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.
An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
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.
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
Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.
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.
Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
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.
A 3-oxoacyl reductase that has specificity for ACYL CARRIER PROTEIN-derived FATTY ACIDS.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
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.
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.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. EC 6.2.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
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)
The addition of an organic acid radical into a molecule.
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.
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.
Thiolester hydrolases are enzymes that catalyze the hydrolysis of thioester bonds, commonly found in acetyl-CoA and other coenzyme A derivatives, to produce free carboxylic acids and CoASH.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
A diphenyl ether derivative used in cosmetics and toilet soaps as an antiseptic. It has some bacteriostatic and fungistatic action.
Proteins found in any species of bacterium.
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.
An epoxydodecadienamide isolated from several species, including ACREMONIUM, Acrocylindrum, and Helicoceras. It inhibits the biosynthesis of several lipids by interfering with enzyme function.
A genus of gram-positive bacteria whose spores are round to oval and covered by a sheath.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Compounds based on ANTHRACENES which contain two KETONES in any position. Substitutions can be in any position except on the ketone groups.
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.
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.
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.
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.
Malonates are organic compounds containing a malonate group, which is a dicarboxylic acid functional group with the structure -OC(CH2COOH)2, and can form salts or esters known as malonates.
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.
Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.
Polyacenes with four ortho-fused benzene rings in a straight linear arrangement. This group is best known for the subclass called TETRACYCLINES.
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).
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.
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.
The rate dynamics in chemical or physical systems.
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.
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.
Proteins obtained from ESCHERICHIA COLI.
Proteins prepared by recombinant DNA technology.
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.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The condition of harboring an infective organism without manifesting symptoms of infection. The organism must be readily transmissible to another susceptible host.
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)
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.
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.
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.
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 acids are complex, long-chain fatty acids that are a major component of the cell wall of Mycobacterium species, including the causative agents of tuberculosis and leprosy, providing them with unique characteristics such as resistance to acid-alkali stability, pigmentation, and protection against host immune responses.
Compounds containing the -SH radical.
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.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
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
The functional hereditary units of BACTERIA.
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.
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).
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
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).
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.
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.
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).
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
Any salt or ester of glycerophosphoric acid.
"Esters are organic compounds that result from the reaction between an alcohol and a carboxylic acid, playing significant roles in various biological processes and often used in pharmaceutical synthesis."
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.
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)
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.

Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. (1/346)

Palmitoleate is not present in lipid A isolated from Escherichia coli grown at 30 degrees C or higher, but it comprises approximately 11% of the fatty acyl chains of lipid A in cells grown at 12 degrees C. The appearance of palmitoleate at 12 degrees C is accompanied by a decline in laurate from approximately 18% to approximately 5.5%. We now report that wild-type E. coli shifted from 30 degrees C to 12 degrees C acquire a novel palmitoleoyl-acyl carrier protein (ACP)-dependent acyltransferase that acts on the key lipid A precursor Kdo2-lipid IVA. The palmitoleoyl transferase is induced more than 30-fold upon cold shock, as judged by assaying extracts of cells shifted to 12 degrees C. The induced activity is maximal after 2 h of cold shock, and then gradually declines but does not disappear. Strains harboring an insertion mutation in the lpxL(htrB) gene, which encodes the enzyme that normally transfers laurate from lauroyl-ACP to Kdo2-lipid IVA (Clementz, T., Bednarski, J. J., and Raetz, C. R. H. (1996) J. Biol. Chem. 271, 12095-12102) are not defective in the cold-induced palmitoleoyl transferase. Recently, a gene displaying 54% identity and 73% similarity at the protein level to lpxL was found in the genome of E. coli. This lpxL homologue, designated lpxP, encodes the cold shock-induced palmitoleoyl transferase. Extracts of cells containing lpxP on the multicopy plasmid pSK57 exhibit a 10-fold increase in the specific activity of the cold-induced palmitoleoyl transferase compared with cells lacking the plasmid. The elevated specific activity of the palmitoleoyl transferase under conditions of cold shock is attributed to greatly increased levels of lpxP mRNA. The replacement of laurate with palmitoleate in lipid A may reflect the desirability of maintaining the optimal outer membrane fluidity at 12 degrees C.  (+info)

Acyl homoserine-lactone quorum-sensing signal generation. (2/346)

Acyl homoserine lactones (acyl-HSLs) are important intercellular signaling molecules used by many bacteria to monitor their population density in quorum-sensing control of gene expression. These signals are synthesized by members of the LuxI family of proteins. To understand the mechanism of acyl-HSL synthesis we have purified the Pseudomonas aeruginosa RhlI protein and analyzed the kinetics of acyl-HSL synthesis by this enzyme. Purified RhlI catalyzes the synthesis of acyl-HSLs from acyl-acyl carrier proteins and S-adenosylmethionine. An analysis of the patterns of product inhibition indicated that RhlI catalyzes signal synthesis by a sequential, ordered reaction mechanism in which S-adenosylmethionine binds to RhlI as the initial step in the enzymatic mechanism. Because pathogenic bacteria such as P. aeruginosa use acyl-HSL signals to regulate virulence genes, an understanding of the mechanism of signal synthesis and identification of inhibitors of signal synthesis has implications for development of quorum sensing-targeted antivirulence molecules.  (+info)

Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. (3/346)

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

The pro1(+) gene from Sordaria macrospora encodes a C6 zinc finger transcription factor required for fruiting body development. (4/346)

During sexual morphogenesis, the filamentous ascomycete Sordaria macrospora differentiates into multicellular fruiting bodies called perithecia. Previously it has been shown that this developmental process is under polygenic control. To further understand the molecular mechanisms involved in fruiting body formation, we generated the protoperithecia forming mutant pro1, in which the normal development of protoperithecia into perithecia has been disrupted. We succeeded in isolating a cosmid clone from an indexed cosmid library, which was able to complement the pro1(-) mutation. Deletion analysis, followed by DNA sequencing, subsequently demonstrated that fertility was restored to the pro1 mutant by an open reading frame encoding a 689-amino-acid polypeptide, which we named PRO1. A region from this polypeptide shares significant homology with the DNA-binding domains found in fungal C6 zinc finger transcription factors, such as the GAL4 protein from yeast. However, other typical regions of C6 zinc finger proteins, such as dimerization elements, are absent in PRO1. The involvement of the pro1(+) gene in fruiting body development was further confirmed by trying to complement the mutant phenotype with in vitro mutagenized and truncated versions of the pro1 open reading frame. Southern hybridization experiments also indicated that pro1(+) homologues are present in other sexually propagating filamentous ascomycetes.  (+info)

Kinetic analysis of the actinorhodin aromatic polyketide synthase. (5/346)

Type II polyketide synthases (PKSs) are bacterial multienzyme systems that catalyze the biosynthesis of a broad range of natural products. A core set of subunits, consisting of a ketosynthase, a chain length factor, an acyl carrier protein (ACP) and possibly a malonyl CoA:ACP transacylase (MAT) forms a "minimal" PKS. They generate a poly-beta-ketone backbone of a specified length from malonyl-CoA derived building blocks. Here we (a) report on the kinetic properties of the actinorhodin minimal PKS, and (b) present further data in support of the requirement of the MAT. Kinetic analysis showed that the apoACP is a competitive inhibitor of minimal PKS activity, demonstrating the importance of protein-protein interactions between the polypeptide moiety of the ACP and the remainder of the minimal PKS. In further support of the requirement of MAT for PKS activity, two new findings are presented. First, we observe hyperbolic dependence of PKS activity on MAT concentration, saturating at very low amounts (half-maximal rate at 19.7 +/- 5.1 nM). Since MAT can support PKS activity at less than 1/100 the typical concentration of the ACP and ketosynthase/chain length factor components, it is difficult to rule out the presence of trace quantities of MAT in a PKS reaction mixture. Second, an S97A mutant was constructed at the nucleophilic active site of the MAT. Not only can this mutant protein support PKS activity, it is also covalently labeled by [(14)C]malonyl-CoA, demonstrating that the serine nucleophile (which has been the target of PMSF inhibition in earlier studies) is dispensible for MAT activity in a Type II PKS system.  (+info)

Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme A:ACP transacylase (FabD). (6/346)

A DNA fragment containing the Pseudomonas aeruginosa fabD (encoding malonyl-coenzyme A [CoA]:acyl carrier protein [ACP] transacylase), fabG (encoding beta-ketoacyl-ACP reductase), acpP (encoding ACP), and fabF (encoding beta-ketoacyl-ACP synthase II) genes was cloned and sequenced. This fab gene cluster is delimited by the plsX (encoding a poorly understood enzyme of phospholipid metabolism) and pabC (encoding 4-amino-4-deoxychorismate lyase) genes; the fabF and pabC genes seem to be translationally coupled. The fabH gene (encoding beta-ketoacyl-ACP synthase III), which in most gram-negative bacteria is located between plsX and fabD, is absent from this gene cluster. A chromosomal temperature-sensitive fabD mutant was obtained by site-directed mutagenesis that resulted in a W258Q change. A chromosomal fabF insertion mutant was generated, and the resulting mutant strain contained substantially reduced levels of cis-vaccenic acid. Multiple attempts aimed at disruption of the chromosomal fabG gene were unsuccessful. We purified FabD as a hexahistidine fusion protein (H6-FabD) and ACP in its native form via an ACP-intein-chitin binding domain fusion protein, using a novel expression and purification scheme that should be applicable to ACP from other bacteria. Matrix-assisted laser desorption-ionization spectroscopy, native polyacrylamide electrophoresis, and amino-terminal sequencing revealed that (i) most of the purified ACP was properly modified with its 4'-phosphopantetheine functional group, (ii) it was not acylated, and (iii) the amino-terminal methionine was removed. In an in vitro system, purified ACP functioned as acyl acceptor and H(6)-FabD exhibited malonyl-CoA:ACP transacylase activity.  (+info)

Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase. (7/346)

BACKGROUND: Polyketide synthases (PKSs) are bacterial multienzyme systems that synthesize a broad range of natural products. The 'minimal' PKS consists of a ketosynthase, a chain length factor, an acyl carrier protein and a malonyl transferase. Auxiliary components (ketoreductases, aromatases and cyclases are involved in controlling the oxidation level and cyclization of the nascent polyketide chain. We describe the heterologous expression and reconstitution of several auxiliary PKS components including the actinorhodin ketoreductase (act KR), the griseusin aromatase/cyclase (gris ARO/CYC), and the tetracenomycin aromatase/cyclase (tcm ARO/CYC). RESULTS: The polyketide products of reconstituted act and tcm PKSs were identical to those identified in previous in vivo studies. Although stable protein-protein interactions were not detected between minimal and auxiliary PKS components, kinetic analysis revealed that the extended PKS comprised of the act minimal PKS, the act KR and the gris ARO/CYC had a higher turnover number than the act minimal PKS plus the act KR or the act minimal PKS alone. Adding the tcm ARO/CYC to the tcm minimal PKS also increased the overall rate. CONCLUSIONS: Until recently the principal strategy for functional analysis of PKS subunits was through heterologous expression of recombinant PKSs in Streptomyces. Our results corroborate the implicit assumption that the product isolated from whole-cell systems is the dominant product of the PKS. They also suggest that an intermediate is channeled between the various subunits, and pave the way for more detailed structural and mechanistic analysis of these multienzyme systems.  (+info)

Molecular cloning and nucleotide sequence of a gene encoding a cotton palmitoyl-acyl carrier protein thioesterase. (8/346)

A cotton genomic clone containing a 17.4-kb DNA segment was found to encompass a palmitoyl-acyl carrier protein (ACP) thioesterase (Fat B1) gene. The gene spans 3.6 kb with six exons and five introns, and is apparently the first plant FatB acyl-ACP thioesterase gene to be completely sequenced. The six exons are identical in nucleotide sequence to the open reading frame of the corresponding cDNA, and would encode a preprotein of 413 amino acids. The preprotein can clearly be identified as a FatB acyl-ACP thioesterase from its similarity to the deduced amino acid sequences of other FatB thioesterase preproteins. A 5'-flanking region of 914 bp was sequenced, with the potential TATA basal promoter 324 bp upstream from the ATG initiation codon. The 5'-flanking sequence also has a putative CAAT box and two presumptive basic region helixloop-helix (bHLH) elements with the consensus motif CANNTG (termed an E box), implicated as being a positive regulatory element in seed-specific gene expression.  (+info)

Acyl Carrier Protein (ACP) is a small, acidic protein that plays a crucial role in the fatty acid synthesis process. It functions as a cofactor by carrying acyl groups during the elongation cycles of fatty acid chains. The ACP molecule has a characteristic prosthetic group known as 4'-phosphopantetheine, to which the acyl groups get attached covalently. This protein is highly conserved across different species and is essential for the production of fatty acids in both prokaryotic and eukaryotic organisms.

Pantetheine is not a medical term per se, but it is a biochemical compound with relevance to medicine. Pantetheine is the alcohol form of pantothenic acid (vitamin B5), and it plays a crucial role in the metabolism of proteins, carbohydrates, and fats. It is a component of coenzyme A, which is involved in numerous biochemical reactions within the body.

Coenzyme A, containing pantetheine, participates in oxidation-reduction reactions, energy production, and the synthesis of various compounds, such as fatty acids, cholesterol, steroid hormones, and neurotransmitters. Therefore, pantetheine is essential for maintaining proper cellular function and overall health.

While there isn't a specific medical condition associated with pantetheine deficiency, ensuring adequate intake of vitamin B5 (through diet or supplementation) is vital for optimal health and well-being.

Fatty acid synthase type II (FASN2) is an alternative form of fatty acid synthase, which is a multi-functional enzyme complex responsible for the de novo synthesis of palmitate, a 16-carbon saturated fatty acid. In contrast to the classical type I fatty acid synthase (FASN), which is found in the cytoplasm and exists as a homodimer, FASN2 is localized in the mitochondria and consists of individual, monofunctional enzymes that catalyze each step of the fatty acid synthesis process.

The type II fatty acid synthase system includes several enzymes: acetyl-CoA carboxylase (ACC), which provides malonyl-CoA; 3-ketoacyl-CoA thiolase, which catalyzes the initial condensation of acetyl-CoA and malonyl-CoA to form acetoacetyl-CoA; 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (HAD), which catalyzes the reduction, dehydration, and isomerization of acetoacetyl-CoA to form hydroxybutyryl-CoA; 3-ketoacyl-CoA reductase, which reduces hydroxybutyryl-CoA to butyryl-CoA; and enoyl-CoA reductase (ECR), which catalyzes the final reduction of butyryl-CoA to palmitate.

FASN2 is involved in various cellular processes, including energy metabolism, lipid biosynthesis, and protein acetylation. Dysregulation of FASN2 has been implicated in several diseases, such as cancer, obesity, and neurodegenerative disorders.

Polyketide synthases (PKSs) are a type of large, multifunctional enzymes found in bacteria, fungi, and other organisms. They play a crucial role in the biosynthesis of polyketides, which are a diverse group of natural products with various biological activities, including antibiotic, antifungal, anticancer, and immunosuppressant properties.

PKSs are responsible for the assembly of polyketide chains by repetitively adding two-carbon units derived from acetyl-CoA or other extender units to a growing chain. The PKS enzymes can be classified into three types based on their domain organization and mechanism of action: type I, type II, and type III PKSs.

Type I PKSs are large, modular enzymes that contain multiple domains responsible for different steps in the polyketide biosynthesis process. These include acyltransferase (AT) domains that load extender units onto the PKS, acyl carrier proteins (ACPs) that tether the growing chain to the PKS, and ketosynthase (KS) domains that catalyze the condensation of the extender unit with the growing chain.

Type II PKSs are simpler enzymes that consist of several separate proteins that work together in a complex to synthesize polyketides. These include ketosynthase, acyltransferase, and acyl carrier protein domains, as well as other domains responsible for reducing or modifying the polyketide chain.

Type III PKSs are the simplest of the three types and consist of a single catalytic domain that is responsible for both loading extender units and catalyzing their condensation with the growing chain. These enzymes typically synthesize shorter polyketide chains, such as those found in certain plant hormones and pigments.

Overall, PKSs are important enzymes involved in the biosynthesis of a wide range of natural products with significant medical and industrial applications.

Acyl-Carrier Protein S-Malonyltransferase is an enzyme that plays a crucial role in the biosynthesis of fatty acids. The systematic name for this enzyme is 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH).

The enzyme catalyzes the following reaction:
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]

This reaction is part of the fatty acid synthase complex, which is responsible for the synthesis of long-chain fatty acids. The enzyme transfers a malonyl group from malonyl-CoA to an acyl carrier protein (ACP), which acts as a cofactor in the reaction. This transfer forms a malonyl-ACP, which is then used as a building block for the synthesis of fatty acids.

The enzyme is found in bacteria, plants, and animals, including humans. In humans, it is encoded by the MAT1A gene and is primarily located in the liver, where it plays a role in the production of palmitate, a 16-carbon saturated fatty acid that is an important precursor for the synthesis of other lipids.

Deficiencies in Acyl-Carrier Protein S-Malonyltransferase have been associated with various metabolic disorders, including cardiovascular disease and nonalcoholic fatty liver disease.

Fatty acid synthases (FAS) are a group of enzymes that are responsible for the synthesis of fatty acids in the body. They catalyze a series of reactions that convert acetyl-CoA and malonyl-CoA into longer chain fatty acids, which are then used for various purposes such as energy storage or membrane formation.

The human genome encodes two types of FAS: type I and type II. Type I FAS is a large multifunctional enzyme complex found in the cytoplasm of cells, while type II FAS consists of individual enzymes located in the mitochondria. Both types of FAS play important roles in lipid metabolism, but their regulation and expression differ depending on the tissue and physiological conditions.

Inhibition of FAS has been explored as a potential therapeutic strategy for various diseases, including cancer, obesity, and metabolic disorders. However, more research is needed to fully understand the complex mechanisms regulating FAS activity and its role in human health and disease.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Pantothenic Acid, also known as Vitamin B5, is a water-soluble vitamin that plays a vital role in the metabolism of proteins, carbohydrates, and fats. It is essential for the synthesis of coenzyme A (CoA), which is involved in various biochemical reactions in the body, including energy production, fatty acid synthesis, and cholesterol metabolism.

Pantothenic Acid is widely distributed in foods, including meat, poultry, fish, whole grains, legumes, and vegetables. Deficiency of this vitamin is rare but can lead to symptoms such as fatigue, irritability, sleep disturbances, muscle cramps, and gastrointestinal problems.

In addition to its role in metabolism, Pantothenic Acid also has potential benefits for wound healing, reducing inflammation, and supporting the immune system.

Carbon-sulfur ligases are a class of enzymes that catalyze the formation of carbon-sulfur bonds, which are covalent bonds between carbon and sulfur atoms. These enzymes play important roles in various biological processes, including the biosynthesis of cofactors, vitamins, and other organic compounds.

Carbon-sulfur ligases typically use ATP as an energy source to activate a sulfur atom, which is then transferred to a carbon atom in a substrate molecule. The resulting carbon-sulfur bond can be either thioether or thioester linkages, depending on the specific enzyme and reaction.

Examples of carbon-sulfur ligases include biotin synthase, lipoic acid synthase, and thiamine biosynthesis enzymes. These enzymes are essential for the function of various metabolic pathways and are therefore important targets for drug development and therapeutic intervention.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Thiol esters are chemical compounds that contain a sulfur atom (from a mercapto group, -SH) linked to a carbonyl group (a carbon double-bonded to an oxygen atom, -CO-) through an ester bond. Thiolester hydrolases are enzymes that catalyze the hydrolysis of thiol esters, breaking down these compounds into a carboxylic acid and a thiol (a compound containing a mercapto group).

In biological systems, thiolester bonds play important roles in various metabolic pathways. For example, acetyl-CoA, a crucial molecule in energy metabolism, is a thiol ester that forms between coenzyme A and an acetyl group. Thiolester hydrolases help regulate the formation and breakdown of these thiol esters, allowing cells to control various biochemical reactions.

Examples of thiolester hydrolases include:

1. CoA thioesterases (CoATEs): These enzymes hydrolyze thiol esters between coenzyme A and fatty acids, releasing free coenzyme A and a fatty acid. This process is essential for fatty acid metabolism.
2. Acetyl-CoA hydrolase: This enzyme specifically breaks down the thiol ester bond in acetyl-CoA, releasing acetic acid and coenzyme A.
3. Thioesterases involved in non-ribosomal peptide synthesis (NRPS): These enzymes hydrolyze thiol esters during the biosynthesis of complex peptides, allowing for the formation of unique amino acid sequences and structures.

Understanding the function and regulation of thiolester hydrolases can provide valuable insights into various metabolic processes and potential therapeutic targets in disease treatment.

Malonyl Coenzyme A (CoA) is not a medical term per se, but rather a biochemical concept. Here's the scientific or biochemical definition:

Malonyl Coenzyme A is an important intermediate in various metabolic pathways, particularly in fatty acid synthesis. It is formed through the reaction between malonic acid and coenzyme A, catalyzed by the enzyme acetyl-CoA carboxylase. Malonyl CoA plays a crucial role in the elongation step of fatty acid synthesis, where it provides the two-carbon unit that is added to a growing fatty acid chain.

In a medical context, understanding the function and regulation of Malonyl CoA metabolism can be relevant for several pathological conditions, including metabolic disorders like diabetes and obesity.

Triclosan is an antimicrobial agent that has been used in various consumer products, such as soaps, toothpastes, and cosmetics, to reduce or prevent bacterial contamination. It works by inhibiting the growth of bacteria and other microorganisms. The chemical formula for triclosan is 5-chloro-2-(2,4-dichlorophenoxy)phenol.

It's worth noting that in recent years, there has been some controversy surrounding the use of triclosan due to concerns about its potential health effects and environmental impact. Some studies have suggested that triclosan may interfere with hormone regulation and contribute to antibiotic resistance. As a result, the U.S. Food and Drug Administration (FDA) banned the use of triclosan in over-the-counter consumer antiseptic washes in 2016, citing concerns about its safety and effectiveness. However, it is still allowed in other products such as toothpaste.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Streptomyces is a genus of Gram-positive, aerobic, saprophytic bacteria that are widely distributed in soil, water, and decaying organic matter. They are known for their complex morphology, forming branching filaments called hyphae that can differentiate into long chains of spores.

Streptomyces species are particularly notable for their ability to produce a wide variety of bioactive secondary metabolites, including antibiotics, antifungals, and other therapeutic compounds. In fact, many important antibiotics such as streptomycin, neomycin, tetracycline, and erythromycin are derived from Streptomyces species.

Because of their industrial importance in the production of antibiotics and other bioactive compounds, Streptomyces have been extensively studied and are considered model organisms for the study of bacterial genetics, biochemistry, and ecology.

Cerulenin is a fungal metabolite that inhibits the enzyme delta-9-desaturase, which is involved in fatty acid synthesis. This compound is often used in research to study the biology and function of fatty acid synthase and lipid metabolism. It has been investigated for its potential as an anti-cancer agent, but its clinical use is not approved due to its limited specificity and potential toxicity.

"Saccharopolyspora" is a genus of Gram-positive, aerobic bacteria that forms branched hyphae and spores. These bacteria are known for their ability to produce various bioactive compounds, including antibiotics and enzymes. They are commonly found in soil, water, and decaying vegetation. One species of this genus, Saccharopolyspora erythraea (formerly known as Actinomyces erythreus), is the source of the antibiotic erythromycin.

It's important to note that "Saccharopolyspora" is a taxonomic category used in bacterial classification, and individual species within this genus may have different characteristics and medical relevance. Some species of Saccharopolyspora can cause infections in humans, particularly in immunocompromised individuals, but these are relatively rare.

If you're looking for information on a specific species of Saccharopolyspora or its medical relevance, I would need more context to provide a more detailed answer.

Apoproteins are the protein components of lipoprotein complexes, which are responsible for transporting fat molecules, such as cholesterol and triglycerides, throughout the body. Apoproteins play a crucial role in the metabolism of lipids by acting as recognition signals that allow lipoproteins to interact with specific receptors on cell surfaces.

There are several different types of apoproteins, each with distinct functions. For example, apolipoprotein A-1 (apoA-1) is the major protein component of high-density lipoproteins (HDL), which are responsible for transporting excess cholesterol from tissues to the liver for excretion. Apolipoprotein B (apoB) is a large apoprotein found in low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a). ApoB plays a critical role in the assembly and secretion of VLDL from the liver, and it also mediates the uptake of LDL by cells.

Abnormalities in apoprotein levels or function can contribute to the development of various diseases, including cardiovascular disease, diabetes, and Alzheimer's disease. Therefore, measuring apoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Acyl Coenzyme A (often abbreviated as Acetyl-CoA or Acyl-CoA) is a crucial molecule in metabolism, particularly in the breakdown and oxidation of fats and carbohydrates to produce energy. It is a thioester compound that consists of a fatty acid or an acetate group linked to coenzyme A through a sulfur atom.

Acyl CoA plays a central role in several metabolic pathways, including:

1. The citric acid cycle (Krebs cycle): In the mitochondria, Acyl-CoA is formed from the oxidation of fatty acids or the breakdown of certain amino acids. This Acyl-CoA then enters the citric acid cycle to produce high-energy electrons, which are used in the electron transport chain to generate ATP (adenosine triphosphate), the main energy currency of the cell.
2. Beta-oxidation: The breakdown of fatty acids occurs in the mitochondria through a process called beta-oxidation, where Acyl-CoA is sequentially broken down into smaller units, releasing acetyl-CoA, which then enters the citric acid cycle.
3. Ketogenesis: In times of low carbohydrate availability or during prolonged fasting, the liver can produce ketone bodies from acetyl-CoA to supply energy to other organs, such as the brain and heart.
4. Protein synthesis: Acyl-CoA is also involved in the modification of proteins by attaching fatty acid chains to them (a process called acetylation), which can influence protein function and stability.

In summary, Acyl Coenzyme A is a vital molecule in metabolism that connects various pathways related to energy production, fatty acid breakdown, and protein modification.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Anthraquinones are a type of organic compound that consists of an anthracene structure (a chemical compound made up of three benzene rings) with two carbonyl groups attached to the central ring. They are commonly found in various plants and have been used in medicine for their laxative properties. Some anthraquinones also exhibit antibacterial, antiviral, and anti-inflammatory activities. However, long-term use of anthraquinone-containing laxatives can lead to serious side effects such as electrolyte imbalances, muscle weakness, and liver damage.

'Coriandrum' is the medical term for a plant species that belongs to the family Apiaceae, also known as the carrot or parsley family. The most common and well-known member of this genus is Coriandrum sativum, which is commonly referred to as coriander or cilantro.

Coriander has been used for centuries in cooking and traditional medicine. Both its leaves and seeds have a distinct aroma and flavor that are widely used in various cuisines around the world. The leaves are often called cilantro, especially in North America, while the seeds are known as coriander.

In addition to its culinary uses, coriander has been reported to possess several medicinal properties. It has been traditionally used to treat digestive disorders such as nausea, bloating, and flatulence. Some studies suggest that coriander may have antimicrobial, anti-inflammatory, and antioxidant effects, although more research is needed to confirm these potential benefits.

It's worth noting that while 'Coriandrum' is a medical term for the plant genus, it is not typically used in clinical or medical contexts unless discussing its medicinal properties or potential therapeutic applications.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Acyl-Carrier Protein (ACP) S-Acetyltransferase is an enzyme that plays a crucial role in the initiation and elongation steps of fatty acid synthesis. This enzyme catalyzes the transfer of an acetyl group from acetyl-CoA to the sulfhydryl group of the acyl carrier protein (ACP). The reaction can be summarized as follows:

acetyl-CoA + ACP → CoA + ACP-S-acetyl

The ACP-S-acetyl is then used as a starter molecule for the synthesis of fatty acids through a series of reactions involving other enzymes in the fatty acid synthase complex. The formation of ACP-S-acetyl is the first and rate-limiting step in fatty acid biosynthesis, making ACP S-acetyltransferase an essential regulator of this metabolic pathway. Inhibition of this enzyme has been explored as a potential therapeutic strategy for treating diseases associated with aberrant lipid metabolism, such as obesity and diabetes.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

"Malonates" is not a recognized medical term. However, in chemistry, malonates refer to salts or esters of malonic acid, a dicarboxylic acid with the formula CH2(COOH)2. Malonic acid and its derivatives have been used in the synthesis of various pharmaceuticals and chemicals, but they are not typically associated with any specific medical condition or treatment. If you have encountered the term "malonates" in a medical context, it may be helpful to provide more information or seek clarification from the source.

Thioctic acid is also known as alpha-lipoic acid. It is a vitamin-like chemical compound that is made naturally in the body and is found in small amounts in some foods like spinach, broccoli, and potatoes. Thioctic acid is an antioxidant that helps to protect cells from damage caused by free radicals. It also plays a role in energy production in the cells and has been studied for its potential benefits in the treatment of diabetes and nerve-related symptoms of diabetes such as pain, burning, itching, and numbness. Thioctic acid is available as a dietary supplement.

Medical Definition: Thioctic acid (also known as alpha-lipoic acid) is a vitamin-like antioxidant that is made naturally in the body and is found in small amounts in some foods. It plays a role in energy production in the cells, and has been studied for its potential benefits in the treatment of diabetes and nerve-related symptoms of diabetes such as pain, burning, itching, and numbness. Thioctic acid is also available as a dietary supplement.

Lipid A is the biologically active component of lipopolysaccharides (LPS), which are found in the outer membrane of Gram-negative bacteria. It is responsible for the endotoxic activity of LPS and plays a crucial role in the pathogenesis of gram-negative bacterial infections. Lipid A is a glycophosphatidylinositol (GPI) anchor, consisting of a glucosamine disaccharide backbone with multiple fatty acid chains and phosphate groups attached to it. It can induce the release of proinflammatory cytokines, fever, and other symptoms associated with sepsis when introduced into the bloodstream.

Naphthacenes are hydrocarbon compounds that consist of a naphthalene ring fused to two additional benzene rings. They belong to the class of polycyclic aromatic hydrocarbons (PAHs) and have been studied for their potential carcinogenic properties. Naphthacenes can be found in various environmental sources, including air pollution from vehicle emissions and cigarette smoke. However, it's important to note that specific medical definitions related to diseases or conditions are not typically associated with naphthacenes.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Peptide synthases are a group of enzymes that catalyze the formation of peptide bonds between specific amino acids to produce peptides or proteins. They are responsible for the biosynthesis of many natural products, including antibiotics, bacterial toxins, and immunomodulatory peptides.

Peptide synthases are large, complex enzymes that consist of multiple domains and modules, each of which is responsible for activating and condensing specific amino acids. The activation of amino acids involves the formation of an aminoacyl-adenylate intermediate, followed by transfer of the activated amino acid to a thiol group on the enzyme. The condensation of two activated amino acids results in the formation of a peptide bond and release of adenosine monophosphate (AMP) and pyrophosphate.

Peptide synthases are found in all three domains of life, but are most commonly associated with bacteria and fungi. They play important roles in the biosynthesis of many natural products that have therapeutic potential, making them targets for drug discovery and development.

Acetyl Coenzyme A, often abbreviated as Acetyl-CoA, is a key molecule in metabolism, particularly in the breakdown and oxidation of carbohydrates, fats, and proteins to produce energy. It is a coenzyme that plays a central role in the cellular process of transforming the energy stored in the chemical bonds of nutrients into a form that the cell can use.

Acetyl-CoA consists of an acetyl group (two carbon atoms) linked to coenzyme A, a complex organic molecule. This linkage is facilitated by an enzyme called acetyltransferase. Once formed, Acetyl-CoA can enter various metabolic pathways. In the citric acid cycle (also known as the Krebs cycle), Acetyl-CoA is further oxidized to release energy in the form of ATP, NADH, and FADH2, which are used in other cellular processes. Additionally, Acetyl-CoA is involved in the biosynthesis of fatty acids, cholesterol, and certain amino acids.

In summary, Acetyl Coenzyme A is a vital molecule in metabolism that connects various biochemical pathways for energy production and biosynthesis.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

"Vibrio" is a genus of Gram-negative, facultatively anaerobic, curved-rod bacteria that are commonly found in marine and freshwater environments. Some species of Vibrio can cause diseases in humans, the most notable being Vibrio cholerae, which is the causative agent of cholera, a severe diarrheal illness. Other pathogenic species include Vibrio vulnificus and Vibrio parahaemolyticus, which can cause gastrointestinal or wound infections. These bacteria are often transmitted through contaminated food or water and can lead to serious health complications, particularly in individuals with weakened immune systems.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

A carrier state is a condition in which a person carries and may be able to transmit a genetic disorder or infectious disease, but does not show any symptoms of the disease themselves. This occurs when an individual has a recessive allele for a genetic disorder or is infected with a pathogen, but does not have the necessary combination of genes or other factors required to develop the full-blown disease.

For example, in the case of cystic fibrosis, which is caused by mutations in the CFTR gene, a person who carries one normal allele and one mutated allele for the disease is considered a carrier. They do not have symptoms of cystic fibrosis themselves, but they can pass the mutated allele on to their offspring, who may then develop the disease if they inherit the mutation from both parents.

Similarly, in the case of infectious diseases, a person who is infected with a pathogen but does not show any symptoms may still be able to transmit the infection to others. This is known as being an asymptomatic carrier or a healthy carrier. For example, some people who are infected with hepatitis B virus (HBV) may not develop any symptoms of liver disease, but they can still transmit the virus to others through contact with their blood or other bodily fluids.

It's important to note that in some cases, carriers of certain genetic disorders or infectious diseases may have mild or atypical symptoms that do not meet the full criteria for a diagnosis of the disease. In these cases, they may be considered to have a "reduced penetrance" or "incomplete expression" of the disorder or infection.

A multigene family is a group of genetically related genes that share a common ancestry and have similar sequences or structures. These genes are arranged in clusters on a chromosome and often encode proteins with similar functions. They can arise through various mechanisms, including gene duplication, recombination, and transposition. Multigene families play crucial roles in many biological processes, such as development, immunity, and metabolism. Examples of multigene families include the globin genes involved in oxygen transport, the immune system's major histocompatibility complex (MHC) genes, and the cytochrome P450 genes associated with drug metabolism.

A genetic complementation test is a laboratory procedure used in molecular genetics to determine whether two mutated genes can complement each other's function, indicating that they are located at different loci and represent separate alleles. This test involves introducing a normal or wild-type copy of one gene into a cell containing a mutant version of the same gene, and then observing whether the presence of the normal gene restores the normal function of the mutated gene. If the introduction of the normal gene results in the restoration of the normal phenotype, it suggests that the two genes are located at different loci and can complement each other's function. However, if the introduction of the normal gene does not restore the normal phenotype, it suggests that the two genes are located at the same locus and represent different alleles of the same gene. This test is commonly used to map genes and identify genetic interactions in a variety of organisms, including bacteria, yeast, and animals.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Nuclear Magnetic Resonance (NMR) Biomolecular is a research technique that uses magnetic fields and radio waves to study the structure and dynamics of biological molecules, such as proteins and nucleic acids. This technique measures the magnetic properties of atomic nuclei within these molecules, specifically their spin, which can be influenced by the application of an external magnetic field.

When a sample is placed in a strong magnetic field, the nuclei absorb and emit electromagnetic radiation at specific frequencies, known as resonance frequencies, which are determined by the molecular structure and environment of the nuclei. By analyzing these resonance frequencies and their interactions, researchers can obtain detailed information about the three-dimensional structure, dynamics, and interactions of biomolecules.

NMR spectroscopy is a non-destructive technique that allows for the study of biological molecules in solution, which makes it an important tool for understanding the function and behavior of these molecules in their natural environment. Additionally, NMR can be used to study the effects of drugs, ligands, and other small molecules on biomolecular structure and dynamics, making it a valuable tool in drug discovery and development.

Macrolides are a class of antibiotics derived from natural products obtained from various species of Streptomyces bacteria. They have a large ring structure consisting of 12, 14, or 15 atoms, to which one or more sugar molecules are attached. Macrolides inhibit bacterial protein synthesis by binding to the 50S ribosomal subunit, thereby preventing peptide bond formation. Common examples of macrolides include erythromycin, azithromycin, and clarithromycin. They are primarily used to treat respiratory, skin, and soft tissue infections caused by susceptible gram-positive and gram-negative bacteria.

Mycolic acids are complex, long-chain fatty acids that are a major component of the cell wall in mycobacteria, including the bacteria responsible for tuberculosis and leprosy. These acids contribute to the impermeability and resistance to chemical agents of the mycobacterial cell wall, making these organisms difficult to eradicate. Mycolic acids are unique to mycobacteria and some related actinomycetes, and their analysis can be useful in the identification and classification of these bacteria.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

Polyketides are a diverse group of natural compounds that are synthesized biochemically through the condensation of acetate or propionate units. They are produced by various organisms, including bacteria, fungi, and plants, and have a wide range of biological activities, such as antibiotic, antifungal, anticancer, and immunosuppressant properties. Polyketides can be classified into several types based on the number of carbonyl groups, the length of the carbon chain, and the presence or absence of cyclization. They are synthesized by polyketide synthases (PKSs), which are large enzyme complexes that share similarities with fatty acid synthases (FASs). Polyketides have attracted significant interest in drug discovery due to their structural diversity and potential therapeutic applications.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

Glycerol-3-Phosphate O-Acyltransferase (GPAT) is an enzyme that plays a crucial role in the biosynthesis of triacylglycerols and phospholipids, which are major components of cellular membranes and energy storage molecules. The GPAT enzyme catalyzes the initial and rate-limiting step in the glycerolipid synthesis pathway, specifically the transfer of an acyl group from an acyl-CoA donor to the sn-1 position of glycerol-3-phosphate, forming lysophosphatidic acid (LPA). This reaction is essential for the production of various glycerolipids, including phosphatidic acid, diacylglycerol, and triacylglycerol. There are four isoforms of GPAT (GPAT1-4) in humans, each with distinct subcellular localizations and functions. Dysregulation of GPAT activity has been implicated in several pathological conditions, such as metabolic disorders, cardiovascular diseases, and cancers.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

'Brassica' is a term used in botanical nomenclature, specifically within the family Brassicaceae. It refers to a genus of plants that includes various vegetables such as broccoli, cabbage, cauliflower, kale, and mustard greens. These plants are known for their nutritional value and health benefits. They contain glucosinolates, which have been studied for their potential anti-cancer properties. However, it is not a medical term per se, but rather a taxonomic category used in the biological sciences.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.

Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).

In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.

Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.

Esters are organic compounds that are formed by the reaction between an alcohol and a carboxylic acid. They are widely found in nature and are used in various industries, including the production of perfumes, flavors, and pharmaceuticals. In the context of medical definitions, esters may be mentioned in relation to their use as excipients in medications or in discussions of organic chemistry and biochemistry. Esters can also be found in various natural substances such as fats and oils, which are triesters of glycerol and fatty acids.

"Streptomyces coelicolor" is a species name for a type of bacteria that belongs to the genus Streptomyces. This bacterium is gram-positive, meaning that it stains positive in the Gram stain test, which is used to classify bacteria based on their cell wall structure. It is an aerobic organism, which means it requires oxygen to grow and survive.

Streptomyces coelicolor is known for its ability to produce a variety of antibiotics, including actinomycin and undecylprodigiosin. These antibiotics have been studied for their potential therapeutic uses in medicine. The bacterium also produces a blue-pigmented compound called pigmentactinorhodin, which it uses to protect itself from other microorganisms.

Streptomyces coelicolor is widely used as a model organism in research due to its genetic tractability and its ability to produce a diverse array of secondary metabolites. Scientists study the genetics, biochemistry, and ecology of this bacterium to better understand how it produces antibiotics and other bioactive compounds, and how these processes can be harnessed for industrial and medical applications.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Chloroplasts are specialized organelles found in the cells of green plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy from the sun into chemical energy in the form of organic compounds, such as glucose.

Chloroplasts contain the pigment chlorophyll, which absorbs light energy from the sun. They also contain a system of membranes and enzymes that convert carbon dioxide and water into glucose and oxygen through a series of chemical reactions known as the Calvin cycle. This process not only provides energy for the organism but also releases oxygen as a byproduct, which is essential for the survival of most life forms on Earth.

Chloroplasts are believed to have originated from ancient cyanobacteria that were engulfed by early eukaryotic cells and eventually became integrated into their host's cellular machinery through a process called endosymbiosis. Over time, chloroplasts evolved to become an essential component of plant and algal cells, contributing to their ability to carry out photosynthesis and thrive in a wide range of environments.

4'-Phosphopantetheine is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty ... The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. It is one of the most ... the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). Cronan ... Acyl Carrier Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short description ...
The enzyme [acyl-carrier-protein] phosphodiesterase (EC catalyzes the reaction holo-[acyl-carrier-protein] + H2O ⇌ {\ ... Vagelos PR, Larrabes AR (1967). "Acyl carrier protein. IX. Acyl carrier protein hydrolase". J. Biol. Chem. 242 (8): 1776-81. ... The systematic name is holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. Other names in common use include ACP ... Thomas J, Cronan JE (2005). "The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and ...
... dodecanoyl-acyl-carrier-protein hydrolase, dodecyl-acyl-carrier protein hydrolase, and dodecanoyl-[acyl-carrier protein] ... The enzyme dodecanoyl-[acyl-carrier-protein] hydrolase (EC catalyzes the reaction a dodecanoyl-[acyl-carrier-protein ... acyl-carrier-protein] hydrolase. Other names in common use include lauryl-acyl-carrier-protein hydrolase, ... acyl-carrier-protein] + dodecanoate This enzyme belongs to the family of hydrolases, specifically those acting on thioester ...
Other names in common use include acyl-[acyl-carrier-protein] hydrolase, acyl-ACP-hydrolase, acyl-acyl carrier protein ... The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins". Arch. Biochem. ... The enzyme oleoyl-[acyl-carrier-protein] hydrolase (EC catalyzes the reaction an oleoyl-[acyl-carrier-protein] + H2O ... The systematic name is oleoyl-[acyl-carrier-protein] hydrolase. ... acyl-carrier-protein] + oleate This enzyme belongs to the ...
... acyl carrier protein synthetase (ACPS), PPTase, acyl carrier protein synthase, P-pant transferase, and CoA:apo-[acyl-carrier- ... Elovson J, Vagelos PR (July 1968). "Acyl carrier protein. X. Acyl carrier protein synthetase". The Journal of Biological ... Acyl Carrier Protein):Holo-(Acyl Carrier Protein) Synthase Complex". Journal of Molecular Biology. 429 (23): 3763-3775. doi: ... apo-acyl carrier protein ⇌ {\displaystyle \rightleftharpoons } adenosine 3',5'-bisphosphate + holo-acyl carrier protein This ...
Schultz, D; Suh, M.; Ohlrogge (2000). "Stearoyl-Acyl Carrier Protein and Unusual Acyl-Acyl Carrier Protein Desaturase ... acyl-carrier-protein] + acceptor + 2 H2O The systematic name of this enzyme class is acyl-[acyl-carrier-protein], hydrogen- ... acyl-carrier-protein), reduced acceptor, and O2, whereas its 3 products are oleoyl-(acyl-carrier-protein), acceptor, and H2O. ... acyl-carrier-protein] desaturase (EC is an enzyme that catalyzes the chemical reaction stearoyl-[acyl-carrier- ...
... acyl-carrier-protein] hydro-lyase, beta-hydroxybutyryl acyl carrier protein dehydrase, beta-hydroxybutyryl acyl carrier protein ... beta-hydroxybutyryl acyl carrier protein dehydrase, enoyl acyl carrier protein hydrase, crotonyl acyl carrier protein hydratase ... MAJERUS PW, ALBERTS AW, VAGELOS PR (1965). "ACYL CARRIER PROTEIN. 3. AN ENOYL HYDRASE SPECIFIC FOR ACYL CARRIER PROTEIN ... acyl-carrier-protein]]], and two products, [[but-2-enoyl-[acyl-carrier-protein]]] and H2O. This enzyme belongs to the family of ...
Enoyl-(acyl-carrier-protein) reductase (NADPH, A-specific) Enoyl-(acyl-carrier-protein) reductase (NADPH, B-specific) Cis-2- ... Enoyl-acyl carrier protein reductase (or ENR) (EC, is a key enzyme of the type II fatty acid synthesis (FAS) system. ... acyl-carrier protein) reductase from Plasmodium falciparum". The Biochemical Journal. 381 (Pt 3): 735-41. doi:10.1042/ ... "Identification and characterization of inhibitors of bacterial enoyl-acyl carrier protein reductase". Antimicrobial Agents and ...
... 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. Other names in common use include acetyl coenzyme A-acyl-carrier-protein ... In enzymology, a [acyl-carrier-protein] S-acetyltransferase (EC is an enzyme that catalyzes the reversible chemical ... Rangan VS, Smith S (1997). "Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S- ...
... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] The transfer of malonate to acyl-carrier-protein (ACP) converts the ... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] Thus, the two substrates of this enzyme are malonyl-CoA and acyl ... Other names in common use include malonyl coenzyme A-acyl carrier protein transacylase, [acyl carrier protein] ... carrier protein, whereas its two products are CoA and malonyl-acyl-carrier-protein. This enzyme belongs to the family of ...
... acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase ... Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP ... beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, 3-ketoacyl ACP reductase, NADPH- ... acyl-carrier-protein](ACP) + NADPH + H+ ⇌ {\displaystyle \rightleftharpoons } (3R)-3-hydroxyacyl-[acyl-carrier-protein](ACP) + ...
... acyl-carrier protein] dehydratase, 3-hydroxydecanoyl-acyl carrier protein dehydrase, 3-hydroxydecanoyl-acyl carrier protein ... acyl-carrier-protein] hydro-lyase) is an enzyme with systematic name (3R)-3-hydroxydecanoyl-(acyl-carrier protein) hydro-lyase ... acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } a trans-dec-2-enoyl-[acyl-carrier protein] + H2O (2) a (3R)-3- ... acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } a cis-dec-3-enoyl-[acyl-carrier protein] + H2O This enzyme is ...
... acyl-carrier-protein) synthase (EC is an enzyme with systematic name octanoyl-CoA:malonyl-(acyl-carrier protein) C- ... acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2 This enzyme is ... Beta-ketodecanoyl-(acyl-carrier-protein)+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ...
... acyl carrier protein] dehydratase, D-3-hydroxyoctanoyl-acyl carrier protein dehydratase, beta-hydroxyoctanoyl-acyl carrier ... acyl-carrier-protein] hydro-lyase (oct-2-enoyl-[acyl-carrier protein]-forming). Other names in common use include D-3- ... acyl-carrier-protein] hydro-lyase. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase Mizugaki M, Swindell AC, Wakil SJ ( ... acyl-carrier-protein] dehydratase (EC catalyzes the chemical reaction (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein ...
... acyl-carrier-protein] hydro-lyase (hexadec-2-enoyl-[acyl-carrier protein]-forming). Other names in common use include D-3- ... acyl-carrier-protein]]], and two products, [[hexadec-2-enoyl-[acyl-carrier-protein]]] and H2O. This enzyme belongs to the ... acyl-carrier-protein] ⇌ {\displaystyle \rightleftharpoons } hexadec-2-enoyl-[acyl-carrier-protein] + H2O Hence, this enzyme has ... acyl-carrier-protein] dehydratase, beta-hydroxypalmitoyl-acyl carrier protein dehydrase, beta-hydroxypalmitoyl thioester ...
... (EC, [BtrI acyl-carrier protein]-L-glutamate ligase, BtrJ) is an ... BtrI acyl-carrier protein] (2) ATP + L-glutamate + 4-amino butanoyl-[BtrI acyl-carrier protein] ⇌ {\displaystyle \ ... butirosin+acyl-carrier+protein)-L-glutamate+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... BtrI acyl-carrier protein] This enzyme catalyses two steps in the biosynthesis of the side chain of the aminoglycoside ...
... acyl-carrier-protein]]], and one product, [[cis-dec-3-enoyl-[acyl-carrier-protein]]]. This enzyme belongs to the family of ... acyl-carrier-protein] ⇌ {\displaystyle \rightleftharpoons } cis-dec-3-enoyl-[acyl-carrier-protein] Hence, this enzyme has one ... The systematic name of this enzyme class is decenoyl-[acyl-carrier-protein] Delta2-trans-Delta3-cis-isomerase. Other names in ... In enzymology, a trans-2-decenoyl-[acyl-carrier protein] isomerase (EC is an enzyme that catalyzes the chemical ...
... acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine ⇌ {\displaystyle \rightleftharpoons } [acyl-carrier protein ... The systematic name of this enzyme class is acyl-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O- ... Other names in common use include acyl-[acyl-carrier, protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine, and O- ... the two substrates of this enzyme are acyl-acyl-carrier protein and O-(2-acyl-sn-glycero-3-phospho)ethanolamine, whereas its ...
... acyl-carrier protein] + diphosphate The delta subunit of malonate decarboxylase serves as an acyl-carrier protein (ACP) . ... Malonate+decarboxylase+holo-(acyl-carrier+protein)+synthase at the U.S. National Library of Medicine Medical Subject Headings ( ... Malonate decarboxylase holo-(acyl-carrier protein) synthase (EC, holo ACP synthase, '2'-(5''-triphosphoribosyl)-3'- ... acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } malonate decarboxylase holo-[ ...
BtrI acyl-carrier protein] ⇌ {\displaystyle \rightleftharpoons } 4-amino butanoyl-[BtrI acyl-carrier protein] + CO2 This enzyme ... BtrI acyl-carrier protein) decarboxylase (EC, btrK (gene)) is an enzyme with systematic name L-glutamyl-(BtrI acyl- ... L-glutamyl-(BtrI+acyl-carrier+protein)+decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... possible protective-group chemistry in an acyl carrier protein-mediated pathway". Chemistry & Biology. 12 (6): 665-75. doi: ...
... (EC, long-chain acyl-[acp] reductase, fatty acyl-[acyl-carrier- ... acyl-carrier protein + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+ ... acyl-[acp] reductase) is an enzyme with systematic name long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-(acyl-carrier protein ... Long-chain+acyl-(acyl-carrier-protein)+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ...
... acyl-carrier-protein] + NADH + H+ Thus, the two substrates of this enzyme are [[(3R)-3-hydroxyacyl-[acyl-carrier-protein]]] and ... acyl-carrier-protein]:NAD+ oxidoreductase. Other names in common use include 3-oxoacyl-[acyl carrier protein] (reduced ... In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) (EC is an enzyme that catalyzes the chemical ... acyl-carrier-protein]]], NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the ...
... acyl-carrier protein] methyl ester esterase (EC, BioH; systematic name pimelyl-[acyl-carrier protein] methyl ester ... acyl-carrier protein] methyl ester + H2O ⇌ {\displaystyle \rightleftharpoons } pimelyl-[acyl-carrier protein] + methanol This ... Pimelyl-(acyl-carrier+protein)+methyl+ester+esterase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ... "Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway". FEBS Letters. 513 (2-3): 299-304. ...
... acyl-carrier-protein] + NADPH + H+ Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, ... enoyl acyl-carrier-protein reductase, enoyl-ACP reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). This ... acyl-carrier-protein] reductase (NADPH, B-specific) (EC is an enzyme that catalyzes the chemical reaction acyl-[acyl- ... The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific). Other names in ...
... acyl-carrier-protein] + NADPH + H+ Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP+, ... acyl-carrier-protein] reductase (NADPH, A-specific) (EC is an enzyme that catalyzes the chemical reaction acyl-[acyl- ... acyl-carrier-protein]:NADP+ oxidoreductase (A-specific). Other names in common use include acyl-ACP dehydrogenase, enoyl-[acyl ... acyl-carrier-protein]]], NADPH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on ...
... acyl-carrier-protein] synthetase, acyl-[acyl carrier protein] synthetase, acyl-ACP synthetase, acyl-[acyl-carrier-protein] ... acyl-[acyl-carrier-protein] The 3 substrates of this enzyme are ATP, acid, and acyl-carrier-protein, whereas its 3 products are ... "Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein ... acyl-carrier-protein] ligase (EC is an enzyme that catalyzes the chemical reaction ATP + an acid + [acyl-carrier- ...
3-hydroxytetradecanoyl-acyl-carrier-protein and UDP-N-acetylglucosamine, whereas its two products are acyl-carrier-protein and ... acyl-carrier-protein] + UDP-N-acetylglucosamine ⇌ {\displaystyle \rightleftharpoons } [acyl-carrier-protein] + UDP-3-O-(3- ... In enzymology, an acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (EC is an enzyme that ... The systematic name of this enzyme class is (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3- ...
BtrI acyl-carrier protein] + FMN + H2O 4-(gamma-L-glutamylamino)butanoyl-(BtrI acyl-carrier protein) monooxygenase catalyses a ... 4-(gamma-L-glutamylamino)butanoyl-(BtrI acyl-carrier protein) monooxygenase (EC, btrO (gene)) is an enzyme with ... 4-(gamma-L-glutamylamino)butanoyl-(BtrI+acyl-carrier+protein)+monooxygenase at the U.S. National Library of Medicine Medical ... BtrI acyl-carrier protein),FMN:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction 4 ...
BtrI acyl-carrier protein] + ribostamycin ⇌ {\displaystyle \rightleftharpoons } gamma-L-glutamyl-butirosin B + BtrI acyl- ... Ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-(BtrI acyl-carrier protein) 4-(gamma-L-glutamylamino)-(S)-2- ... Ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-(BtrI+acyl-carrier+protein)+4-(gamma-L-glutamylamino)-(S)-2- ... BtrI acyl-carrier protein) 4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoate transferase. This enzyme catalyses the following ...
Fatty acid synthase Pantothenic acid Elovson J, Vagelos PR (July 1968). "Acyl carrier protein. X. Acyl carrier protein ... is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs ... the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). It is ... Subsequent to the expression of the apo acyl carrier protein, 4'-phosphopantetheine moiety is attached to a serine residue. The ...
4-Phosphopantetheine is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty ... The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. It is one of the most ... the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). Cronan ... Acyl Carrier Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH) (Articles with short description ...
3-oxoacyl-[acyl-carrier-protein] reductase. A, B. 249. Rickettsia prowazekii. Mutation(s): 0 Gene Names: fabG, RP762. EC: 1.1. ... Here, the structure of the third enzyme in the FAS pathway, 3-ketoacyl-(acyl-carrier-protein) reductase, is reported at a ... Structure of 3-ketoacyl-(acyl-carrier-protein) reductase from Rickettsia prowazekii at 2.25 A resolution.. Subramanian, S., ... Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase Rickettsia prowazekii. *PDB DOI: ...
Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K- ... wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary ... knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound ...
... acyl-carrier-protein) reductase (FabG)(Y155F) from Vibrio cholerae ... 3-oxoacyl-[acyl-carrier protein] reductase. A, B, C, D. 251. Vibrio cholerae MJ-1236. Mutation(s): 1 Gene Names: VC2021, VCD_ ... β-Ketoacyl-(acyl carrier protein) reductase (FabG) catalyzes the key reductive reaction in the elongation cycle of fatty acid ... β-Ketoacyl-(acyl carrier protein) reductase (FabG) catalyzes the key reductive reaction in the elongation cycle of fatty acid ...
... proteins are critical components of fatty acid and polyketide biosynthesis. Their primary function is to shuttle intermediates ... acyl. carrier protein. labeling G. Prasad, J. W. Amoroso, L. S. Borketey and N. A. Schnarr, Org. Biomol. Chem., 2012, 10, 1992 ... Acyl. carrier proteins. are critical components of fatty acid. and polyketide. biosynthesis. Their primary function is to ... acyl. carrier proteins. is demonstrated indicating that only the phosphopantetheine. -. thiol. is modified. Incorporation of an ...
... acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein] ... 3-oxo-decanoyl-[acyl-carrier protein], 3-oxodecanoyl-[acyl-carrier-protein], a 3-oxodecanoyl-[acyl-carrier protein] ... octanoyl-CoA + malonyl-[acyl-carrier protein] = 3-oxo-decanoyl-[acyl-carrier protein] + CoA + CO2 ... octanoyl-CoA + malonyl-[acyl-carrier protein] = 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2 ...
An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the ... Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)*Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) ... Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in this website by year, and whether "Enoyl-(Acyl-Carrier ... "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" is a descriptor in the National Library of Medicines controlled ...
The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the ... acyl-[acyl-carrier-protein] 4-desaturase Alternative Name(s). Delta(4)-palmitoyl-[acyl carrier protein] desaturase. ...
a (3R)-hydroxyacyl-[ACP] + NAD(+) <=> a 3-oxoacyl-[ACP] + H(+) + ...
... ... Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52(30 ... Acyl hydrolase (AH) domains are a common feature of trans-AT PKSs. They have been hypothesised to perform a proofreading ... This study determines the substrate tolerance of the AH PedC for a range of acyl-ACPs. Clear preference towards short, linear ...
... acyl-carrier-protein) reductase to get latest updates from 3-oxoacyl-(acyl-carrier-protein) reductase ... acyl-carrier-protein) reductase is on Rediff pages, ,Follow 3-oxoacyl-( ... beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, NADPH-specific 3-oxoacyl-reductase, ... to get instant updates about 3-Oxoacyl-(Acyl-Carrier-Protein) Reductase on your MyPage. Meet other similar minded people. Its ...
... acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. ... acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein ... acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. ... 3-oxoacyl-[acyl-carrier-protein] synthase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO_0004315]. Catalysis ...
... enoyl acyl carrier protein hydrase怎麽讀,enoyl acyl carrier protein hydrase的發音是什麽可 ... enoyl acyl carrier protein hydrase的發音讀音, ... acyl 的發音 *carrier 的發音 *protein 的發音 *hydrase 的發音 ... enoyl acyl
PPR proteins represent the most frequent protein class among identified Rfs and they exhibit ideal characteristics to evolve ... PPR proteins represent the most frequent protein class among identified Rfs and they exhibit ideal characteristics to evolve ... Here, we review the literature that highlights those characteristics and help explain why PPR proteins are ideal for the roles ... Here, we review the literature that highlights those characteristics and help explain why PPR proteins are ideal for the roles ...
In the strain naturally expressing the SprG1 toxin, cytoplasmic proteins are excreted into the medium, but this is not due to ... Such a toxin-driven release of the cytoplasmic proteins may modulate the host inflammatory response that, in turn, could ... Comparison of intracellular proteomes among the strains points to the SprF1 antitoxin as moderately downregulating protein ... for the three proteins (6,7-dimethyl-8-ribityllumazine synthase, RibH; 3-hydroxyacyl-(acyl-carrier-protein) dehydratase, FabZ; ...
... acyl-carrier-protein] synthase III. Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /NCTC 11857 / SLCC ... Beta-ketoacyl-[acyl-carrier-protein] synthase III UniProtKBInterProSTRINGInteractive Modelling. 312 aa; Sequence (Fasta) ; 1 ...
acyl-(acyl-carrier-protein)desaturase Associated data * GENBANK/L01418 * GENBANK/L26296 * GENBANK/M87514 ... Mature pollen grains of Brassica napus are shown to contain three major acyl lipid pools as follows: (i) the extracellular ... these lipid classes during pollen maturation and the expression patterns of several lipid biosynthetic genes and their protein ...
Acyl-Carrier-Protein) Reductase ... The Oxford Protein Production Facility, Division of Structural ... Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution. ... Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution. ... Bacillus anthracis, Alcohol Oxidoreductases, DNA Primers, Crystallography, X-Ray, Amino Acid Sequence, Base Sequence, Protein ...
BtrI acyl-carrier protein] + ribostamycin = gamma-L-glutamyl-butirosin B + BtrI acyl-carrier protein [RN:R08909]. ... ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(gamma-L-glutamylamino)-(S)-2- ... ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(gamma-L-glutamylamino)-(S)-2- ... 4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein];. ribostamycin [CPD:C01759]. ...
Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene. ... Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan. Biochemistry ... attributable to binding to the active site of enoyl-acyl carrier protein reductase (217,218). ... Hospital outbreak of infections with group a streptococci traced to an asymptomatic anal carrier. N Engl J Med 1969;280:1224--5 ...
Protein Acyl carrier protein [47338] (7 species). *. Species Escherichia coli [TaxId:562] [47339] (26 PDB entries). Uniprot ... Class a: All alpha proteins [46456] (290 folds). *. Fold a.28: Acyl carrier protein-like [47335] (3 superfamilies). 4 helices, ... Family a.28.1.1: Acyl-carrier protein (ACP) [47337] (7 proteins). *. ... PDB Compounds: (B:) Acyl carrier protein. SCOPe Domain Sequences for d2fadb_:. Sequence; same for both SEQRES and ATOM records ...
3-oxoacyl-[acyl-carrier-protein] reductase ??? RM. AspP4ORF10230P (85% identity) AspP3ORF8695P. 8700 regulator ...
Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. J. Biol. Chem. ... Inhibition of β-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism. J. Biol. Chem ... Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat. Methods 3: 429-438.. Pellois JP, Muir ... Protein engineering and the development of generic biosensors. Trends Biotech. 16: 183-189.. Liu H, Schmidt JJ, Bachand GD, et ...
PA is a part of the CoA and acyl carrier protein of fatty acid synthase in many metabolic pathways. Maternal PA deficiency ... Transcriptome Profile Based on Protein-Protein Interaction Networks Provides a Set of Core Genes for Understanding the ... Ott, T. L., Mirando, M. A., Davis, M. A. & Bazer, F. W. Effects of ovine conceptus secretory proteins and progesterone on ... and intrauterine infusion of ovine conceptus secretory proteins. Biol. Reprod. 42, 98-105 (1990). ...
A Rational Approach to Identify Inhibitors of Mycobacterium tuberculosis Enoyl Acyl Carrier Protein Reductase. Journal: Current ...
long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). R01704 palmitaldehyde:NAD+ oxidoreductase. ...
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. ... acyl-carrier- protein] derivatives of the elongating fatty acid moiety. -!- The enzyme from the bacterium Escherichia coli ... CATH: Protein Structure Classification Database by I. Sillitoe, N. Dawson, T. Lewis, D. Lee, J. Lees, C. Orengo is licensed ... The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[ ...
Beta-Ketoacyl-Acyl-Carrier-Protein Synthase I Enzyme, Catalysis, Chemical reaction, Enzyme substrate (biology), Transferase, ...
  • Here, the structure of the third enzyme in the FAS pathway, 3-ketoacyl-(acyl-carrier-protein) reductase, is reported at a resolution of 2.25 Å. (
  • β-Ketoacyl-(acyl carrier protein) reductase (FabG) catalyzes the key reductive reaction in the elongation cycle of fatty acid synthesis (FAS), which is a vital metabolic pathway in bacteria and a promising target for new antibiotic development. (
  • Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (
  • This graph shows the total number of publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in this website by year, and whether "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" was a major or minor topic of these publications. (
  • Below are the most recent publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in Profiles. (
  • to get instant updates about '3-Oxoacyl-(Acyl-Carrier-Protein) Reductase' on your MyPage . (
  • Other names in common use include beta-ketoacyl-(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 , NADPH-specific 3-oxoacyl-reductase , and 3-oxoacyl-reductase . (
  • Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution. (
  • This coupling is mediated by acyl carrier protein synthase (ACPS), a 4'-phosphopantetheinyl transferase. (
  • Fatty acid synthase is a multifunctional protein. (
  • The distance is too large to be traversed by the long arm of a statically positioned acyl carrier protein, needed to ferry growing polyketides along the synthase backbone. (
  • 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. (
  • The ivy enzyme can also act on oleoyl-[acyl-carrier protein] and palmitoleoyl-[acyl-carrier protein], generating the corresponding 4,9-diene. (
  • The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety. (
  • Some enzymes are made of just one component protein that works on its own, but others are made of multiple proteins that are all required for the enzyme to work properly. (
  • However, many enzymes can bind to different combinations of proteins to form groups (or 'complexes') with a variety of three-dimensional shapes, so there may be a variety of enzyme complexes in the solution. (
  • Further experiments used a mutant form of the TERT protein that cannot interact with other TERT molecules and found that complexes that contain this mutant protein still have normal enzyme activity. (
  • The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E 2 domain), 2-oxoglutarate dehydrogenase (E 2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [6]. (
  • This enzyme complex metabolizes long-chain fatty acids, and the long-chain 3-hydroxy acyl-coenzyme A dehydrogenase activity is specific for compounds of C12-C16 chain length. (
  • Maple syrup urine disease is caused by a deficiency of the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex, which catalyses the decarboxylation of the alpha-keto acids of leucine, isoleucine, and valine to their respective branched-chain acyl-CoAs. (
  • Quental et al identified a homozygous 1-bp deletion (117delC) in the BCKDHA gene (this gene codes for the alpha subunit of the BCKD enzyme complex, specifically E1) in Portuguese Gypsies and estimated the carrier frequency for this deletion to be as high as 1.4% (about 1 case per 71 live births). (
  • The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. (
  • Long-chain 3-hydroxy acyl-coenzyme A dehydrogenase (LCHAD) is 1 of 3 enzymatic activities that make up the trifunctional protein of the inner mitochondrial membrane. (
  • The protein is an octamer composed of 4 alpha subunits that contain the LCEH and long-chain 3-hydroxy acyl-coenzyme A dehydrogenase activities, and 4 beta subunits that contain the LCKT activity. (
  • Affected infants with long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency, which is inherited as an autosomal recessive trait, present in infancy with acute hypoketotic hypoglycemia. (
  • Some patients who are deficient in all 3 enzymatic activities of the protein have been described, although most have an isolated long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency, which results in the inability to metabolize long-chain fatty acids. (
  • Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain acyl CoA dehydrogenase deficiency (LCHAD) deficiency. (
  • Patients with long-chain 3-hydroxy acyl-coenzyme A dehydrogenase deficiency may develop a profound CNS deficiency of docosahexanoic acid ethyl ester (DHA), 22:6n-3. (
  • Occurrence frequency of either isolated long-chain 3-hydroxy acyl-coenzyme A dehydrogenase activity deficiency or trifunctional protein deficiency is unknown in the United States. (
  • Patients with long-chain 3-hydroxy acyl-coenzyme A dehydrogenase activity deficiency usually present with hypoketotic hypoglycemia, cardiomyopathy, hypotonia, and hepatomegaly at a median age of 6 months. (
  • Outcomes in pediatric studies of medium-chain acyl-coA dehydrogenase (MCAD) deficiency and phenylketonuria (PKU): a review. (
  • The contributors describe the mechanisms by which the agents disrupt cell wall assembly and maintenance, membrane synthesis and integrity, DNA and RNA metabolism, protein synthesis, and the folate cycle. (
  • Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12. (
  • Morris, T.W., Reed, K.E. and Cronan, J.E., Jr. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli . (
  • Mce1C and Mce1D facilitate the internalization of Escherichia coli expressing Mce1C protein or latex beads coated with Mce1D protein by HeLa cells, respectively. (
  • An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH. (
  • acyl-carrier-protein S-malonyltransferase [Bacillus anthracis str. (
  • The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. (
  • 4'-Phosphopantetheine is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS). (
  • Acyl carrier proteins are critical components of fatty acid and polyketide biosynthesis. (
  • The fragment contained full-length ketosythase (KS) and acyl transferase (AT) domains, and the linkers that are part of the polyketide chain elongation process. (
  • This perspective focuses on two areas that have yielded new useful information during the last 20 years: (i) structure-activity relationship (SAR) studies of contact allergy based on the concept of hapten-protein binding and (ii) mechanistic investigations regarding activation of nonsensitizing compounds to contact allergens by air oxidation or skin metabolism. (
  • Selectivity for the holo over apo -form of acyl carrier proteins is demonstrated indicating that only the phosphopantetheine - thiol is modified. (
  • malonyl CoA-acyl carrier protein transacylase, putative [Geobacter sulf. (
  • Small molecules capable of acylating this prosthetic group will provide a simple and reversible means of introducing novel functionality onto carrier protein domains. (
  • In anabolism, water is removed from molecules (through energy requiring enzymatic chemical reactions) in order to grow larger molecules (e.g. starches, triglycerides and proteins for storage of fuels and information). (
  • In the majority of cases, Rf genes produce proteins that act directly on the CMS conferring mitochondrial transcripts by binding them specifically and promoting processing events. (
  • These unusual ORFs are maternally inherited, and effectively translated into novel mitochondrial proteins, with the resulting failure to produce functional pollen as the sole observed phenotype ( Chen and Liu, 2014 ). (
  • In the majority of cases, Rf genes produce proteins that bind specifically to the CMS conferring transcripts in the mitochondria and promote processing events leading to a strong reduction in the production of mitochondrial CMS-inducing proteins (reviewed in Chen and Liu, 2014 ). (
  • How do Fatty Acyl-CoA's pass the mitochondrial intermembrane space? (
  • The molecular defect occurs in the mitochondrial trifunctional protein (MTP). (
  • Owing to its small genome (about 800 protein-coding genes), it relies on the host for many basic biosynthetic processes, hindering the identification of potential antipathogenic drug targets. (
  • This paper reports on the kinetics of accumulation of these lipid classes during pollen maturation and the expression patterns of several lipid biosynthetic genes and their protein products that are differentially regulated in developing microspores/ pollen grains (gametophyte) and tapetal cells (sporophyte) of B. napus. (
  • The ACPs are small negatively charged α-helical bundle proteins with a high degree of structural and amino acid similarity. (
  • The ACPs are related in structure and mechanism to the peptidyl carrier proteins (PCP) from nonribosomal peptide synthases. (
  • This study determines the substrate tolerance of the AH PedC for a range of acyl-ACPs. (
  • Clear preference towards short, linear acyl-ACPs is shown, with acetyl-ACP the best substrate. (
  • The etiology of the severe peripheral neuropathy of trifunctional protein deficiency may result from the unique metabolite, 3-keto-acyl-CoA, after conversion to a methylketone via spontaneous decarboxylation. (
  • To cause sensitization, a chemical must bind to macromolecules (proteins) in the skin. (
  • The didomain structure also revealed a novel protein fold for the KS-to-AT linker. (
  • Thus, the clinical features may result from either toxicity due to long-chain acyl-CoA esters that cause cardiomyopathy and cardiac arrhythmias or from a block in long-chain fatty acid oxidation that leads to an inability to synthesize ketone bodies and/or adenosine triphosphate from long-chain fatty acids. (
  • It has a preference for acyl derivatives with carbon chain length from 4 to 16. (
  • malonyl CoA-acyl carrier protein transacylase [Campylobacter jejuni RM1. (
  • The gene for the protein has been cloned and a common mutation, G1528C , has been identified in 87% of mutant alleles. (
  • Analysis of the frequency of the most common mutation ( G1528C ) revealed a carrier frequency of 1:240 in Finland. (
  • Frequent loss of mutation-specific mismatch repair protein expression in nonneoplastic endometrium of Lynch syndrome patients. (
  • Risk-reducing salpingo-oophorectomy, natural menopause, and breast cancer risk: an international prospective cohort of BRCA1 and BRCA2 mutation carriers. (
  • It is one of the most abundant proteins in cells of E. coli. (
  • Expert systems containing information about the relationship between the chemical structure and the ability of chemicals to haptenate proteins are available. (
  • PPR proteins have in common a canonical P-type 35 amino acid domain repeated in tandem up to 30 times. (
  • The most common of these are E-3M2H and (RS)-3-hydroxy-3-methlyhexanoic acid (HMHA), which are released through the action of a specific zinc-dependent N -alpha-acyl-glutamine aminoacylase (N-AGA) from Corynebacterium species. (
  • They have been hypothesised to perform a proofreading function by removing acyl chains from stalled sites. (
  • We predict this structure to be a membrane protein. (
  • The mammalian cell entry (Mce) family of proteins consists of invasin-like membrane-associated proteins. (
  • The most abundant of these acids is (E)-3-methyl-2-hexanoic acid (E-3M2H), which is brought to the skin surface bound by 2 apocrine secretion odor-binding proteins, ASOB1 and ASOB2. (
  • SCOPe: Structural Classification of Proteins - extended. (
  • The structures of a number of acyl carrier proteins have been solved using various NMR and crystallography techniques. (
  • Here, we review the literature that highlights those characteristics and help explain why PPR proteins are ideal for the roles they play as restorers of fertility. (
  • The roles of Mce1C and Mce1D proteins in host-pathogen interactions have not been investigated. (
  • Here we report the findings of structural, enzymatic, and binding studies of the FabG protein found in the causative agent of cholera, Vibrio cholerae (vcFabG). (