fatty acids synthesized and that the enzymes catalyzing the subsequent chain-elongation reactions do not have the same specificity restriction.  (+info)

Biochemical and genetic characterization of an auxotroph of Bacillus subtilis altered in the Acyl-CoA:acyl-carrier-protein transacylase. (6/8)

We have analyzed a mutation of Bacillus subtilis (bfmB) that results in an acyl-CoA:acyl-carrier-protein transacylase with low affinity for branched acyl-CoA substrates; it maps in the acf-hisH region of the chromosome. The aceA mutation, present in the parent of the bfmB mutant, causes a deficiency in pyruvate dehydrogenase and maps in the pycA-pyrA region. Strains carrying the bfmB mutation synthesize branched-chain fatty acids at a rate sufficient for normal growth only if branched acyl-CoA precursors are present in the medium. They grow well if the medium is supplemented with 0.1 mM 2-methylbutyrate, isobutyrate or isovalerate, or with 1.0 mM isoleucine or valine; leucine does not support growth. Growth supported by valine and isoleucine is inhibited by butyrate and other straight short-chain fatty acids at concentrations (0.1 mM) which do not inhibit growth of the standard strain; the inhibition is prevented by short branched fatty acids which are converted to long-chain fatty acids appearing as activity of B. subtilis is controlled by separate enzymatic sites for the acyl-CoA precursors of branched and straight-chain fatty acids. Whether these sites are contained in one or two enzymes is not known.  (+info)

The purification and function of acetyl coenzyme A:acyl carrier protein transacylase. (7/8)

When individual enzyme activities of the fatty acid synthetase (FAS) system were assayed in extracts from five different plant tissues, acetyl-CoA:acyl carrier protein (ACP) transacylase and beta-ketoacyl-ACP synthetases I and II had consistently low specific activities in comparison with the other enzymes of the system. However, two of these extracts synthesized significant levels of medium chain fatty acids (rather than C16 and C18 acid) from [14C]malonyl-CoA; these extracts had elevated levels of acetyl-CoA:ACP transacylase. To explore the role of the acetyl transacylase more carefully, this enzyme was purified some 180-fold from spinach leaf extracts. Varying concentrations of the transacylase were then added either to spinach leaf extracts or to a completely reconstituted FAS system consisting of highly purified enzymes. The results suggested that: (a) acetyl-CoA:ACP transacylase was the enzyme catalyzing the rate-limiting step in the plant FAS system; (b) increasing concentration of this enzyme markedly increased the levels of the medium chain fatty acids, whereas increase of the other enzymes of the FAS system led to increased levels of stearic acid synthesis; and (c) beta-ketoacyl-ACP synthetase I was not involved in the rate-limiting step. It is suggested that modulation of the activity of acetyl-CoA:ACP transacylase may have important implications in the type of fatty acid synthesized, as well as the amount of fatty acids formed.  (+info)

Beta-lactams SB 212047 and SB 216754 are irreversible, time-dependent inhibitors of coenzyme A-independent transacylase. (8/8)

The enzyme coenzyme A-independent transacylase (CoA-IT) has been demonstrated to be the key mediator of arachidonate remodeling, a process that moves arachidonate into 1-ether-containing phospholipids. Blockade of CoA-IT by reversible inhibitors has been shown to block the release of arachidonate in stimulated neutrophils and inhibit the production of eicosanoids and platelet-activating factor. We describe novel inhibitors of CoA-IT activity that contain a beta-lactam nucleus. beta-Lactams were investigated as potential mechanism-based inhibitors of CoA-IT on the basis of the expected formation of an acyl-enzyme intermediate complex. Two beta-lactams, SB 212047 and SB 216754, were shown to be specific, time-dependent inhibitors of CoA-IT activity (IC50 = 6 and 20 microM, respectively, with a 10-min pretreatment time). Extensive washing and dilution could not remove the inhibition, suggesting it was irreversible. In stimulated human monocytes, SB 216754 decreased the production of eicosanoids in a time-dependent manner. In an in vivo model of phorbol ester-induced ear inflammation, SB 216754 was able to inhibit indices of both edema and cell infiltration. Taken together, the results support two hypotheses: 1) CoA-IT activity is important for the production of inflammatory lipid mediators in stimulated cells and in vivo and 2) the mechanism by which CoA-IT acts to transfer arachidonate is through an acyl-enzyme intermediate.  (+info)

B-Specific) Enoyl-(Acyl-Carrier Protein) Reductase (NADPH: An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the fatty acid biosynthesis pathway. It has a preference for acyl derivatives with carbon chain length from 4 to 16.
The citrate lyase activation starts with a 3-dephospho-CoA reacting with ATP and a hydrogen ion through a triphosphoribosyl-dephospho-CoA synthase resulting in a adenine and a 2-(5-triphospho-alpha-D-ribosyl)-3-dephospho-CoA. The latter compound in turn reacts with with a citrate lyase acyl-carrier protein through a apo-citrate lyase phosphoribosyl-dephospho-CoA transferase resulting in the release of a pyrophosphate and a hydrogen ion and a holo citrate lyase acyl-carrier protein.This protein complex can either react with a hydrogen ion and a acetate resulting in the release of a water and an acetyl-holo citrate lyase acyl-carrier protein. The holo acyl-carrier protein creacts with an ATP and an acetate through a citrate lyase synthase resulting in the release of an AMP, a pyrophosphate and an acetyl-holo citrate lyase acyl-ccarrier protein. The holo citrate lyase acyl-carrier protein can also interact with an S-acetyl phosphopantethiene resulting in the release of a 4-phosphopantethiene and ...
Accepted name: oleoyl-[acyl-carrier-protein] hydrolase. Reaction: an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate. Other name(s): acyl-[acyl-carrier-protein] hydrolase; acyl-ACP-hydrolase; acyl-acyl carrier protein hydrolase; oleoyl-ACP thioesterase; oleoyl-acyl carrier protein thioesterase. Systematic name: oleoyl-[acyl-carrier protein] hydrolase. Comments: Acts on acyl-carrier-protein thioesters of fatty acids from C12 to C18, but the derivative of oleic acid is hydrolysed much more rapidly than any other compound tested.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 68009-83-6. References:. 1. Ohlrogge, J.B., Shine, W.E. and Stumpf, P.K. Fat metabolism in higher plants. Characterization of plant acyl-ACP and acyl-CoA hydrolases. Arch. Biochem. Biophys. 189 (1978) 382-391. [PMID: 30409]. 2. Shine, W.E., Mancha, M. and Stumpf, P.K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of ...
Accepted name: trans-2-decenoyl-[acyl-carrier protein] isomerase. Reaction: a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein]. Other name(s): β-hydroxydecanoyl thioester dehydrase; trans-2-cis-3-decenoyl-ACP isomerase; trans-2,cis-3-decenoyl-ACP isomerase; trans-2-decenoyl-ACP isomerase; FabM. Systematic name: decenoyl-[acyl-carrier protein] Δ2-trans-Δ3-cis-isomerase. Comments: While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs [3]. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-80-2. References:. 1. Brock, ...
The synthesis of lipids and acyl thioesters was studied in microsomal preparations from germinating pea (Pisum sativum cv. Feltham First) seeds. Under conditions of maximal synthesis (in the presence of exogenous acyl-carrier protein) acyl-acyl-carrier proteins accounted for about half the total incorporation from [14C]malonyl-CoA. Decreasing the concentrations of exogenous acyl-carrier protein lowered the overall synthesis of fatty acids by decreasing, almost exclusively, the radioactivity associated with acyl-acyl-carrier proteins. A time-course experiment showed that acyl-acyl-carrier proteins accumulated most of the radioactive label at the beginning of the incubation but, eventually, the amount of radioactivity in that fraction decreased, while a simultaneous increase in the acyl-CoA and lipid fractions was noticed. Addition of exogenous CoA (1 mM) produced a decrease of total incorporation, but an increase in the radioactivity incorporated into acyl-CoA. The microsomal preparations ...
The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Eicosanoyl-CoA + 4 Methylmalonyl-CoA + 8 NADPH + 8 H+ + Acyl-carrier protein ,=, C32-Mycocerosyl-[acp] + 5 CoA + 4 CO2 + 8 NADP+ + 4 ...
Abstract: The enoyl acyl-carrier protein reductase (ENR) enzyme of the apicomplexan parasite family has been intensely studied for antiparasitic drug design for over a decade, with the most potent inhibitors targeting the NAD+ bound form of the enzyme. However, the higher affinity for the NADH co-factor over NAD+ and its availability in the natural environment makes the NADH complex form of ENR an attractive target. Herein, we have examined a benzimidazole family of inhibitors which target the NADH form of Francisella ENR, but despite good efficacy against Toxoplasma gondii, the IC50 for T. gondii ENR is poor, with no inhibitory activity at 1 μM. Moreover similar benzimidazole scaffolds are potent against fungi which lack the ENR enzyme and as such we believe that there may be significant off target effects for this family of inhibitors ...
Complete information for DLAT gene (Protein Coding), Dihydrolipoamide S-Acetyltransferase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for DLAT gene (Protein Coding), Dihydrolipoamide S-Acetyltransferase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
DLAT antibody (dihydrolipoamide S-acetyltransferase) for ICC/IF, IHC-P, WB. Anti-DLAT pAb (GTX109766) is tested in Human samples. 100% Ab-Assurance.
Malonyl-CoA:acyl-carrier protein transacylase (MCAT), encoded by the fabd gene, is a key enzyme in type II fatty-acid biosynthesis. It is responsible for transferring the malonyl group from malonyl-CoA to the holo acyl-carrier protein (ACP). Since the type II system differs from the type I system that mammals use, it has received enormous attention as a possible antibiotic target. In particular, only a single isoform of MCAT has been reported and a continuous coupled enzyme assay has been developed. MCAT from Staphylococcus aureus was overexpressed in Escherichia coli and the protein was purified and crystallized. Diffraction data were collected to 1.2 A ° resolution. The crystals belonged to space group P21, with unit-cell parameters a = 41.608, b = 86.717, c = 43.163 A ° , α = γ = 90, β = 106.330 °. The asymmetric unit contains one SaMCAT molecule ...
Essential role in the production of HC-toxin and in pathogenicity of the fungus on maize. May contribute to the synthesis of the decanoic backbone of 2-amino-9,10-epoxi-8-oxodecanoic acid. This protein contains domains similar to those of a fatty acid synthase beta subunit, namely: [acyl-carrier protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.
Hordeum pusillum is a small annual grass with a rachis that falls apart when mature. The glumes of the central spikelet and the inner glumes of the outer spikelets widen above the base. Like all Hordeums, the spikelets are borne in threes. The awns are less than a centimeter long. The auricles are under 1mm in length. Hordeum pusillum is found in disturbed ground in town ...
WoRMS (2015). Anisonema pusillum Stokes, 1888. In: Guiry, M.D. & Guiry, G.M. (2017). AlgaeBase. World-wide electronic publication, National University of Ireland, Galway (taxonomic information republished from AlgaeBase with permission of M.D. Guiry). Accessed through: World Register of Marine Species at http://marinespecies.org/aphia.php?p=taxdetails&id=163252 on 2017-12- ...
Discover Lifes page about the biology, natural history, ecology, identification and distribution of Arceuthobium pusillum image
casSAR Dugability of Q8RFU2 | lpxA | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase - Also known as LPXA_FUSNN, lpxA. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Homotrimer.
Buy fabZ recombinant protein, (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase (fabZ) Recombinant Protein-YP_145081.1 (MBS1409712) product datasheet at MyBioSource, Recombinant Proteins
Pantethine, a highly absorbable and biologically active form of pantothenic acid (Vitamin B-5), is the reactive component of Coenzyme A (CoA) and the acyl-carrier protein (ACP). CoA and ACP are extensively involved in the metabolism of carbohydrates, lipids and amino acids. Numerous clinical and nonclinical studies suggest that pantethine can support healthy serum lipid levels that are already within the normal range. Pantethine has also been shown to exert a number of beneficial effects on the liver and vascular endothelium through its ability to support healthy lipid metabolism in these tissues.
Pine bark extract acts to be a catalyst on the NO Synthase system, which permits vasodilation. Furthermore, it minimizes inflammation while in the arterial blood vessels and boosts their elasticity even though guarding the endothelial cells. Pine bark extract is hence in some cases referred to as a Nitric Oxide Booster ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Update August 3, 2009 - Updated with latest enzyme list from REBASE. Update January 2, 2009 - Updated to latest enzyme file from REBASE.. Update May 26, 2008 - Updated the rest of the site (help page, FAQ, etc.) to look better and be XHTML compliant.. Update March 17, 2008 - Fixed bug in virtual digest where the reported length of the last fragment of a virtual digest was one base too short.. Update October 20, 2007 - Fixed bug caused by the front page update that had disabled individual enzyme selection.. Update October 16, 2007 - Updated the front page to XHTML 1.0 Transitional. Also changed the look and added some Javascript input validation.. Update May 29, 2006 - Updated the front page to be W3C compliant. Should look better in Firefox and Netscape now.. Update March 10, 2005 - Moved to new servers this week, sorry for the temporary outage this caused. RestrictionMapper can now handle larger sequences than previously. I have tested successfully with a 200 kilobase sequence at the most ...
Thus, the two substrates of this enzyme are (3R)-3-hydroxyacyl-[acyl-carrier-protein] and NADP+, whereas its 3 products are 3-oxoacyl-[acyl-carrier-protein], NADPH, and H+.. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.. ...
The mitochondrial acyl-carrier protein (ACP) functions in the synthesis of fatty acids within the mitochondrial matrix. Fatty acids are elongated on the covalently bound 4-phosphopantetheine cofactor on ACP. ACP has a second essential function within the mitochondria in the biogenesis of iron-sulfur clusters. Cells depleted of ACP are impaired in FeS cluster formation throughout the cell. ACP is a stable subunit of the cysteine desulfurase (Nfs1) and Isd11 subcomplex that generates sulfide ions for FeS cluster formation. The FeS defect observed in cells depleted of ACP can be partially suppressed by overexpression of the mitochondrial iron transporter Mrs3. The stability of ACP is dependent of the iron status of mitochondria. Thus, the central role of Acp1 in mitochondrial fatty acid synthesis, lipoic acid formation and FeS cluster biogenesis suggests that these processes are tied to Fe availability within the mitochondria. ...
Double Strength- Cardiovascular Health- Supports Healthy Serum Lipids-- Coenzyme A PrecursorPantethine is a highly absorbable and biologically active form of pantothenic acid (Vitamin B-5). Pantethine forms the reactive component of Coenzyme A (CoA) and the acyl-carrier protein (ACP). CoA and ACP are extensively involved in carbohydrate lipid and amino acid metabolism. In addition to possessing the metabolic activity of pantothenic acid, Pantethine helps to support healthy serum lipids. Pantethine is also important for healthy cardiovascular function through its antioxidant activity.Nutrition Info Serving Size 1 SoftgelAmount Per Serving % Daily ValuePantesin Pantethine (Coenzyme A Precursor) 600 mg- - Percent Daily Values are based on 2,000 calorie diet.† Daily Value not established. DetailsSuggested Usage: As a dietary supplement, take 1 softgel 1 to 2 times daily, preferably with meals. For maximum utilization use this product with other NOW B-Vitamins. Other Ingredients: Softgel Capsule
Localization of apicoplast and mitochondrial LipDH. The localization of aLipDH and mLipDH was investigated by expressing the putative N-terminal presequences fused to GFP in P. falciparum intraerythrocytic parasites. A and B. Colocalization with antibodies directed against the apicoplast-resident acyl-carrier protein PFB0385w (ACP; A) and with MitoTracker Red (B) demonstrates that the putative apicoplast targeting presequence of aLipDH targets the marker protein GFP exclusively to the apicoplast. C-E. Colocalization experiments with the apicoplast protein ACP (C) and with the two mitochondrial markers MitoTracker Red and HSP60 PF10_0153 (D and E) indicate that mLipDH is localized exclusively in the mitochondrion.McMillan PJ, Stimmler LM, Foth BJ, McFadden GI, Müller S. The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol. 2005 55:27-38. Copyright John Wiley & Sons Ltd. 2010.. See original on MMP ...
Chemical Entities of Biological Interest (ChEBI) is a freely available dictionary of molecular entities focused on small chemical compounds.
This special edition of Patent Picks features a cornucopia of recently issued patents relevant to cosmetic product development; from water-dispersible cellulose thickeners and polyunsaturated fatty acid (PUFA) polyketide synthase systems, to odorant receptor modulators.
SWISS-MODEL Repository entry for C3LMG6 (FABA_VIBCM), 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase. Vibrio cholerae serotype O1 (strain M66-2)
The lung has been shown to be a target organ for the effects of Benzo[a]pyrene (B[a]P). 8-hydroxy-2-deoxyguanosine (oxo8dG) is a mutagenic oxidized base formed in DNA during the metabolism of B[a]P by the peroxidase and prostaglandin H synthetase systems. The objective of this study was to determine the capacity to cleave oxo8dG in the lung, liver, and kidney by measuring the activity of 8-oxogua
MetabolismFatty acid and phospholipid metabolismBiosynthesismalonyl CoA-acyl carrier protein transacylase (TIGR00128; EC 2.3.1.39; HMM-score: 328.4) ...
18635006] Characterization of the azinomycin B biosynthetic gene cluster revealing a different iterative type I polyketide synthase for naphthoate biosynthesis. (Chem Biol. , 2008 ...
Following a request from the European Commission, the Panel on Dietetic Products, Nutrition and Allergies (NDA) derived Dietary Reference Values (DRVs) for pantothenic acid. Pantothenic acid is a water-soluble vitamin, which is a component of coenzyme A (CoA) and acyl-carrier proteins. Pantothenic acid is ubiquitous and deficiency is rare. There are no suitable biomarkers that can be used to derive the requirement for pantothenic acid. Data available on pantothenic acid intakes and health consequences are very limited and cannot be used to derive DRVs for pantothenic acid. As there is insufficient evidence available to derive an Average Requirement and a Population Reference Intake, an Adequate Intake (AI) is proposed. The setting of AIs is based on observed pantothenic acid intakes with a mixed diet and the apparent absence of signs of deficiency in the EU, suggesting that current intake levels are adequate. The AI for adults is set at 5 mg/day. The AI for adults also applies to pregnant women. ...
Our collective results have shown that LEKTI1-12 and LEKTI multidomains had a strong inhibitory effect on trypsin, plasmin, KLK5, KLK6, KLK13, KLK14, cathepsin G, HNE, and subtilisin A. They had no inhibitory effect on KLK1, chymase, chymotrypsin and cysteine proteinases papain or cathepsins K, L, or S (Table 1). To understand whether LEKTI behaves as a slow - or fast-binding inhibitor, we measured the time course of various proteinase activities in the presence of different concentrations of rLEKTI. We have observed that the product formation over the 60 min assay period in the absence and presence of inhibitor was linear with respect to time [19,31,49,54]. The linear shapes of these inhibition curves indicate that rLEKTI is not a time-dependent inhibitor, suggesting that LEKTI binds rapidly to these proteinases and inactivates them. To classify the type of inhibition, the kinetic constants (Km and Vmax) of plasmin, trypsin, subtilisin A, cathepsin G, HNE, KLK5, KLK6, KLK13 and KLK14 were ...
ID PROAS_1_PE1015 STANDARD; PRT; 332 AA. AC PROAS_1_PE1015; D4HDE3; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3; EC=2.3.1 DE 180;AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III;AltName: DE Full=Beta-ketoacyl-ACP synthase III; (PROAS_1.PE1015). GN Name=fabH; OrderedLocusNames=HMPREF0675_4043; OS PROPIONIBACTERIUM ACNES SK137. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Propionibacterineae; Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=553199; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROAS_1.PE1015. CC Propionibacterium acnes SK137 chromosome, complete genome. CC annotated by Ensembl Genomes CC -!- ANNOTATIONS ORIGIN:D4HDE3_PROAS CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC ...
1MLA: The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.
15797213] The neocarzinostatin biosynthetic gene cluster from Streptomyces carzinostaticus ATCC 15944 involving two iterative type I polyketide synthases. (Chem Biol. , 2005 ...
Whereas enzymes are widely renowned for the exquisite specificity, we showed that enzymes also have low levels of catalysis for alternative reactions, an observation we described as catalytic promiscuity.. Catalytic promiscuity has been a key driver in the evolution of new enzymes, providing a head start and selective advantage for enzymes already possessing a low level of advantageous activity.. Catalytic promiscuity provides a powerful tool for addressing evolutionary and mechanistic questions. We are exploiting catalytic promiscuity across an enzyme superfamily to gain an understanding of the fundamental underpinnings of catalysis. Unlike traditional site-directed mutagenesis, experiments that are often limited to studying a single reaction catalyzed by an individual enzyme, we are using a comparative approach to ask not simply what the consequence is of removing a particular side chain, but how that removal and change in the side chain affects normal and promiscuous reactions. Because the ...
Using computational database searches, we have demonstrated previously that no gene sequences could be found for at least 36% of enzyme activities that have been assigned an Enzyme Commission number. Here we present a follow-up literature-based survey involving a statistically significant sample of such orphan activities. The survey was intended to determine whether sequences for these enzyme activities are truly unknown, or whether these sequences are absent from the public sequence databases but can be found in the literature. We demonstrate that for ~80% of sampled orphans, the absence of sequence data is bona fide. Our analyses further substantiate the notion that many of these enzyme activities play biologically important roles. This survey points toward significant scientific cost of having such a large fraction of characterized enzyme activities disconnected from sequence data. It also suggests that a larger effort, beginning with a comprehensive survey of all putative orphan activities, would
The activities of glycerol 3-phosphate dehydrogenase (EC 1.1.1.8), glycerol kinase (EC 2.7.1.30), lactate dehydrogenase (EC 1.1.1.27), "malic enzyme (L-malate-NADP+ oxidoreductase; EC 1.1.1.40) and the beta-oxoacyl-(acyl-carrier protein) reductase component of the fatty acid synthetase complex were measured in nine hepatoma lines (8 in rats, 1 in mouse) and in the livers of host animals. With the single exception of Morris hepatoma 16, which had unusually high glycerol 3-phosphate dehydrogenase activity, the activities of glycerol 3-phosphate dehydrogenase and glycerol kinase were highly correlated in normal livers and hepatomas (r = 0.97; P less than 0.01). The activities of these two enzymes were not strongly correlated with the activities of any of the other three enzymes. The primary function of hepatic glycerol 3-phosphate dehydrogenase appears to be in gluconeogenesis from glycerol.. ...
Multiple myeloma is a haematological malignancy characterized by the clonal proliferation of plasma cells. It has been proposed that targeting cancer cell metabolism would provide a new selective anticancer therapeutic strategy. In this work, we tested the hypothesis that inhibition of β-oxidation and de novo fatty acid synthesis would reduce cell proliferation in human myeloma cells. We evaluated the effect of etomoxir and orlistat on fatty acid metabolism, glucose metabolism, cell cycle distribution, proliferation, cell death and expression of G1/S phase regulatory proteins in myeloma cells. Etomoxir and orlistat inhibited β-oxidation and de novo fatty acid synthesis respectively in myeloma cells, without altering significantly glucose metabolism. These effects were associated with reduced cell viability and cell cycle arrest in G0/G1. Specifically, etomoxir and orlistat reduced by 40-70% myeloma cells proliferation. The combination of etomoxir and orlistat resulted in an additive inhibitory effect
The existence of subtle differences in the Sn subsites of closely-related (chymo)trypsin-like serine proteases, and the fact that the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold docks to the active site of (chymo)trypsin-like enzymes in a substrate-like fashion, suggested that the introduction of recognition elements that can potentially interact with the Sn subsites of these proteases might provide an effective means for optimizing enzyme potency and selectivity. Accordingly, a series of heterocyclic sulfide derivatives based on the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold (I) was synthesized and the inhibitory activity and selectivity of these compounds toward human leukocyte elastase (HLE), proteinase 3 (PR 3) and cathepsin G (Cat G) were then determined. Compounds with P1 = isobutyl were found to be potent, time-dependent inhibitors of HLE and, to a lesser extent PR 3, while those with P1 = benzyl inactivated Cat G rapidly and irreversibly. This study has demonstrated that ...
We have described GECKO, a simple method for constraining metabolic fluxes with enzymatic data that can be implemented for any GEM. Our method shares elements with previous approaches but stands out as the first method developed for implementing enzyme constraints on a genome‐scale model using experimentally measured turnover numbers and enabling the direct integration of absolute proteomic measurements. GECKO is based on the FBAwMC approach (Beg et al, 2007) but extended to limit each individual enzyme, thereby giving a physiologically constrained and thus more feasible solution. On the other hand, as GECKO uses inequalities instead of equalities, it is less constrained than RBA (Goelzer et al, 2015), thus relying less on the quality of the experimental data. Finally, GECKO does not require a detailed description of protein synthesis, and therefore, its implementation to model eukaryal organisms is less demanding compared to the ME‐modeling strategy (OBrien et al, 2013). Furthermore, the ...
Enzymes are a type of protein which helps to catalyze a chemical reaction. Individual enzymes have unique chemical structures which can speed up the reaction of specific substrates. All body functions involve enzymes including digestion DeMar DeRozan Jersey , respiration, transportation and detoxification. If some critical enzymes experience deficiency or malfunction it can lead to serious illness or death.There are two types of enzymes which are particularly important to our health, the digestive and antioxidant enzymes. Digestive enzymes help to break down food, enabling our body to absorb the nutrients necessary to sustain life. Antioxidant enzymes help to protect the body from attack by free radicals. Free radicals are linked to degenerative diseases such as aging, cancer Delon Wright Jersey , heart disease and other major illnesses.There are three further categories for digestive enzymes: amylase, protease and lipase. Saliva, pancreatic and intestinal secretions contain amylases. These work ...
TABLE-US-00022 TABLE 23 Pfam domain Accession Gathering name number cutoff Domain description 14-3-3 PF00244.9 25 14-3-3 protein 2OG-FeII_Oxy PF03171.10 11.5 2OG-Fe(II) oxygenase superfamily AAA PF00004.19 12.3 ATPase family associated with various cellular activities (AAA) AAA_2 PF07724.3 -5 ATPase family associated with various cellular activities (AAA) AAA_5 PF07728.4 4 ATPase family associated with various cellular activities (AAA) ABC2_membrane PF01061.13 -17.9 ABC-2 type transporter ABC_tran PF00005.16 9.5 ABC transporter ACP_syn_III_C PF08541.1 -24.4 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal ADH_N PF08240.2 -14.5 Alcohol dehydrogenase GroES-like domain ADH_zinc_N PF00107.16 23.8 Zinc-binding dehydrogenase AOX PF01786.8 25 Alternative oxidase AP2 PF00847.10 0 AP2 domain AT_hook PF02178.8 3.6 AT hook motif Aa_trans PF01490.7 -128.4 Transmembrane amino acid transporter protein Abhydrolase_1 PF00561.10 10.3 alpha/beta hydrolase fold Acid_phosphat_A PF00328.12 -64.5 ...
Lymphocytes. Lactic dehydrogenase isoenzymes. Total LDH is actually a group of enzymes. The individual enzymes (isoenzymes) that make up total LDH have different concentrations in different tissues. Therefore, the tissue responsible for an elevated total LDH value may often be identified by fractionation (separation) and measurement of individual isoenzymes. In addition, since the population normal range for total LDH is rather wide, abnormal elevation of one isoenzyme may occur without lifting total LDH out of the total LDH normal range.. Five main fractions (isoenzymes) of LDH are measured. With use of the standard international nomenclature (early U.S. investigators used opposite terminology), fraction 1 is found mainly in RBCs and in heart and kidney, fraction 3 comes from lung, and fraction 5 is located predominantly in liver and to a lesser extent in skeletal muscle. Skeletal muscle contains some percentage of all the fractions, although fraction 5 predominates. Various methods of ...
Enzymes for Baking As a result of our R&D over the past few years, today Maps has a versatile product range of enzymes for the baking industry. Apart from individual enzymes like amylase, xylanase, protease, cellulase, we also have a range of tailored enzyme cocktails (mixtures of different enzymes) to solve problems in certain baking applications. Our customers for our baking enzymes are the baking improver industry or the milling industry, the Wafer, Biscuit and Cracker industry, etc. Like all other living material, the cells in cereal grains used for flour contain enzymes. The most important enzymes in flour are the amylases and proteases. However, the quantities of these enzymes are not always ideal for baking purposes and supplementary enzymes often need to be added.. Bread-making Bread is the most common and traditional foods around the world. But bread actually has close links with enzymes. For years, enzymes such as malt and fungal alpha-amylase have been used in bread making. Due to the ...
acyl-carrier-protein S-acetyltransferase activity]. • hydrolase activity, acting on ester bonds. • [acyl-carrier-protein S- ... 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity]. • hydrolase activity. • ... enoyl-[acyl-carrier-protein reductase (NADPH, B-specific) activity]. • protein binding. • 3-oxoacyl-[acyl-carrier-protein ... acyl-carrier-protein dehydratase activity]. • 3-hydroxyoctanoyl-[acyl-carrier-protein dehydratase activity]. • protein ...
These include the acyl carrier protein (ACP), acetyl transferase (AT), ketosynthase (KS), malonyl transferase (MT; which can ... In vitro, annonacin is under study for its potential to affect the protein p21, cultured cancer cells, and the size of tumors ...
CurA contains a unique GCN5-related N-acetyltransferase (GNAT) loading domain and an associated acyl carrier protein (ACP). The ... "Tandem Acyl Carrier Proteins in the Curacin Biosynthetic Pathway Promote Consecutive Multienzyme Reactions with a Synergistic ...
acyl-carrier-protein S-acetyltransferase activity]. • hydrolase activity, acting on ester bonds. • [acyl-carrier-protein S- ... 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity]. • hydrolase activity. • ... enoyl-[acyl-carrier-protein reductase (NADPH, B-specific) activity]. • protein binding. • 3-oxoacyl-[acyl-carrier-protein ... acyl-carrier-protein dehydratase activity]. • 3-hydroxyoctanoyl-[acyl-carrier-protein dehydratase activity]. • protein ...
... acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the ... acyl-carrier protein] The enzyme catalyses a step of lipid A biosynthesis. Bartling, C.M.; Raetz, C.R. (2009). "Crystal ... acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine ⇌ {\displaystyle \rightleftharpoons } UDP-2,3-bis ... Bainbridge, B.W.; Karimi-Naser, L.; Reife, R.; Blethen, F.; Ernst, R.K.; Darveau, R.P. (2008). "Acyl chain specificity of the ...
... acyl-carrier-protein) S-acetyltransferase EC 2.3.1.39: (acyl-carrier-protein) S-malonyltransferase EC 2.3.1.40: acyl-(acyl- ... ribosomal-protein-alanine N-acetyltransferase EC 2.3.1.129: acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine O- ... acyl-carrier-protein) synthase II EC 2.3.1.180: beta-ketoacyl-(acyl-carrier-protein) synthase III EC 2.3.1.181: lipoyl(octanoyl ... carrier-protein)-phospholipid O-acyltransferase EC 2.3.1.41: 3-oxoacyl-(acyl-carrier-protein) synthase EC 2.3.1.42: glycerone- ...
... acyl-carrier protein s-acetyltransferase MeSH D08.811.913.050.134.060 --- acetyl-CoA C-acetyltransferase MeSH D08.811.913.050. ... acyl-carrier-protein) reductase (nadh) MeSH D08.811.682.660.390 --- enoyl-(acyl-carrier protein) reductase (nadph, b-specific) ... serine O-acetyltransferase MeSH D08.811.913.050.170 --- acyl-carrier protein s-malonyltransferase MeSH D08.811.913.050.173 --- ... acyl-carrier-protein) synthase MeSH D08.811.913.050.625 --- phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050. ...
... acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein ... acyl-carrier-protein] Thus, the two substrates of this enzyme are acetyl-CoA and acyl carrier protein, whereas its two products ... acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38) is an enzyme that catalyzes the chemical reaction acetyl-CoA + [acyl- ... acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis. ...
PPT attaches the 4′-phosphopantetheine prosthetic group of CoA to the acyl carrier protein (ACP) domain, which is found in the ... Here, acetyltransferase transfers the acetate group from acetyl-CoA onto the SH group of the 4′-phosphopantetheine prosthetic ... Leibundgut M, Jenni S, Frick C, Ban N (April 2007). "Structural basis for substrate delivery by acyl carrier protein in the ... Yeast fatty acyl synthase belongs to the Type I FAS and was the first of Type I FAS to be studied. Yeast fatty acyl synthase, ...
Price AC, Choi KH, Heath RJ, Li Z, White SW, Rock CO (March 2001). "Inhibition of beta-ketoacyl-acyl carrier protein synthases ... Acetyl-CoA C-Acetyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) This article incorporates ... Mammalian nonspecific lipid-transfer protein (nsL-TP) (also known as sterol carrier protein 2) is a protein which seems to ... or acyl carrier protein (ACP). All thiolases, whether they are biosynthetic or degradative in vivo, preferentially catalyze the ...
... acyl-carrier-protein) reductase (NADH) EC 1.3.1.10: enoyl-(acyl-carrier-protein) reductase (NADPH, B-specific) EC 1.3.1.11: 2- ... formate-C-acetyltransferase)-activating enzyme EC 1.97.1.5: now *EC 1.20.4.1 EC 1.97.1.6: now *EC 1.20.99.1 EC 1.97.1.7: now * ... acyl-(acyl-carrier-protein) desaturase EC 1.14.19.3: linoleoyl-CoA desaturase EC 1.14.19.4: Delta8-fatty-acid desaturase EC ... long-chain acyl-(acyl-carrier-protein) reductase EC 1.2.1.81: sulfoacetaldehyde dehydrogenase (acylating) EC 1.2.1.82: beta-apo ...
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase) ACRV1: encoding protein Acrosomal protein SP-10 ... fatty acyl-coA reductase 1 FAT3: fat atypical cadherin 3 FHIP: FTS and Hook-interacting protein FNBP4: Formin-binding protein 4 ... encoding protein Solute carrier family 17 (vesicular glutamate transporter), member 6 SMPD1: sphingomyelin phosphodiesterase 1 ... encoding protein Uncharacterized protein C11orf16 C11orf49: encoding protein UPF0705 protein C11orf49 C11orf52 encoding protein ...
Acetyl-Coenzyme A acetyltransferase 1) gene. Acetyl-Coenzyme A acetyltransferase 1 is an acetyl-CoA C-acetyltransferase enzyme ... "Protein Information: P24752". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 23 July 2016. Guo, ZY; Chang, ... Ge, J; Zhai, W; Cheng, B; He, P; Qi, B; Lu, H; Zeng, Y; Chen, X (September 2013). "Insulin induces human acyl-coenzyme A: ... This disease is inherited in an autosomal recessive manner, meaning that carriers of the gene do not show symptoms of the ...
"Spinach holo-acyl carrier protein: overproduction and phosphopantetheinylation in Escherichia coli BL21(DE3), in vitro ... "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins". J Mol Biol 325 (4 ... "Protein Expression and Purification 15 (3): 314-26. PMID 10092491. doi:10.1006/prep.1998.1016. Cite uses deprecated parameter , ... Glozak MA, Sengupta N, Zhang X, Seto E (2005). "Acetylation and deacetylation of non-histone proteins". Gene 363: 15-23. PMID ...
The acyl group at the C2 carbon is an acetate unit (as opposed to a fatty acid) whose short length increases the solubility of ... Using lab rats and mice, Jacques Benveniste found that ionophore A23187 (a mobile ion carrier that allows the passage of Mn2+, ... Marx F, Binder U, Leiter E, Pócsi I (Feb 2008). "The Penicillium chrysogenum antifungal protein PAF, a promising tool for the ... An acetyl group is then added by LPC acetyltransferase (LPCAT) to produce PAF. Using the de novo pathway, PAF is produced from ...
2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ... RCSB Protein Data Bank. doi:10.2210/rcsb_pdb/mom_2007_9.. ; PDB: 1CSC, 5CSC, 5CTS​ ... transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer. • citrate (Si)-synthase activity ... This protein may use the morpheein model of allosteric regulation.[11] ...
EC 6.2.1.19: Long-chain-fatty-acid--protein ligase. *EC 6.2.1.20: [[Long-chain-fatty-acid--[acyl-carrier-protein] ligase]] ... Choline acetyltransferase EC 2.3.1.6. *Category:EC 2.3.2 *Factor XIII EC 2.3.2.13 ... EC 6.2.1.46: [[L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase]] ... Category:EC 1.7.7 (with an iron-sulfur protein as acceptor). *Category:EC 1.7.99 (with other acceptors) *Nitrite reductase EC ...
... acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein ... acyl-carrier-protein] Thus, the two substrates of this enzyme are acetyl-CoA and acyl carrier protein, whereas its two products ... acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38) is an enzyme that catalyzes the chemical reaction acetyl-CoA + [acyl- ... acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis. ...
Abbreviations of gene symbols: acp, acyl carrier protein; alcA, monooxygenase; alcB, acetyltransferase; alcC, urease homolog; ... acyl carrier protein;. AT,. acyl transferase;. KS,. β-ketoacyl-ACP synthase;. NRPS,. nonribosomal peptide synthetase;. PKS,. ... abc, ABC transporter; acd, acyl-CoA dehydrogenase; acp, acyl carrier protein; aro, aromatase; ave, avermectin PKS; clf, chain- ... the modular PKS contains several catalytic domains in which the acyl-chain elongation involves acyl carrier protein (ACP), and ...
acyl-carrier-protein S-acetyltransferase activity]. • hydrolase activity, acting on ester bonds. • [acyl-carrier-protein S- ... 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity]. • hydrolase activity. • ... enoyl-[acyl-carrier-protein reductase (NADPH, B-specific) activity]. • protein binding. • 3-oxoacyl-[acyl-carrier-protein ... acyl-carrier-protein dehydratase activity]. • 3-hydroxyoctanoyl-[acyl-carrier-protein dehydratase activity]. • protein ...
2.3.1.38 [acyl-carrier-protein] S-acetyltransferase 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase ... malonyl CoA-acyl carrier protein transacylase Rv2243 fabD; malonyl CoA-acyl carrier protein transacylase K00645 fabD; [acyl- ... carrier-protein] S-malonyltransferase [EC:2.3.1.39] K00645 fabD; [acyl-carrier-protein] S-malonyltransferase [EC:2.3.1.39] ... 2.3.1.129 acyl-[acyl-carrier-protein]---UDP-N-acetylglucosamine O-acyltransferase 2.3.1.130 galactarate O- ...
... acyl carrier protein) synthase; 4, acetyl-CoA acetyltransferase; 5, 3-hydroxyacyl-CoA dehydrogenase; 6, enoyl-CoA hydratase; 7 ... protein plus protein, 16S plus 16S, metabolomics plus metabolomics, 16S plus protein, protein plus metabolomics, and 16S plus ... enoyl-(acyl carrier protein) reductase (NADH); 8, acetate CoA-transferase; 9, butyrate kinase; 10, citrate synthase; 11, ... of protein were normalized as described below (42): Normalized. SC. i. =. ∑. j. =. 1. M. ∑. k. =. 1. N. SC. k. M. ∑. k. =. 1. N ...
These include the acyl carrier protein (ACP), acetyl transferase (AT), ketosynthase (KS), malonyl transferase (MT; which can ... In vitro, annonacin is under study for its potential to affect the protein p21, cultured cancer cells, and the size of tumors ...
EC 2.3.1.178 diaminobutyrate acetyltransferase. EC 2.3.1.179 β-ketoacyl-acyl-carrier-protein synthase II. EC 2.3.1.180 β- ... acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadeca-13-enoyl-[acyl-carrier protein] + CO2 + an [acyl ... acyl-carrier protein]. cis-vaccenoyl-[acyl-carrier protein] = (Z)-octadeca-13-enoyl-[acyl-carrier protein]. Systematic name: (Z ... S-acyl carrier protein:malonate acyl carrier protein-SH transferase. Systematic name: acetyl-[acyl-carrier-protein]:malonate S ...
Acyl-carrier-protein] S acetyltransferase antibody. *[Acyl-carrier-protein] S malonyltransferase antibody ... This multifunctional protein has 7 catalytic activities and an acyl carrier protein. ... PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex miRNA assays. By ...
CurA contains a unique GCN5-related N-acetyltransferase (GNAT) loading domain and an associated acyl carrier protein (ACP). The ... "Tandem Acyl Carrier Proteins in the Curacin Biosynthetic Pathway Promote Consecutive Multienzyme Reactions with a Synergistic ...
acyl-carrier-protein S-acetyltransferase activity]. • hydrolase activity, acting on ester bonds. • [acyl-carrier-protein S- ... 3-oxoacyl-[acyl-carrier-protein synthase activity]. • acyl-[acyl-carrier-protein hydrolase activity]. • hydrolase activity. • ... enoyl-[acyl-carrier-protein reductase (NADPH, B-specific) activity]. • protein binding. • 3-oxoacyl-[acyl-carrier-protein ... acyl-carrier-protein dehydratase activity]. • 3-hydroxyoctanoyl-[acyl-carrier-protein dehydratase activity]. • protein ...
Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology ... PedD displayed malonyl- but not acetyltransferase activity toward various acyl carrier proteins (ACPs). In contrast, the AT2 ... especially for heterologous protein production. Here, the nature of the foreign protein makes it impossible to predict the, e.g ... As the best SP for a target protein of choice cannot be predicted a priori, screening of homologous SPs has been shown to be a ...
Lowe PN, Rhodes S; Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.; ... Fatty acyl CoA. Malonyl-CoA. less than 6 iterations. Palmitate. Acetyl-ACP. trans-delta2-enoyl-CoA. Acyl-CoA (n+2). ... Fatty acyl CoA. HADHSC. GeneProduct. Long-Chain fatty acid. CHEBI:15904 (ChEBI) Malonyl-ACP. Malonyl-CoA. Oxaloacetate. 2509917 ... Acyl-CoA (n+2). Butyryl-ACP. CG11198. GeneProduct. 35761 (Entrez Gene) CG1516. GeneProduct. 36020 (Entrez Gene) CG16935. ...
Lowe PN, Rhodes S; Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.; ... Fatty acyl CoA. trans-delta2-enoyl-CoA. Palmitoyl-ACP. Long-Chain fatty acid. Citrate. Butyryl-ACP. Acyl-CoA (n+2). 6 ... Acyl-CoA (n+2). Butyryl-ACP. Metabolite. 8040 (PubChem-substance) CG11198. GeneProduct. 35761 (Entrez Gene) CG1516. GeneProduct ... Fatty acyl CoA. HADHSC. GeneProduct. Long-Chain fatty acid. Metabolite. CHEBI:15904 (ChEBI) Malonyl-ACP. Metabolite. C01209 ( ...
Lowe PN, Rhodes S; Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.; ... Fatty acyl CoA. Malonyl-CoA. 6 iterations. trans-delta2-enoyl-CoA. Acetyl-ACP. Citrate. Malonyl-ACP. Palmitate. Acyl-CoA (n+2) ... Fatty acyl CoA. Metabolite. CHEBI:37554 (ChEBI) HADHSC. GeneProduct. Long-Chain fatty acid. Metabolite. CHEBI:15904 (ChEBI) ... Acyl-CoA (n+2). Metabolite. CHEBI:37554 (ChEBI) Butyryl-ACP. Metabolite. CHEBI:3247 (ChEBI) CG11198. GeneProduct. 35761 (Entrez ...
... a gene encoding the type II acyl-CoA:diacylglycerol acyltransferase 5. Combined with bio-flocculation, this approach led to ... ACP, acyl carrier protein; AT, acetyltransferase; MPT, malonyl/palmitoyl transferase; ACSL, acyl-CoA synthetase; KS, β-ketoacyl ... The construct generated DGTT5 fused to the cerulean fluorescent protein, and the presence of the cerulean protein in DGTT5ox3 ... 13068_2018_1172_MOESM8_ESM.pdf Additional file 8: Table S2. Predicted genes and proteins involved in fatty acid and ...
Stearoyl-acyl carrier protein desaturase. SAT2: Strepothricin AcetylTransferase 2. T-DNA: Transfer DNA ... A second pair of primers and a probe are used to detect a 68 bp fragment of stearoyl-acyl carrier protein desaturase (SAD) as a ... stearoyl-acyl carrier protein desaturase (SAD) in the commercial tests). As a result, this assay halves the number of PCR ... The repeated fragment starts at the NOS promoter of the Nos gene and extends to just past the streptothricin acetyltransferase ...
The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel ... and subsequently transacylation of the methylmalonyl group to the phosphopantetheinyl group of the LnmL acyl carrier protein [ ... Protein Workshop , Ligand Explorer. Global Symmetry: Cyclic - C2 (3D View). Global Stoichiometry: Homo 2-mer - A2 Biological ... The β-branched C3 unit in leinamycin biosynthesis is installed by a set of four proteins, LnmFKLM. In vitro biochemical ...
Protein Coding), Fatty Acid Synthase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards ... acyl-carrier-protein] S-acetyltransferase activity. IEA. --. GO:0004314. [acyl-carrier-protein] S-malonyltransferase activity. ... Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein ... An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH. *FAS_HUMAN,P49327 ...
... acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier- ... protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. ... acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].. Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl- ... acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC. *[acyl-carrier-protein] S-malonyltransferase activity ...
... acyl-carrier protein):UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the ... acyl-carrier protein] The enzyme catalyses a step of lipid A biosynthesis. Bartling, C.M.; Raetz, C.R. (2009). "Crystal ... acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine ⇌ {\displaystyle \rightleftharpoons } UDP-2,3-bis ... Bainbridge, B.W.; Karimi-Naser, L.; Reife, R.; Blethen, F.; Ernst, R.K.; Darveau, R.P. (2008). "Acyl chain specificity of the ...
... acyl-carrier-protein) S-acetyltransferase EC 2.3.1.39: (acyl-carrier-protein) S-malonyltransferase EC 2.3.1.40: acyl-(acyl- ... ribosomal-protein-alanine N-acetyltransferase EC 2.3.1.129: acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine O- ... acyl-carrier-protein) synthase II EC 2.3.1.180: beta-ketoacyl-(acyl-carrier-protein) synthase III EC 2.3.1.181: lipoyl(octanoyl ... carrier-protein)-phospholipid O-acyltransferase EC 2.3.1.41: 3-oxoacyl-(acyl-carrier-protein) synthase EC 2.3.1.42: glycerone- ...
... acyl-carrier protein s-acetyltransferase MeSH D08.811.913.050.134.060 --- acetyl-CoA C-acetyltransferase MeSH D08.811.913.050. ... acyl-carrier-protein) reductase (nadh) MeSH D08.811.682.660.390 --- enoyl-(acyl-carrier protein) reductase (nadph, b-specific) ... serine O-acetyltransferase MeSH D08.811.913.050.170 --- acyl-carrier protein s-malonyltransferase MeSH D08.811.913.050.173 --- ... acyl-carrier-protein) synthase MeSH D08.811.913.050.625 --- phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050. ...
... acyl-carrier protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier- ... protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase. ... This protein contains domains similar to those of a fatty acid synthase beta subunit, namely: [ ... acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].. Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl- ...
Transcription of other putative amino acid biosynthesis-related genes and the acyl carrier protein (ACP; GRMZM2G091715) ... serine acetyltransferase (SAT; GRMZM2G048740), which is involved in cysteine biosynthesis, was upregulated by 3.67-fold; the ... translation-related proteins (eEF1A and some ribosomal proteins) (Hunter et al., 2002), and lysine-rich proteins (sorbitol ... Nineteen genes related to protein folding, most of which encode chaperones such as heat shock protein 70 (HSP70; GRMZM2G001500 ...
Acyl carrier-protein] acetyltransferase Current Synonym true false 3753781016 Acyl carrier-protein acetyltransferase Current ... Acyl carrier-protein acetyltransferase (substance). Code System Preferred Concept Name. Acyl carrier-protein acetyltransferase ...
  • Coding sequences (CDSs) encoding proteins whose function previously was imputed or not known were re-evaluated, and putative functions were assigned by manually evaluating the results from BLAST and DARWIN (data analysis and retrieval with indexed nucleotide/peptide sequences) analyses. (biomedcentral.com)
  • We show that that the polymerase-δ interacting protein 2 (Poldip2) is an oxygen-sensitive protein that regulates the lipoylation and activation of the pyruvate and α-ketoglutarate dehydrogenase complexes. (pnas.org)
  • The E. coli K-12 chromosome is currently represented by 4,401 genes encoding 116 RNAs and 4,285 proteins. (biomedcentral.com)
  • Proteins whose genes are observed to be correlated in expression, across a large number of experiments. (string-db.org)
  • DNA microarray-based experiments have shown that INH induces several genes in Mycobacterium tuberculosis that encode proteins physiologically relevant to the drug's mode of action. (asm.org)
  • Several bacterial proteins are now known to undergo glycosylation, including potential virulence factors of pathogenic bacteria, such as the pilins of Neisseria gonorrhoeae ( 2 ), Neisseria meningitidis ( 3 ), and one strain of Pseudomonas aeruginosa ( 4 ), an adhesin of Chlamydia ( 5 ), a surface-exposed immunodominant protein of two Ehrlichia species ( 6 ), and the TiBA adhesin of ETEC ( 7 ). (pnas.org)
  • The genetic basis of glycosylation of selected bacterial proteins has been only recently approached. (pnas.org)
  • Bacterial cells were disrupted in a lysis buffer containing 30 mM Tris, 2 M thiourea, 7 M urea, 4% CHAPS, 2% IPG buffer pH 3-10 and protease inhibitors and then subjected to sonication in order to solubilize as much as possible the bacterial proteins. (bvsalud.org)
  • The analyses of the 309 cell wall proteins provided theoretical molecular mass and p I distributions and determined that 18 proteins are shared with the cell surface-exposed proteome. (biomedcentral.com)
  • Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. (yeastgenome.org)
  • Most Streptomyces chromosomal DNA molecules are about 8-Mb-long, with terminal-inverted repeats and covalently bound terminal proteins supposedly at the 5′ end. (pnas.org)
  • Protein glycosylation in prokaryotic organisms is a relatively uncommon posttranslation modification process, first described in Archea, where the S layer proteins were shown to contain covalently attached sugars ( 1 ). (pnas.org)
  • The coding sequences (CDSs) are represented by modules (protein elements of at least 100 amino acids with biological activity and independent evolutionary history). (biomedcentral.com)
  • P. aeruginosa can be classified into two groups (a- and b-types) ( 19 ) on the basis of the expression of the flagellin protein of a specific primary amino acid sequence ( 20 ). (pnas.org)
  • The resulting transcript encodes ACAT1, which is a 45.1 kDa protein composed of 427 amino acids. (wikipedia.org)
  • We identified polypeptides that showed homology to most major proteins needed for production of glycoprotein-binding fimbriae, structures that could possibly be important for adhesion and persistence in the GIT. (pnas.org)
  • Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure. (supfam.org)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • The observed difference in the mobility of the flagellin protein from the strain PAK (a-type) from its predicted size by sequence ( 21 ) was assumed to be because of posttranslational modification. (pnas.org)
  • Download DNA or protein sequence, view genomic context and coordinates. (yeastgenome.org)
  • Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein. (yeastgenome.org)
  • We also identify a paralogous version of the methionyl-tRNA synthetase, which is widespread in bacteria, and present evidence using contextual information that it might function independently of protein synthesis as a peptide ligase in the formation of a peptide- derived secondary metabolite. (biomedcentral.com)