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.
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.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
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.
The vitamin K-dependent cofactor of activated PROTEIN C. Together with protein C, it inhibits the action of factors VIIIa and Va. A deficiency in protein S; (PROTEIN S DEFICIENCY); can lead to recurrent venous and arterial thrombosis.
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 2.3.1.41.
Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.
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.
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.
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.
An autosomal dominant disorder showing decreased levels of plasma protein S antigen or activity, associated with venous thrombosis and pulmonary embolism. PROTEIN S is a vitamin K-dependent plasma protein that inhibits blood clotting by serving as a cofactor for activated PROTEIN C (also a vitamin K-dependent protein), and the clinical manifestations of its deficiency are virtually identical to those of protein C deficiency. Treatment with heparin for acute thrombotic processes is usually followed by maintenance administration of coumarin drugs for the prevention of recurrent thrombosis. (From Harrison's Principles of Internal Medicine, 12th ed, p1511; Wintrobe's Clinical Hematology, 9th ed, p1523)
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
A ribosomal protein that may play a role in controlling cell growth and proliferation. It is a major substrate of RIBOSOMAL PROTEIN S6 KINASES and plays a role in regulating the translation (TRANSLATION, GENETIC) of RNAs that contain an RNA 5' TERMINAL OLIGOPYRIMIDINE SEQUENCE.
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.
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 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.
The addition of an organic acid radical into a molecule.
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 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.
Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.
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 degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
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.
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 sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
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.
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.
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 rate dynamics in chemical or physical systems.
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 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.
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 prepared by recombinant DNA technology.
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.
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.
Proteins obtained from ESCHERICHIA COLI.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
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.
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.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation.
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.
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 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.
The condition of harboring an infective organism without manifesting symptoms of infection. The organism must be readily transmissible to another susceptible host.
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.
Serum proteins that negatively regulate the cascade process of COMPLEMENT ACTIVATION. Uncontrolled complement activation and resulting cell lysis is potentially dangerous for the host. The complement system is tightly regulated by inactivators that accelerate the decay of intermediates and certain cell surface receptors.
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.
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).
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.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
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 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 family of protein serine/threonine kinases which act as intracellular signalling intermediates. Ribosomal protein S6 kinases are activated through phosphorylation in response to a variety of HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Phosphorylation of RIBOSOMAL PROTEIN S6 by enzymes in this class results in increased expression of 5' top MRNAs. Although specific for RIBOSOMAL PROTEIN S6 members of this class of kinases can act on a number of substrates within the cell. The immunosuppressant SIROLIMUS inhibits the activation of ribosomal protein S6 kinases.
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.

Polyketide synthase acyl carrier protein (ACP) as a substrate and a catalyst for malonyl ACP biosynthesis. (1/41)

BACKGROUND: Using an acyl-acyl carrier protein (ACP) as a starter unit, type II polyketide synthases (PKSs) generate a wide range of polyketide products by successive decarboxylative condensations with the two-carbon donor malonyl (ACP). In vitro experiments have demonstrated that polyketide biosynthesis in reconstituted PKS systems requires the fatty acid synthase (FAS) enzyme malonyl CoA:ACP acyltransferase (FabD) from streptomycetes. It has also been shown that holo-ACPs from a type II PKS can catalyze self-malonylation in the presence of malonyl CoA and negate this FabD requirement. The relative roles of FabD and ACP self-malonylation in PKS biosynthesis in vivo are still not known. RESULTS: We have examined the ACP specificity of the Streptomyces glaucescens FabD and shown that it reacts specifically with monomeric forms of ACP, with comparable k(cat)/K(M) values for ACPs from both type II PKS and FAS systems. Incubations of tetracenomycin ACP (TcmM) with the Escherichia coli FAS ACP (AcpP) unexpectedly revealed that, in addition to the self-malonylation process, TcmM can catalyze the malonylation of AcpP. The k(cat)/K(M) value for the TcmM-catalyzed malonylation of S. glaucescens FAS ACP is two orders of magnitude smaller than that observed for the FabD-catalyzed process. CONCLUSIONS: The ability of a PKS ACP to catalyze malonylation of a FAS ACP is a surprising finding and demonstrates for the first time that PKS ACPs and FabD can catalyze the same reaction. The differences in the catalytic efficiency of these two proteins rationalizes in vitro observations that FabD-independent polyketide biosynthesis proceeds only at high concentrations of a PKS ACP.  (+info)

Kinetic analysis of the actinorhodin aromatic polyketide synthase. (2/41)

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). (3/41)

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. (4/41)

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)

Fatty acid and lipoic acid biosynthesis in higher plant mitochondria. (5/41)

Fatty acid and lipoic acid biosynthesis were investigated in plant mitochondria. Although the mitochondria lack acetyl-CoA carboxylase, our experiments reveal that they contain the enzymatic equipment necessary to transform malonate into the two main building units for fatty acid synthesis: malonyl- and acetyl-acyl carrier protein (ACP). We demonstrated, by a new method based on a complementary use of high performance liquid chromatography and mass spectrometry, that the soluble mitochondrial fatty-acid synthase produces mainly three predominant acyl-ACPs as follows: octanoyl(C8)-, hexadecanoyl(C16)-, and octadecanoyl(C18)-ACP. Octanoate production is of primary interest since it has been postulated long ago to be a precursor of lipoic acid. By using a recombinant H apoprotein mutant as a potential acceptor for newly synthesized lipoic acid, we were able to detect limited amounts of lipoylated H protein in the presence of malonate, several sulfur donors, and cofactors. Finally, we present a scheme outlining the new biochemical pathway of fatty acid and lipoic acid synthesis in plant mitochondria.  (+info)

Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. (6/41)

Malonyl coenzyme A (CoA)-acyl carrier protein (ACP) transacylase (MCAT) is an essential enzyme in the biosynthesis of fatty acids in all bacteria, including Mycobacterium tuberculosis. MCAT catalyzes the transacylation of malonate from malonyl-CoA to activated holo-ACP, to generate malonyl-ACP, which is an elongation substrate in fatty acid biosynthesis. To clarify the roles of the mycobacterial acyl carrier protein (AcpM) and MCAT in fatty acid and mycolic acid biosynthesis, we have cloned, expressed, and purified acpM and mtfabD (malonyl-CoA:AcpM transacylase) from M. tuberculosis. According to the culture conditions used, AcpM was produced in Escherichia coli in two or three different forms: apo-AcpM, holo-AcpM, and palmitoylated-AcpM, as revealed by electrospray mass spectrometry. The mtfabD gene encoding a putative MCAT was used to complement a thermosensitive E. coli fabD mutant. Expression and purification of mtFabD resulted in an active enzyme displaying strong MCAT activity in vitro. Enzymatic studies using different ACP substrates established that holo-AcpM constitutes the preferred substrate for mtFabD. In order to provide further insight into the structure-function relationship of mtFabD, different mutant proteins were generated. All mutations (Q9A, R116A, H194A, Q243A, S91T, and S91A) completely abrogated MCAT activity in vitro, thus underlining the importance of these residues in transacylation. The generation and characterization of the AcpM forms and mtFabD opens the way for further studies relating to fatty acid and mycolic acid biosynthesis to be explored in M. tuberculosis. Since a specific type of FabD is found in mycobacterial species, it represents an attractive new drug target waiting to be exploited.  (+info)

The Endoplasmic reticulum-associated maize GL8 protein is a component of the acyl-coenzyme A elongase ivolved in the production of cuticular waxes. (7/41)

The gl8 gene is required for the normal accumulation of cuticular waxes on maize (Zea mays) seedling leaves. The predicted GL8 protein exhibits significant sequence similarity to a class of enzymes that catalyze the reduction of a ketone group to a hydroxyl group. Polyclonal antibodies raised against the recombinant Escherichia coli-expressed GL8 protein were used to investigate the function of this protein in planta. Subcellular fractionation experiments indicate that the GL8 protein is associated with the endoplasmic reticulum membranes. Furthermore, polyclonal antibodies raised against the partially purified leek (Allium porrum) microsomal acyl-coenzyme A (CoA) elongase can react with the E. coli-expressed GL8 protein. In addition, anti-GL8 immunoglobulin G inhibited the in vitro elongation of stearoyl-CoA by leek and maize microsomal acyl-CoA elongase. In combination, these findings indicate that the GL8 protein is a component of the acyl-CoA elongase. In addition, the finding that anti-GL8 immunoglobulin G did not significantly inhibit the 3-ketoacyl-CoA synthase, 3-ketoacyl-CoA dehydrase, and (E) 2,3-enoyl-CoA reductase partial reactions of leek or maize acyl-CoA elongase lends further support to our previous hypothesis that the GL8 protein functions as a beta-ketoacyl reductase during the elongation of very long-chain fatty acids required for the production of cuticular waxes.  (+info)

Site-specific mutagenesis and domain substitutions in the loading module of the nystatin polyketide synthase, and their effects on nystatin biosynthesis in Streptomyces noursei. (8/41)

The loading module for the nystatin polyketide synthase (PKS) in Streptomyces noursei is represented by the NysA protein composed of a ketosynthase (KS(S)), acyltransferase, dehydratase, and an acyl carrier protein. The absolute requirement of this protein for initiation of nystatin biosynthesis was demonstrated by the in-frame deletion of the nysA gene in S. noursei. The role of the NysA KS(S) domain, however, remained unclear, since no data on the significance of the "active site" serine (Ser-170) residue in the loading modules of type I PKSs were available. Site-specific mutagenesis of Ser-170 both in the wild-type NysA and in the hybrid loading module containing malonyl-specific acyltransferase domain from the extender module had no effect on nystatin biosynthesis. A second mutation (S413N) of the NysA KS(S) domain was discovered that completely abolished the ability of the hybrids to restore nystatin biosynthesis, presumably by affecting the ability of the resulting proteins to catalyze the required substrate decarboxylation. In contrast, NysA and its Ser-170 mutants bearing the same S413N mutation were able to restore nystatin production to significant levels, probably by using acetyl-CoA as a starter unit. Together, these data suggest that the KS(S) domain of NysA differs from the KS(Q) domains found in the loading modules of several PKS type I systems in that the active site residue is not significant for its activity.  (+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.

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.

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.

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.

Protein S is a vitamin K-dependent protein found in the blood that functions as a natural anticoagulant. It plays a crucial role in regulating the body's clotting system by inhibiting the activation of coagulation factors, thereby preventing excessive blood clotting. Protein S also acts as a cofactor for activated protein C, which is another important anticoagulant protein.

Protein S exists in two forms: free and bound to a protein called C4b-binding protein (C4BP). Only the free form of Protein S has biological activity in inhibiting coagulation. Inherited or acquired deficiencies in Protein S can lead to an increased risk of thrombosis, or abnormal blood clot formation, which can cause various medical conditions such as deep vein thrombosis (DVT) and pulmonary embolism (PE). Regular monitoring of Protein S levels is essential for patients with a history of thrombotic events or those who have a family history of thrombophilia.

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.

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.

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.

'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.

Protein S deficiency is a genetic disorder that affects the body's ability to coagulate blood properly. Protein S is a naturally occurring protein in the blood that helps regulate the clotting process by deactivating clotting factors when they are no longer needed. When Protein S levels are too low, it can lead to an increased risk of abnormal blood clots forming within blood vessels, a condition known as thrombophilia.

There are three types of Protein S deficiency: Type I (quantitative deficiency), Type II (qualitative deficiency), and Type III (dysfunctional protein). These types refer to the amount or function of Protein S in the blood. In Type I, there is a decrease in both free and total Protein S levels. In Type II, there is a decrease in functional Protein S despite normal total Protein S levels. In Type III, there is a decrease in free Protein S with normal total Protein S levels.

Protein S deficiency can be inherited or acquired. Inherited forms of the disorder are caused by genetic mutations and are usually present from birth. Acquired forms of Protein S deficiency can develop later in life due to certain medical conditions, such as liver disease, vitamin K deficiency, or the use of certain medications that affect blood clotting.

Symptoms of Protein S deficiency may include recurrent blood clots, usually in the legs (deep vein thrombosis) or lungs (pulmonary embolism), skin discoloration, pain, and swelling in the affected area. In severe cases, it can lead to complications such as chronic leg ulcers, pulmonary hypertension, or damage to the heart or lungs.

Diagnosis of Protein S deficiency typically involves blood tests to measure Protein S levels and function. Treatment may include anticoagulant medications to prevent blood clots from forming or growing larger. Lifestyle modifications such as regular exercise, maintaining a healthy weight, and avoiding smoking can also help reduce the risk of blood clots in people with Protein S deficiency.

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.

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.

Ribosomal Protein S6 (RP S6) is a protein component of the 40S subunit of eukaryotic ribosomes, which are complexes responsible for protein synthesis in cells. Specifically, RP S6 is part of the heterodimer that makes up the head of the 40S subunit.

RP S6 plays a role in regulating translation, the process by which mRNA (messenger RNA) molecules are decoded to produce proteins. It has been found to be involved in the initiation and elongation steps of translation, particularly in response to various cellular signals such as growth factors, hormones, and nutrients.

Phosphorylation of RP S6 is a key regulatory mechanism that modulates its activity during translation. This phosphorylation can be mediated by several kinases, including the p70S6 kinase (p70S6K), which is activated in response to growth factor signaling and nutrient availability.

Abnormalities in RP S6 regulation have been implicated in various diseases, such as cancer, where increased RP S6 phosphorylation has been observed in many tumor types, suggesting a role in promoting cell proliferation and survival.

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.

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.

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.

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.

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.

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.

Ribosomal proteins are a type of protein that play a crucial role in the structure and function of ribosomes, which are complex molecular machines found within all living cells. Ribosomes are responsible for translating messenger RNA (mRNA) into proteins during the process of protein synthesis.

Ribosomal proteins can be divided into two categories based on their location within the ribosome:

1. Large ribosomal subunit proteins: These proteins are associated with the larger of the two subunits of the ribosome, which is responsible for catalyzing peptide bond formation during protein synthesis.
2. Small ribosomal subunit proteins: These proteins are associated with the smaller of the two subunits of the ribosome, which is responsible for binding to the mRNA and decoding the genetic information it contains.

Ribosomal proteins have a variety of functions, including helping to stabilize the structure of the ribosome, assisting in the binding of substrates and cofactors necessary for protein synthesis, and regulating the activity of the ribosome. Mutations in ribosomal proteins can lead to a variety of human diseases, including developmental disorders, neurological conditions, and cancer.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

"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.

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.

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.

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.

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.

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.

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.

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.

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.

'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.

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 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.

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.

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.

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.

Protein C is a vitamin K-dependent protease that functions as an important regulator of coagulation and inflammation. It is a plasma protein produced in the liver that, when activated, degrades clotting factors Va and VIIIa to limit thrombus formation and prevent excessive blood clotting. Protein C also has anti-inflammatory properties by inhibiting the release of pro-inflammatory cytokines and reducing endothelial cell activation. Inherited or acquired deficiencies in Protein C can lead to an increased risk of thrombosis, a condition characterized by abnormal blood clot formation within blood vessels.

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.

"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.

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.

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.

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.

Complement inactivator proteins are a group of regulatory proteins that help to control and limit the activation of the complement system, which is a part of the immune system. The complement system is a complex series of biochemical reactions that help to eliminate pathogens and damaged cells from the body. However, if not properly regulated, the complement system can also cause damage to healthy tissues and contribute to the development of various diseases.

Complement inactivator proteins work by inhibiting specific components of the complement system, preventing them from activating and causing an immune response. Some examples of complement inactivator proteins include:

1. C1 inhibitor (C1INH): This protein regulates the activation of the classical pathway of the complement system by inhibiting the C1 complex, which is a group of proteins that initiate this pathway.
2. Decay-accelerating factor (DAF or CD55): This protein regulates the activation of both the classical and alternative pathways of the complement system by accelerating the decay of the C3/C5 convertases, which are enzymes that activate the complement components C3 and C5.
3. Membrane cofactor protein (MCP or CD46): This protein regulates the activation of the alternative pathway of the complement system by serving as a cofactor for the cleavage and inactivation of C3b, a component of the C3 convertase.
4. Factor H: This protein also regulates the activation of the alternative pathway of the complement system by acting as a cofactor for the cleavage and inactivation of C3b, and by preventing the formation of the C3 convertase.

Deficiencies or dysfunction of complement inactivator proteins can lead to various diseases, including hereditary angioedema (C1INH deficiency), atypical hemolytic uremic syndrome (factor H deficiency or dysfunction), and age-related macular degeneration (complement component overactivation).

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.

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.

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.

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.

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.

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.

Ribosomal Protein S6 Kinases (RSKs) are a family of serine/threonine protein kinases that play a crucial role in the regulation of cell growth, proliferation, and survival. They are so named because they phosphorylate and regulate the function of the ribosomal protein S6, which is a component of the 40S ribosomal subunit involved in protein synthesis.

RSKs are activated by various signals, including growth factors, hormones, and mitogens, through a cascade of phosphorylation events involving several upstream kinases such as MAPK/ERK kinase (MEK) and extracellular signal-regulated kinase (ERK). Once activated, RSKs phosphorylate a wide range of downstream targets, including transcription factors, regulators of translation, and cytoskeletal proteins, thereby modulating their activities and functions.

There are four isoforms of RSKs in humans, namely RSK1, RSK2, RSK3, and RSK4, which share a common structural organization and functional domains, including an N-terminal kinase domain, a C-terminal kinase domain, and a linker region that contains several regulatory motifs. Dysregulation of RSKs has been implicated in various pathological conditions, including cancer, cardiovascular diseases, neurological disorders, and diabetes, making them attractive targets for therapeutic intervention.

'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.

... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] The transfer of malonate to acyl-carrier-protein (ACP) converts the ... acyl carrier protein]malonyltransferase, FabD, malonyl transacylase, malonyl transferase, malonyl-CoA-acyl carrier protein ... acyl-carrier-protein] S-malonyltransferase. Other names in common use include malonyl coenzyme A-acyl carrier protein ... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] Thus, the two substrates of this enzyme are malonyl-CoA and acyl ...
Malonyltransferase and acyl carrier protein". The Journal of Biological Chemistry. 278 (41): 40067-74. doi:10.1074/jbc. ... Malonyl CoA-acyl carrier protein transacylase, mitochondrial is an enzyme that in humans is encoded by the MCAT gene. The ... where it catalyzes the transfer of a malonyl group from malonyl-CoA to the mitochondrial acyl carrier protein. The encoded ... The human Malonyl CoA-acel carrier protein transacylase in human mitochondria associates with respiratory complex one, such ...
A crystal structure is available of the S. albidoflavus [acyl-carrier-protein] S-malonyltransferase. S. albidoflavus's ACP S-MT ... Certain strains of S. albidoflavus can be used for heterologous protein expression. The Ku homolog is SCF55.25c. It contains an ... S. albidoflavus produces a (putatively) single-domain protein SC9H11.09c which is homologous to the LigD NucDom which is common ... is located in the intergenic region between anti-sigma factor SCO4677 gene and a putative regulatory protein gene SCO4676. ...
These include the acyl carrier protein (ACP), acetyl transferase (AT), ketosynthase (KS), malonyl transferase (MT; which can ...
... can refer to: (acyl-carrier-protein) S-malonyltransferase Anthocyanin 5-O-glucoside 6'''-O- ... malonyltransferase This set index page lists enzyme articles associated with the same name. If an internal link led you here, ...
... acyl-carrier-protein) S-malonyltransferase, an enzyme This disambiguation page lists articles associated with the title MDCH. ...
... acyl-carrier-protein) S-malonyltransferase, an enzyme MCAT (gene), a gene that in humans encodes the enzyme malonyl CoA-acyl ... carrier protein transacylase, mitochondrial Moraxella catarrhalis, a Gram-negative bacteria m.c.A.T (born 1961), Japanese ...
... may refer to: Florida Association of Band Directors (acyl-carrier-protein) S-malonyltransferase, an enzyme Football ...
... acyl-carrier protein s-malonyltransferase MeSH D08.811.913.050.173 - 1-acylglycerol-3-phosphate O-acyltransferase MeSH D08.811. ... acyl-carrier-protein) reductase (nadh) MeSH D08.811.682.660.390 - enoyl-(acyl-carrier protein) reductase (nadph, b-specific) ... acyl-carrier protein s-acetyltransferase MeSH D08.811.913.050.134.060 - acetyl-CoA C-acetyltransferase MeSH D08.811.913.050. ... acyl-carrier-protein) synthase MeSH D08.811.913.050.625 - phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050.646 ...
... acyl-carrier-protein] S-acetyltransferase EC 2.3.1.39: [acyl-carrier-protein] S-malonyltransferase EC 2.3.1.40: acyl-[acyl- ... acyl-carrier-protein] synthase II EC 2.3.1.180: β-ketoacyl-[acyl-carrier-protein] synthase III EC 2.3.1.181: lipoyl(octanoyl) ... acyl carrier protein) synthase I (*) EC 2.3.1.294: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II (*) EC 2.3. ... acyl-carrier-protein] synthase (*) EC 2.3.1.301: mycobacterial β-ketoacyl-[acyl carrier protein] synthase III (*) EC 2.3.1.302 ...
"Protein-protein recognition between acyltransferases and acyl carrier proteins in multimodular polyketide synthases". ... Other names of this enzyme class is malonyl-CoA:propanoyl-CoA malonyltransferase (cyclizing). Other names in common use include ... or acyl carrier protein. However, in fatty acid synthesis the original molecules are Acyl-CoA or Malonyl-CoA but polyketide ... The DEBS complex also contains a Loading Domain on module 1 consisting of an acyl carrier protein and an acyltransferase. The ...
... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] The transfer of malonate to acyl-carrier-protein (ACP) converts the ... acyl carrier protein]malonyltransferase, FabD, malonyl transacylase, malonyl transferase, malonyl-CoA-acyl carrier protein ... acyl-carrier-protein] S-malonyltransferase. Other names in common use include malonyl coenzyme A-acyl carrier protein ... acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] Thus, the two substrates of this enzyme are malonyl-CoA and acyl ...
Acyl-Carrier Protein S-Malonyltransferase*Acyl-Carrier Protein S-Malonyltransferase. *Acyl Carrier Protein S Malonyltransferase ... "Acyl-Carrier Protein S-Malonyltransferase" by people in this website by year, and whether "Acyl-Carrier Protein S- ... "Acyl-Carrier Protein S-Malonyltransferase" is a descriptor in the National Library of Medicines controlled vocabulary ... Below are the most recent publications written about "Acyl-Carrier Protein S-Malonyltransferase" by people in Profiles. ...
... and an acyl-carrier protein (ACP). The KS domain both accepts the growing polyketide chain from the previous module and ... propanoyl-CoA:(2S)-methylmalonyl-CoA malonyltransferase (cyclizing). Comments:. The product, 6-deoxyerythronolide B, contains a ... erythronolide condensing enzyme; malonyl-CoA:propionyl-CoA malonyltransferase (cyclizing); erythronolide synthase; malonyl-CoA: ... propanoyl-CoA malonyltransferase (cyclizing); deoxyerythronolide B synthase; 6-deoxyerythronolide B synthase; DEBS. ...
acyl-carrier-protein] S-malonyltransferase activity * [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity ...
... acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O. ... acyl-carrier-protein] S-malonyltransferase activity * [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity ... 3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO_ ... acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O. ], comment: [] }, query: Get JSON for Class, version ...
Acyl-Carrier Protein S-Malonyltransferase [D08.811.913.050.170] * 1-Acylglycerol-3-Phosphate O-Acyltransferase [D08.811.913.050 ... 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase [D08.811.913.050.622] * Phosphatidylcholine-Sterol O-Acyltransferase [D08.811.913.050 ... Fatty Acyl-CoA - Sphingosine Acyltransferase Term UI T164315. LexicalTag NON. ThesaurusID NLM (2006). ... Fatty Acyl-CoA - Sphingosine Acyltransferase Sphingosine Acyltransferase Registry Number. EC 2.3.1.24. Public MeSH Note. 2006; ...
Acyl-Carrier-Protein) Malonyltransferase use Acyl-Carrier Protein S-Malonyltransferase (Acyl-Carrier-Protein) S- ... Acetyltransferase use Acyl-Carrier Protein S-Acetyltransferase (Acyl-Carrier-Protein) S-Malonyltransferase use Acyl-Carrier ... Acyl-Carrier-Protein) Acetyltransferase use Acyl-Carrier Protein S-Acetyltransferase ( ... Myelin Basic Protein)-Arginine N-Methyltransferase use Protein-Arginine N-Methyltransferases (N-Methyl-11C)mirtazapine use ...
Acyl-Carrier-Protein) Malonyltransferase use Acyl-Carrier Protein S-Malonyltransferase (Acyl-Carrier-Protein) S- ... Acetyltransferase use Acyl-Carrier Protein S-Acetyltransferase (Acyl-Carrier-Protein) S-Malonyltransferase use Acyl-Carrier ... Acyl-Carrier-Protein) Acetyltransferase use Acyl-Carrier Protein S-Acetyltransferase ( ... 3 Dimensional Homologs, Protein use Structural Homology, Protein 3 Dimensional Homology, Protein use Structural Homology, ...
... "acyl carrier protein S-malonyltransferase [Ensembl]. Acyl transferase domain [InterProScan].","protein_coding" "AGT24860","N559 ... acyl-carrier protein) reductase (3-ketoacyl-acyl carrier protein reductase) [Ensembl]. Enoyl-(Acyl carrier protein) reductase [ ... acyl-carrier-protein) synthase 3 [Ensembl]. 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III, 3-Oxoacyl-[acyl-carrier- ... "protein-export membrane protein SecDF [Ensembl]. Protein-export membrane protein SecD/SecF, Protein-export membrane protein ...
MeSH Terms: Acyl-Carrier Protein S-Malonyltransferase/metabolism; Fungi/enzymology; Kinetics; Polyketide Synthases/biosynthesis ... Polyketide Synthases/chemistry; Polyketide Synthases/metabolism*; Protein Structure, Tertiary; Substrate Specificity ...
Acyl-Carrier-Protein) Malonyltransferase (Acyl-Carrier-Protein) S-Malonyltransferase Malonyl CoA Transferase Malonyl Coenzyme A ... 2006; (ACYL-CARRIER PROTEIN) MALONYLTRANSFERASE was indexed under ACYLTRANSFERASES 1973-2005, & under CARRIER PROTEINS 1973- ... Acyl-Carrier Protein S-Malonyltransferase Preferred Term Term UI T629880. Date02/07/2005. LexicalTag NON. ThesaurusID NLM (2006 ... Acyl-Carrier Protein S-Malonyltransferase [D08.811.913.050.170] * Fatty Acid Synthases [D08.811.913.050.170.500] ...
Acyl-Carrier-Protein) Malonyltransferase (Acyl-Carrier-Protein) S-Malonyltransferase Malonyl CoA Transferase Malonyl Coenzyme A ... 2006; (ACYL-CARRIER PROTEIN) MALONYLTRANSFERASE was indexed under ACYLTRANSFERASES 1973-2005, & under CARRIER PROTEINS 1973- ... Acyl-Carrier Protein S-Malonyltransferase Preferred Term Term UI T629880. Date02/07/2005. LexicalTag NON. ThesaurusID NLM (2006 ... Acyl-Carrier Protein S-Malonyltransferase [D08.811.913.050.170] * Fatty Acid Synthases [D08.811.913.050.170.500] ...
Acyl-carrier-protein malonyltransferase Current Synonym true false 74065010 [Acyl-carrier-protein] malonyltransferase Current ... Acyl-carrier-protein malonyltransferase (substance). Code System Preferred Concept Name. Acyl-carrier-protein ...
Acyl-carrier protein S-malonyltransferase Synonymes. (Acyl-carrier protein) S-malonyltransferase (Acyl-carrier protein) ... Acyl-carrier protein) S-malonyltransferase. (Acyl-carrier protein) malonyltransferase. Malonyl CoA transférase. Malonyl ... Acyl-carrier protein S-malonyltransferase - Concept préféré Concept UI. M0070598. Terme préféré. ... Acyl-Carrier Protein S-Malonyltransferase Descripteur en espagnol: S-Maloniltransferasa de la Proteína Transportadora de Grupos ...
N0000168143 Acyl-Carrier Protein S-Acetyltransferase N0000168126 Acyl-Carrier Protein S-Malonyltransferase N0000169071 Acyl-CoA ... Acyl-Carrier Protein) Reductase (NADPH, B-Specific) N0000167924 Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) N0000168032 Enoyl ... Acute-Phase Proteins N0000007269 Acyclovir N0000179390 Acyclovir Sodium N0000169553 Acyl Carrier Protein N0000170825 Acyl ... N0000169241 HMGB3 Protein N0000169206 HMGN Proteins N0000169207 HMGN1 Protein N0000169208 HMGN2 Protein N0000171143 HN Protein ...
Acyl-Carrier Protein S-Malonyltransferase. *Aminoacyltransferases. *ATP Citrate (pro-S)-Lyase. *Carnitine Acyltransferases ...
acyl-carrier-protein] S-malonyltransferase activity * [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity ...
PROTEINS 1970-1973 MH - Acyl-Carrier Protein S-Malonyltransferase UI - D051080 MN - D8.811.913.50.170 MS - This enzyme ... acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon ... An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the ... acyl-carrier protein to form COENZYME A and acetyl-acyl-carrier protein. HN - 2006(1980); use ACETYLTRANSFERASES 1970-1979, ...
Acyl-Carrier Protein S-Malonyltransferase [D08.811.913.050.170] * 1-Acylglycerol-3-Phosphate O-Acyltransferase [D08.811.913.050 ... 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase [D08.811.913.050.622] * Phosphatidylcholine-Sterol O-Acyltransferase [D08.811.913.050 ...
Acyl-Carrier Protein S-Malonyltransferase [D08.811.913.050.170] * 1-Acylglycerol-3-Phosphate O-Acyltransferase [D08.811.913.050 ... acyl carrier protein) to another molecule of fatty acyl-(acyl carrier protein), giving a beta-ketoacyl-(acyl carrier protein) ... acyl carrier protein) to another molecule of fatty acyl-(acyl carrier protein), giving a beta-ketoacyl-(acyl carrier protein) ... Acyl-Malonyl-ACP Condensing Enzyme beta Keto Acyl Synthetase beta Keto-Acyl Carrier Protein Synthase I beta Keto-Acyl Carrier ...
Acyl Coenzyme A Acyl-Butyrolactones Acyl-Carrier Protein S-Acetyltransferase Acyl-Carrier Protein S-Malonyltransferase Acyl-CoA ... Acyl-Carrier-Protein) Reductase 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase 3-Phosphoinositide-Dependent Protein Kinases 3- ... ADAMTS Proteins ADAMTS1 Protein ADAMTS13 Protein ADAMTS4 Protein ADAMTS5 Protein ADAMTS7 Protein ADAMTS9 Protein Adansonia ... Acyl-Carrier Protein) Reductase (NADPH, B-Specific) Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) Enoyl-CoA Hydratase Enoyl-CoA ...
... acyl-carrier protein] + alpha-KDO-(2-,4)-alpha-KDO-(2-,6)-lipid IVA = KDO2-(palmitoleoyl)-lipid IVA + a holo-[acyl-carrier ... S-malonyltransferase activity. Details: Catalysis of the transfer of a malonyl group to a sulfur atom on the acceptor molecule. ... Catalysis of the transfer of an acyl group to a sulfur atom on the cysteine of a protein molecule. ... Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). ...
  • In enzymology, a [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) is an enzyme that catalyzes the chemical reaction malonyl-CoA + acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] Thus, the two substrates of this enzyme are malonyl-CoA and acyl carrier protein, whereas its two products are CoA and malonyl-acyl-carrier-protein. (wikipedia.org)
  • The systematic name of this enzyme class is malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase. (wikipedia.org)
  • Malony-CoA:ACP Transacylase (FabD) is one such individual soluble protein and catalyzes the following reaction: malonyl-CoA + acyl carrier protein ⇌ CoA + malonyl-[acyl-carrier-protein] The transfer of malonate to acyl-carrier-protein (ACP) converts the acyl groups into thioester forms which are characteristic of acyl intermediates in fatty acid synthesis and which are strictly required for the condensation reactions catalyzed by β-ketoacyl-ACP synthetase. (wikipedia.org)
  • Malonyl-CoA:ACP Transacylase uses a ping-pong kinetic mechanism with a bound malonyl ester as the acyl intermediate attached to a serine residue residing within a GHSLG pentapeptide. (wikipedia.org)
  • 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. (ucdenver.edu)
  • Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP). (enzyme-database.org)
  • An enzyme that catalyzes the acyltransferase of SPHINGOSINE to N-acylsphingosine using acyl-COENZYME A as donor and COENZYME A as acceptor. (nih.gov)
  • protein_coding" "AAC74888","manY","Escherichia coli","mannose-specific enzyme IIC component of PTS [Ensembl]. (ntu.edu.sg)
  • The fatty acid synthetic pathway is the principal route for the production of membrane phospholipid acyl chains in bacterial and plants. (wikipedia.org)
  • protein_coding" "AAC73882","ybhG","Escherichia coli","putative membrane fusion protein (MFP) component of efflux pump, membrane anchor [Ensembl]. (ntu.edu.sg)
  • Queuosine biosynthesis protein [Interproscan]. (ntu.edu.sg)
  • The reaction sequence is carried out by a series of individual soluble proteins that are each encoded by a discrete gene, and the pathway intermediates are shuttled between the enzymes. (wikipedia.org)
  • On the other hand, each enzymatic activity (Condensation reaction, Reduction Reaction, Dehydration reaction) is found as a discrete protein in type II systems. (wikipedia.org)
  • Catalysis of the reaction: a (3R)-hydroxyacyl-[acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O. (virtualflybrain.org)
  • 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. (nih.gov)
  • Catalysis of the reaction: a (3R)-hydroxyacyl-[acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O. (virtualflybrain.org)
  • Catalysis of the reaction: acyl-CoA + dihydrolipoamide = CoA + S-acyldihydrolipoamide, where the acyl group is a branched chain. (systemsbiology.net)
  • Catalysis of the transfer of an acyl group to an oxygen atom on the acceptor molecule. (systemsbiology.net)
  • Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). (systemsbiology.net)
  • 9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)