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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

*  Fatty acid synthase
... acyl carrier protein (ACP) and thioesterase (TE)). The conventional model for organization of FAS (see the 'head-to-tail' model ... malonyl/acetyltransferase (MAT), and dehydrase (DH)), are separated by a core region of 600 residues from four C-terminal ... "Mechanism of substrate shuttling by the acyl-carrier protein within the fatty acid mega-synthase". J. Am. Chem. Soc. 132 (35): ... between these active sites while attached covalently to the phosphopantetheine prosthetic group of an acyl carrier protein (ACP ...
*  acyl-carrier-protein) S-acetyltransferase
... 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. ...
*  Annonacin
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 ...
*  Curacin A
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 ...
*  List of EC numbers (EC 2)
... 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- ...
*  List of MeSH codes (D08)
... 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. ...
*  UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
... 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 ...
*  Fatty-acyl-CoA synthase
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, ...
*  Thiolase
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 ...
*  List of EC numbers (EC 1)
... 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 ...
*  Chromosome 11 (human)
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 ...
*  ACAT1
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 ...
*  Platelet-activating factor
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 ...
US6995254B1 - Polynucleotide encoding the enoyl-acyl carrier protein reductase of Staphylococcus aureus, FAB I 
        -...  US6995254B1 - Polynucleotide encoding the enoyl-acyl carrier protein reductase of Staphylococcus aureus, FAB I -...
... such as a chloramphenicol acetyl transferase ("CAT") transcription unit, downstream of restriction site or sites for ... Rock et al., "Preparative Enzymatic Synthetic and Hydrophobic Chromatography of Acyl-Acyl Carrier Protein", The Journal of ... Polynucleotide encoding the enoyl-acyl carrier protein reductase of Staphylococcus aureus, FAB I Download PDF Info. Publication ... Fab I (previously designated EnvM) functions as an enoyl-acyl carrier protein (ACP) reductase (Bergler, et al, (1994), J. Biol ...
more infohttps://patents.google.com/patent/US6995254?oq=U.S.+Patent+No.+4%2C528%2C643
acyl-carrier-protein) S-acetyltransferase - Wikipedia  acyl-carrier-protein) S-acetyltransferase - Wikipedia
... 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. ...
more infohttps://en.wikipedia.org/wiki/(acyl-carrier-protein)_S-acetyltransferase
KEGG BRITE: Enzymes - Mycobacterium tuberculosis H37Rv  KEGG BRITE: Enzymes - Mycobacterium tuberculosis H37Rv
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- ...
more infohttp://www.genome.jp/kegg-bin/get_htext?mtu01000+Rv2243
Anti-Fatty Acid Synthase antibody (ab99359) | Abcam  Anti-Fatty Acid Synthase antibody (ab99359) | Abcam
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 ...
more infohttp://www.abcam.com/fatty-acid-synthase-antibody-ab99359.html
Protocols and Video Articles Authored by Marco Oldiges  Protocols and Video Articles Authored by Marco Oldiges
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 ...
more infohttps://www.jove.com/author/Marco_Oldiges
Fatty acid synthase - Wikipedia  Fatty acid synthase - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Fatty_acid_synthase
Annonacin - Wikipedia  Annonacin - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Annonacin
FASN - Wicipedia  FASN - Wicipedia
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 ...
more infohttps://cy.wikipedia.org/wiki/FASN
FAS1 - Fatty acid synthase subunit beta - Candida albicans (Yeast) - FAS1 gene & protein  FAS1 - Fatty acid synthase subunit beta - Candida albicans (Yeast) - FAS1 gene & protein
... 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 ...
more infohttp://www.uniprot.org/uniprot/P34731
TOXC - Putative fatty acid synthase subunit TOXC - Cochliobolus carbonum (Maize leaf spot fungus) - TOXC gene & protein  TOXC - Putative fatty acid synthase subunit TOXC - Cochliobolus carbonum (Maize leaf spot fungus) - TOXC gene & protein
... 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- ...
more infohttp://www.uniprot.org/uniprot/Q92215
Genome sequence of an industrial microorganism Streptomyces avermitilis: Deducing the ability of producing secondary...  Genome sequence of an industrial microorganism Streptomyces avermitilis: Deducing the ability of producing secondary...
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 ...
more infohttps://www.pnas.org/content/98/21/12215
Enhancing oil production and harvest by combining the marine alga Nannochloropsis oceanica and the oleaginous fungus...  Enhancing oil production and harvest by combining the marine alga Nannochloropsis oceanica and the oleaginous fungus...
... 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 ...
more infohttps://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-018-1172-2
EC 2.3.1.151-2.3.1.200  EC 2.3.1.151-2.3.1.200
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 ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/0301d.html
FASN Gene - GeneCards | FAS Protein | FAS Antibody  FASN Gene - GeneCards | FAS Protein | FAS Antibody
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 ...
more infohttp://www.genecards.org/cgi-bin/carddisp.pl?id=3594&id_type=hgnc&search=3594
ENZYME: 2.3.1.  ENZYME: 2.3.1.
Acyl-carrier-protein] S-acetyltransferase 2.3.1.39 [Acyl-carrier-protein] S-malonyltransferase 2.3.1.40 Acyl-[acyl-carrier- ... acyl-carrier-protein] synthase II 2.3.1.180 Beta-ketoacyl-[acyl-carrier-protein] synthase III 2.3.1.181 Lipoyl(octanoyl) ... 1-acyl-sn-glycerol-3-phosphate acyltransferase 2.3.1.n5 Glycerol-3-phosphate acyltransferase (acyl-[acyl-carrier-protein]- ... protein]--phospholipid O-acyltransferase 2.3.1.41 Beta-ketoacyl-[acyl-carrier-protein] synthase I 2.3.1.42 Glycerone-phosphate ...
more infohttps://enzyme.expasy.org/EC/2.3.1.-
NAVER Academic > Search...  NAVER Academic > Search...
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase, genetics, metabolism, Acetyltransferases, Acyl Carrier Protein, Base Sequence, ... Bacterial Proteins, genetics, metabolism, Escherichia coli, Glycoside Hydrolases, Membrane Transport Proteins, Muramic Acids, ... Bacterial Proteins, genetics, metabolism, Escherichia coli, Glycoside Hydrolases, Membrane Transport Proteins, Muramic Acids, ... Bacterial Proteins, genetics, Bacteriophages, pathogenicity, Biofilms, CRISPR-Associated Proteins, CRISPR-Cas Systems, ...
more infohttp://academic.naver.com/search.naver?field=3&query=Journal+of+Bacteriology+198%EA%B6%8C+22%ED%98%B8
Journal: Journal of the American Chemical Society / Publication Year: 2018 / Source: 2018 v.140 no.7 - PubAg Search Results  Journal: Journal of the American Chemical Society / Publication Year: 2018 / Source: 2018 v.140 no.7 - PubAg Search Results
Cylindrospermopsis raciborskii; acetyltransferases; acyl carrier protein; amino acids; biochemical pathways; biosynthesis; ... Mutational analysis is widely used to study the relationship between sequence and structure of proteins and peptides. It is ... We describe the preparation, evaluation, and application of an S100A12 protein-conjugated solid support, hereafter the "A12- ... alanine; bradykinin; gases; geometry; mutants; mutational analysis; proline; proteins; spectroscopy. Abstract:. ... ...
more infohttps://pubag.nal.usda.gov/?f%5Bjournal_name%5D%5B%5D=Journal+of+the+American+Chemical+Society&f%5Bpublication_year_rev%5D%5B%5D=7982-2018&f%5Bsource%5D%5B%5D=2018+v.140+no.7
FERMENTATION AND PURIFICATION OF ACTINOMADURA CHROMOPROTEIN AND RELATED SPECIES - Patent application  FERMENTATION AND PURIFICATION OF ACTINOMADURA CHROMOPROTEIN AND RELATED SPECIES - Patent application
aa, amino acid; KS, ketosynthase; AT, acetyltransferase; ACP, acyl carrier protein; KR, ketoreductase; DH, dehydratase; TD, ... Basic proteins such as myelin basic protein, but not neutral/acidic proteins, are also susceptible to cleavage. [0046]FIG. 31 ... and acyl carrier protein (ACP). It catalyzes the formation of a linear tetraketide from one acetyl-coenzyme A (coA) and 3 ... 30). The chromoprotein also cleaves other basic proteins such as myelin basic protein, but not neutral/acidic proteins such as ...
more infohttp://www.patentsencyclopedia.com/app/20100028952
RCSB PDB - 4HZO: The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic...  RCSB PDB - 4HZO: The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic...
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 ...
more infohttps://www.rcsb.org/structure/4HZO
What are we up to?  What are we up to?
Coenzyme A, Acyl Carrier Protein, Lipoate Acetyl Transferase, and R-dihydrolipoic acid are among the more obvious targets for ... acyl-carrier protein, and R-lipoic acid) it simply accumulates. Consequently, weight gain is not something that anyone should ... A report that 95% of breast cancer tumors contain viral proteins (RAK) and gene fragments (similar to the proteins and genetic ... leaving behind only the binding proteins. These denuded binding proteins, until digested, would tend to absorb fat-soluble ...
more infohttp://www.vitaletherapeutics.org/vtlwhatr.htm
Results for cd08246  Results for cd08246
Acyl-carrier-protein] S-acetyltransferase; Includes: RecName: Full=[Acyl-carrier-protein] S-malonyltransferase; Includes: ... acyl-carrier-protein] synthase; Includes: RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; Includes: RecName: Full=3- ... acyl-carrier-protein] dehydratase; Includes: RecName: Full=Enoyl-[acyl-carrier-protein] reductase; Includes: RecName: Full= ... Oleoyl-[acyl-carrier-protein] hydrolase. CRYZ. 1429. >gi,585013,sp,Q08257.1,QOR_HUMAN RecName: Full=Quinone oxidoreductase; ...
more infohttp://bioinf.umbc.edu/dmdm/genes_domains.php?search_term=cd08246
Results for COG1028  Results for COG1028
Acyl-carrier-protein] S-acetyltransferase; Includes: RecName: Full=[Acyl-carrier-protein] S-malonyltransferase; Includes: ... acyl-carrier-protein] synthase; Includes: RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase; Includes: RecName: Full=3- ... acyl-carrier-protein] dehydratase; Includes: RecName: Full=Enoyl-[acyl-carrier-protein] reductase; Includes: RecName: Full= ... acyl-carrier-protein] reductase; AltName: Full=Protein Ke6; Short=Ke-6; AltName: Full=Really interesting new gene 2 protein; ...
more infohttp://bioinf.umbc.edu/DMDM/genes_domains.php?search_term=COG1028
Localization of proteins in the cell wall of Mycobacterium avium subsp. paratuberculosis K10 by proteomic analysis | Proteome...  Localization of proteins in the cell wall of Mycobacterium avium subsp. paratuberculosis K10 by proteomic analysis | Proteome...
309 different proteins were identified, which included 101 proteins previously annotated as hypothetical or conserved ... 38 proteins were identified as surface-exposed by trypsin treatment. To categorize and analyze these proteomic data on the ... The analyses of the 309 cell wall proteins provided theoretical molecular mass and pI distributions and determined that 18 ... paratuberculosis K10 and an cell surface enzymatic shaving method was used to determine the surface-exposed proteins. ...
more infohttps://proteomesci.biomedcentral.com/articles/10.1186/1477-5956-8-21
Fatty Acid Synthase: Association with Insulin Resistance, Type 2 Diabetes, and Cancer | Clinical Chemistry  Fatty Acid Synthase: Association with Insulin Resistance, Type 2 Diabetes, and Cancer | Clinical Chemistry
... malonyl/acetyltransferase, dehydrase, enoyl reductase, β-ketoacyl reductase, acyl carrier protein, and thioesterase) that ... acyl carrier protein, and thioesterase domains of the adjacent monomer (14)(15)(16)(17). That is, 2 FASN monomers in the ... where they can access the acyl carrier protein of either subunit (19). In 2006, Maier et al. reported the architecture of ... Although the flexibly tethered acyl carrier protein and thioesterase domains remain unresolved, the structure clearly reveals a ...
more infohttp://clinchem.aaccjnls.org/content/55/3/425.full
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase - Wikipedia  UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase - Wikipedia
... 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 ...
more infohttps://en.wikipedia.org/wiki/UDP-3-O-(3-hydroxymyristoyl)glucosamine_N-acyltransferase
  • The resulting β-ketoacyl derivative is then reduced in 3 consecutive steps, β-ketoacyl reduction, β-hydroxyacyl dehydration, and enoyl reduction, to the saturated acyl derivative, which then acts as a primer for further elongation and reduction cycles to yield ultimately a palmitoyl derivative. (aaccjnls.org)
  • Since the genome of Escherichia coli K-12 was initially annotated in 1997, additional functional information based on biological characterization and functions of sequence-similar proteins has become available. (biomedcentral.com)
  • HubP, a Polar Landmark Protein, Regulates Flagellar Number by Assisting in the Proper Polar Localization of FlhG in Vibrio alginolyticus. (naver.com)
  • Localization of proteins in the cell wall of Mycobacterium avium subsp. (biomedcentral.com)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • LnmK shows no sequence homology to proteins of known function, representing a new family of AT/DC enzymes. (rcsb.org)
  • In prokaryotes and lower eukaryotes, such as yeast, bacteria, plants, and parasites, FA biosynthesis is accomplished by a series of monofunctional proteins in a dissociated type-II FASN system (FASN II). (aaccjnls.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)
  • 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)
  • The E. coli K-12 chromosome is currently represented by 4,401 genes encoding 116 RNAs and 4,285 proteins. (biomedcentral.com)
  • In vitro, annonacin is under study for its potential to affect the protein p21, cultured cancer cells, and the size of tumors in nude mice. (wikipedia.org)
  • Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure. (supfam.org)
  • Some protein-coding sequences are compound and encode multimodular proteins. (biomedcentral.com)
  • 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)
  • 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)