Multienzyme complexes. Medical search

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 multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)

An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.

A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.

Oxidoreductases that are specific for KETONES.

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.

A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.

A mitochondrial protein consisting of four alpha-subunits and four beta-subunits. It contains enoyl-CoA hydratase, long-chain-3-hydroxyacyl-CoA dehydrogenase, and acetyl-CoA C-acyltransferase activities and plays an important role in the metabolism of long chain FATTY ACIDS.

An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.

Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.

A PYRIDOXAL PHOSPHATE dependent enzyme that catalyzes the decarboxylation of GLYCINE with the transfer of an aminomethyl group to the LIPOIC ACID moiety of the GLYCINE DECARBOXYLASE COMPLEX H-PROTEIN. Defects in P-protein are the cause of non-ketotic hyperglycinemia. It is one of four subunits of the glycine decarboxylase complex.

A genus of gram-positive, anaerobic bacteria in the family Thermoanaerobacteriaceae. They are thermophilic and saccharolytic.

The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).

A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.

A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.

Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.

A species of gram-positive, thermophilic, cellulolytic bacteria in the family Clostridaceae. It degrades and ferments CELLOBIOSE and CELLULOSE to ETHANOL in the CELLULOSOME.

Extracellular structures found in a variety of microorganisms. They contain CELLULASES and play an important role in the digestion of CELLULOSE.

A LIPOIC ACID-containing protein that plays the pivotal role in the transfer of methylamine groups and reducing equivalents between the three enzymatic components of the glycine decarboxylase complex.

Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.

Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.

A one-carbon group transferase that transfers lipoamide-linked methylamine groups to tetrahydrofolate (TETRAHYDROFOLATES) to form methylenetetrahydrofolate and AMMONIA. It is one of four components of the glycine decarboxylase complex.

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.

Reduction in caloric intake without reduction in adequate nutrition. In experimental animals, caloric restriction has been shown to extend lifespan and enhance other physiological variables.

A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.

The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.

Enzymes that catalyze the transfer of hydroxymethyl or formyl groups. EC 2.1.2.

A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.

Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.

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.

A red yeast-like mitosporic fungal genus generally regarded as nonpathogenic. It is cultured from numerous sources in human patients.

A sulfhydryl reagent that is widely used in experimental biochemical studies.

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.

A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.

The rate dynamics in chemical or physical systems.

An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.

An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.

An autosomal recessive inherited disorder with multiple forms of phenotypic expression, caused by a defect in the oxidative decarboxylation of branched-chain amino acids (AMINO ACIDS, BRANCHED-CHAIN). These metabolites accumulate in body fluids and render a "maple syrup" odor. The disease is divided into classic, intermediate, intermittent, and thiamine responsive subtypes. The classic form presents in the first week of life with ketoacidosis, hypoglycemia, emesis, neonatal seizures, and hypertonia. The intermediate and intermittent forms present in childhood or later with acute episodes of ataxia and vomiting. (From Adams et al., Principles of Neurology, 6th ed, p936)

Polysaccharides consisting of xylose units.

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.

A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

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 sum of the weight of all the atoms in a molecule.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.

A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.

A class of enzymes that catalyze oxidation-reduction reactions of amino acids.

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.

An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

A genus of gram-positive bacteria whose spores are round to oval and covered by a sheath.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)

Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.

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.

Centrifugation with a centrifuge that develops centrifugal fields of more than 100,000 times gravity. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A enzyme complex that catalyzes the oxidative DECARBOXYLATION and DEAMINATION of GLYCINE into CARBON DIOXIDE; AMMONIA; NADH; and N5N10-methylenetetrahydrofolate. It is composed of four different component protein components referred to as H, P, L, and T.

A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).

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 study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Proteins found in any species of bacterium.

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.

In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.

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.

A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).

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.

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.

The functional hereditary units of BACTERIA.

A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.

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 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.

An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

Proteins prepared by recombinant DNA technology.

A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.

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 process by which two molecules of the same chemical composition form a condensation product or polymer.

Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)

A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)

An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.

A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.

Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.

Deoxyribonucleic acid that makes up the genetic material of bacteria.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme Nomenclature, 1992) EC 2.1.3.2.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.

Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.

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.

Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Oxidoreductases that are specific for ALDEHYDES.

Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.

A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)

Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.

Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

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.

Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.

Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. (1/7511)

BACKGROUND: Polyketides are important compounds with antibiotic and anticancer activities. Several modular polyketide synthases (PKSs) contain a terminal thioesterase (TE) domain probably responsible for the release and concomitant cyclization of the fully processed polyketide chain. Because the TE domain influences qualitative aspects of product formation by engineered PKSs, its mechanism and specificity are of considerable interest. RESULTS: The TE domain of the 6-deoxyerythronolide B synthase was overexpressed in Escherichia coli. When tested against a set of N-acetyl cysteamine thioesters the TE domain did not act as a cyclase, but showed significant hydrolytic specificity towards substrates that mimic important features of its natural substrate. Also the overall rate of polyketide chain release was strongly enhanced by a covalent connection between the TE domain and the terminal PKS module (by as much as 100-fold compared with separate TE and PKS 'domains'). CONCLUSIONS: The inability of the TE domain alone to catalyze cyclization suggests that macrocycle formation results from the combined action of the TE domain and a PKS module. The chain-length and stereochemical preferences of the TE domain might be relevant in the design and engineered biosynthesis of certain novel polyketides. Our results also suggest that the TE domain might loop back to catalyze the release of polyketide chains from both terminal and pre-terminal modules, which may explain the ability of certain naturally occurring PKSs, such as the picromycin synthase, to generate both 12-membered and 14-membered macrolide antibiotics. (+info)

Cloning and characterisation of a novel ompB operon from Vibrio cholerae 569B. (2/7511)

The ompB operon of Vibrio cholerae 569B has been cloned and fully sequenced. The operon encodes two proteins, OmpR and EnvZ, which share sequence identity with the OmpR and EnvZ proteins of a variety of other bacteria. Although the order of the ompR and envZ genes of V. cholerae is similar to that of the ompB operon of E. coli, S. typhimurium and X. nematophilus, the Vibrio operon exhibits a number of novel features. The structural organisation and features of the V. cholerae ompB operon are described. (+info)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (3/7511)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport. (+info)

AMP-activated protein kinase phosphorylation of endothelial NO synthase. (4/7511)

The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function. (+info)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (5/7511)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome. (+info)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (6/7511)

We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3'-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3'-untranslated region of tumor necrosis factor-beta mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3'-untranslated region of tumor necrosis factor-alpha, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5' side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences. (+info)

Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. (7/7511)

The formation of a persistently active cAMP-dependent protein kinase (PKA) is critical for establishing long-term synaptic facilitation (LTF) in Aplysia. The injection of bovine catalytic (C) subunits into sensory neurons is sufficient to produce protein synthesis-dependent LTF. Early in the LTF induced by serotonin (5-HT), an autonomous PKA is generated through the ubiquitin-proteasome-mediated proteolysis of regulatory (R) subunits. The degradation of R occurs during an early time window and appears to be a key function of proteasomes in LTF. Lactacystin, a specific proteasome inhibitor, blocks the facilitation induced by 5-HT, and this block is rescued by injecting C subunits. R is degraded through an allosteric mechanism requiring an elevation of cAMP coincident with the induction of a ubiquitin carboxy-terminal hydrolase. (+info)

Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. (8/7511)

PML/RARalpha is the leukemogenetic protein of acute promyelocytic leukemia (APL). Treatment with retinoic acid (RA) induces degradation of PML/RARalpha, differentiation of leukaemic blasts, and disease remission. However, RA resistance arises during RA treatment of APL patients. To investigate the phenomenon of RA resistance in APL, we generated RA-resistant sublines from APL-derived NB4 cells. The NB4.007/6 RA-resistant subline does not express the PML/RARalpha protein, although its mRNA is detectable at levels comparable to those of the parental cell line. In vitro degradation assays showed that the half-life of PML/RARalpha is less than 30 minutes in NB4.007/6 and longer than 3 hours in NB4. Treatment of NB4.007/6 cells with the proteasome inhibitors LLnL and lactacystin partially restored PML/RARalpha protein expression and resulted in a partial release of the RA-resistant phenotype. Similarly, forced expression of PML/RARalpha, but not RARalpha, into the NB4/007.6 cells restored sensitivity to RA treatment to levels comparable to those of the NB4 cells. These results indicate that constitutive degradation of PML/RARalpha protein may lead to RA resistance and that PML/RARalpha expression is crucial to convey RA sensitivity to APL cells. (+info)

MSUD can cause a range of symptoms, including:

* Seizures
* Developmental delays
* Intellectual disability
* Poor muscle tone
* Vision problems
* Increased risk of infections

If left untreated, MSUD can lead to serious complications such as brain damage, coma, and even death. Treatment typically involves a strict diet that limits the intake of branched-chain amino acids, and may also include supplementation with BCKDH enzyme. In some cases, a liver transplant may be necessary.

MSUD is usually diagnosed in infancy, as newborns who are affected by the disorder may have a distinctive 'maple syrup' odor to their urine. However, it can also be diagnosed in older children and adults if they exhibit symptoms of the condition. Treatment and management of MSUD requires lifelong adherence to a special diet and regular monitoring by a healthcare provider.

Quaternary structure Protein complex Macromolecular assembly Biomolecular complex Neuman, Nicole (2016). "The Complex ... Multienzyme complex carries out a single or a series of biochemical reactions taking place in the cells. It allows to segregate ... Multienzyme complex contains several copies of one or several enzymes (polypeptide chains) packed into one assembly. ... Macromolecular Complex: Trends in Biochemical Sciences". Trends in Biochemical Sciences. 41 (1): 1-3. doi:10.1016/j.tibs. ...

https://en.wikipedia.org/wiki/Multienzyme_complex

... s are multi-enzyme extracellular complexes. Cellulosomes are associated with the cell surface and mediate cell ... Cellulosome complexes are intricate, multi-enzyme machines, produced by many cellulolytic microorganisms. They are produced by ... The birth of the discrete, multi-enzyme cellulosome complex was thus documented. Currently known cellulosome-producing ... Cellulosomes exist as extracellular complexes that are either attached to the cell wall of bacteria or free in solution, where ...

https://en.wikipedia.org/wiki/Cellulosome

Multi-enzyme complexes are likely to have more intricate regulatory mechanisms, and studies have already probed such processes ... More recent work on the regulation of eukaryotic PRK has focused on its ability to form multi-enzyme complexes with other ... Avilan L, Gontero B, Lebreton S, Ricard J (December 1997). "Information transfer in multienzyme complexes--2. The role of Arg64 ... Rault M, Gontero B, Ricard J (May 1991). "Thioredoxin activation of phosphoribulokinase in a chloroplast multi-enzyme complex ...

https://en.wikipedia.org/wiki/Phosphoribulokinase

... is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex is responsible for ... de Kok A, Hengeveld AF, Martin A, Westphal AH (Jun 1998). "The pyruvate dehydrogenase multi-enzyme complex from Gram-negative ... "Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex". Science. 255 (5051): 1544-50. Bibcode: ... Typically PDH is the result of a mutation in the X-linked gene for the E1 subunit of the pyruvate dehydrogenase complex. ...

https://en.wikipedia.org/wiki/Dihydrolipoyl_transacetylase

Leopoldseder S, Hettwer S, Sterner R (November 2006). "Evolution of Multi-Enzyme Complexes: The Case of Tryptophan Synthase". ... "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium". The ... TrpB2i formed transient complexes with TrpA and in the process activated TrpA unidirectionally. The other copy remained outside ... Subunits: Tryptophan synthase typically exists as an α-ββ-α complex. The α and β subunits have molecular masses of 27 and 43 ...

https://en.wikipedia.org/wiki/Tryptophan_synthase

Kresge, Nicole; Robert D. Simoni; Robert L. Hill (21 August 2009). "Multienzyme Complexes and Hydrogen Transfer: the Work of ...

https://en.wikipedia.org/wiki/Perry_A._Frey

"Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex". J. Biol. Chem. 276 (20): 17286-90. doi: ... "Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, ... In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter ... sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex". ...

https://en.wikipedia.org/wiki/Sialidase-1

The purinosome is a putative multi-enzyme complex that carries out de novo purine biosynthesis within the cell. It is ... Thus far, isolation of a multienzyme complex inclusive of all purine biosynthesis enzymes has not been achieved. Purinosome ... The enzymes of the multi-step de novo purine biosynthesis pathway have been postulated to form a multi-enzyme complex to ... "Dynamic regulation of a metabolic multi-enzyme complex by protein kinase CK2". J Biol Chem. 285 (15): 11093-11099. doi:10.1074/ ...

https://en.wikipedia.org/wiki/Purinosome

"Purification and partial characterization of the glycine decarboxylase multienzyme complex from Eubacterium acidaminophilum". ...

https://en.wikipedia.org/wiki/Peptoclostridium_acidaminophilum

"Purification and characterization of a cellulolytic multienzyme complex produced by Neocallimastix patriciarum J11". ... "Purification and characterization of a cellulolytic multienzyme complex produced by Neocallimastix patriciarum J11". ...

https://en.wikipedia.org/wiki/Neocallimastix_patriciarum

Enzymes taking part in IMP synthesis constitute a multienzyme complex in the cell. Evidence demonstrates that there are ... The inosinate synthesis is complex, beginning with a 5-phosphoribosyl-1-pyrophosphate (PRPP). ...

https://en.wikipedia.org/wiki/Inosinic_acid

Mowbray J, Moses V (June 1976). "The tentative identification in Escherichia coli of a multienzyme complex with glycolytic ... Consequently, the importance of these complexes for metabolism in general remains unclear. Some protein complexes contain a ... Srere PA (1987). "Complexes of sequential metabolic enzymes". Annu. Rev. Biochem. 56: 89-124. doi:10.1146/annurev.bi.56.070187. ... The cytosol is a complex mixture of substances dissolved in water. Although water forms the large majority of the cytosol, its ...

https://en.wikipedia.org/wiki/Cytosol

... a bacterial dehydrogenase in a multienzyme complex". FEBS Letters. 168 (2): 217-221. doi:10.1016/0014-5793(84)80249-5. ISSN ...

https://en.wikipedia.org/wiki/Methylotroph

Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase ... 1999). "Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex". Proc. Natl. Acad. Sci. U.S.A. 96 ... Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts ... 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys ...

https://en.wikipedia.org/wiki/DARS_(gene)

... function and relationship in other ribonucleolytic multienzyme complexes". Biochem. Soc. Trans. 30 (2): 150-5. doi:10.1042/ ... The exosome complex (or PM/Scl complex, often just called the exosome) is a multi-protein intracellular complex capable of ... Exosome complexes are found in both eukaryotic cells and archaea, while in bacteria a simpler complex called the degradosome ... In yeast, Rrp44 is associated with all exosome complexes and has a crucial role in the activity of the yeast exosome complex. ...

https://en.wikipedia.org/wiki/Exosome_complex

The composition of this multienzyme may vary depending on the organism. The multiprotein complex RNA degradosome in E. coli ... it is really difficult for RNA to scape from the complex. The RNA degradosome is a huge multi-enzyme association that is ... function and relationship in other ribonucleolytic multienzyme complexes". Biochemical Society Transactions. 30 (2): 150-5. doi ... This multi-protein complex is stimulated by a non-coding RNA, called miRNA in Eukaryotic cells and sRNA in bacteria. Small ...

https://en.wikipedia.org/wiki/Degradosome

... exonucleases in mammalian multienzyme DNA polymerase complexes]". Mol. Biol. (Mosk.). 36 (6): 1055-61. PMID 12500544. Shevelev ...

https://en.wikipedia.org/wiki/TREX2

Spring, S (2014). "Function and Evolution of the Sox Multienzyme Complex in the Marine Gammaproteobacterium Congregibacter ... When grown in culture, C. litoralis KT71 has a generation time of 4.5 hours and prefers to grow on complex substrates where the ... used direct plating on complex low-nutrient media called MPM developed by Schut et al. MPM was designed to mimic seawater. ... and fatty acids as well as more complex substrates like yeast extract and trypticase peptone. Within its genome, genes, ...

https://en.wikipedia.org/wiki/Congregibacter_litoralis

Synthesis is conducted by multienzyme complexes, including peptide synthetases, polypeptide synthases, and tailoring enzymes. ... At the molecular level and in further detail, nodularin is processed in a complex manner to induce toxic effects. During ...

https://en.wikipedia.org/wiki/Nodularin

It is a multienzyme complex which possesses alpha-L-rhamnosidase and beta glucosidase active centers. The E.C. No.(EC 3.2.1.40 ...

https://en.wikipedia.org/wiki/Naringinase

Some studies have suggested the SBPase may be part of a large (900 kDa) multi-enzyme complex along with a number of other ... Suss KH, Arkona C, Manteuffel R, Adler K (June 1993). "Calvin cycle multienzyme complexes are bound to chloroplast thylakoid ... "Origin and distribution of Calvin cycle fructose and sedoheptulose bisphosphatases in plantae and complex algae: a single ... secondary origin of complex red plastids and subsequent propagation via tertiary endosymbioses". Protist. 158 (3): 263-76. doi: ...

https://en.wikipedia.org/wiki/Sedoheptulose-bisphosphatase

"Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex". The Journal of ...

https://en.wikipedia.org/wiki/LIG1

This enzyme is also part of a larger multienzyme complex that channels the intermediates in the catalysis between subunits of ... This gene encodes one subunit of the 2-oxoglutarate dehydrogenase complex. This complex catalyzes the overall conversion of 2- ... "Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex". Journal of ... "Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity". The ...

https://en.wikipedia.org/wiki/OGDH

This multi-enzyme complex is related structurally and functionally to the oxoglutarate dehydrogenase and branched-chain oxo- ... acid dehydrogenase multi-enzyme complexes. The reaction catalysed by pyruvate dehydrogenase complex is: The E1 subunit, called ... Pyruvate dehydrogenase complex (PDC) is a complex of three enzymes that converts pyruvate into acetyl-CoA by a process called ... stearothermophilus pyruvate dehydrogenase multienzyme complex and implications for eucaryote evolution". Cell. 17 (1): 85-93. ...

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex

This enzyme is required for the complete reaction of at least five different multi-enzyme complexes. Additionally, DLD is a ... In these complexes, DLD converts dihydrolipoic acid and NAD+ into lipoic acid and NADH. DLD also has diaphorase activity, being ... November 2003). "Reduction of Fe(III) ions complexed to physiological ligands by lipoyl dehydrogenase and other flavoenzymes in ... "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and ...

https://en.wikipedia.org/wiki/Dihydrolipoamide_dehydrogenase

in Russian)[2] Kurganov B.I., Lyubarev A.E. Enzymes and multienzyme complexes as controllable systems. In: Soviet Scientific ... In Chaetomium thermophilum, a complex of a metabolon exists between fatty acid synthase and a MDa carboxylase, and was observed ... This hypothesis was well accepted in the former USSR and further developed for the complex of glycolytic enzymes (Embden- ... in Russian) [1]. Kurganov B. I, Lyubarev A. E. Hypothetical structure of the complex of glycolytic enzymes (glycolytic ...

https://en.wikipedia.org/wiki/Metabolon

Guiral M, Tron P, Aubert C, Gloter A, Iobbi-Nivol C, Giudici-Orticoni MT (Dec 2005). "A membrane-bound multienzyme, hydrogen- ... oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus". The Journal of Biological ...

https://en.wikipedia.org/wiki/Sulfhydrogenase

The protein encoded by the human PDHA2 gene is part of the pyruvate dehydrogenase multienzyme complex. The entire human complex ... The E1 complex specifically uses the TPP cofactor to cleave the Calpha-C(=O) bond of pyruvate, and then transfer the acetyl ... Overall the complex catalyzes five reactions, with the overall reaction being: Pyruvate + CoA + NAD+ → acetyl-CoA + CO2 There ... The pyruvate dehydrogenase complex is responsible for the oxidative decarboxylation of pyruvate, with the final product being ...

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(lipoamide)_alpha_2

April 2002). "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A ... While defects have been identified in all 3 enzymes of the complex, the E1-α subunit is predominantly the culprit. Malfunction ... Pyruvate Dehydrogenase Complex Deficiency at eMedicine Recny MA, Hager LP (1982). "Reconstitution of native Escherichia coli ... Pyruvate dehydrogenase is usually encountered as a component, referred to as E1, of the pyruvate dehydrogenase complex (PDC). ...

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase

"Specific release of the thioesterase component of the fatty acid synthetase multienzyme complex by limited trypsinization". ... Fatty acid synthase is a multi-enzyme protein that catalyzes fatty acid synthesis. It is not a single enzyme but a whole ... as the domains of the FAS II enzymes are largely homologous to their domain counterparts in FAS I multienzyme polypeptides. ... of yeast FAS and mammalian FAS show two distinct organizations of highly conserved catalytic domains/enzymes in this multi-enzyme ...

https://en.wikipedia.org/wiki/Fatty_acid_synthase

Such enzymes are usually secreted as part of multienzyme complexes that may include dockerins and carbohydrate-binding modules ... In plants cellulose is synthesized at the plasma membrane by rosette terminal complexes (RTCs). The RTCs are hexameric protein ... "Immunogold labeling of rosette terminal cellulose-synthesizing complexes in the vascular plant vigna angularis". The Plant Cell ...

https://en.wikipedia.org/wiki/Cellulose

... structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex". J. ... the core of the 2-oxoglutarate dehydrogenase complex". Proc. Natl. Acad. Sci. U.S.A. 68 (6): 1135-7. Bibcode:1971PNAS...68.1135 ...

https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase

Li Z, Deutscher MP (August 1996). "Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo". Cell ... crystal structures of RNase T-product complexes". Nucleic Acids Research. 40 (16): 8144-54. doi:10.1093/nar/gks548. PMC 3439924 ...

https://en.wikipedia.org/wiki/Ribonuclease_T

A complex of the apoenzyme and citrate at 1.87 A resolution". Journal of Molecular Biology. 226 (3): 867-82. doi:10.1016/0022- ... and multienzyme interaction" (PDF). The Journal of Biological Chemistry. 263 (22): 10687-97. doi:10.1016/S0021-9258(18)38026-8 ... The active site of malate dehydrogenase is a hydrophobic cavity within the protein complex that has specific binding sites for ... Studies have indicated that the binding of the enol form oxaloacetate with the malate dehydrogenase:NADH complex forms much ...

https://en.wikipedia.org/wiki/Malate_dehydrogenase

... and rapC encode for three extremely large and complex multienzymes, RapA, RapB, and RapC, respectively. The gene rapL has been ... Unlike the tacrolimus-FKBP12 complex, which inhibits calcineurin (PP2B), the sirolimus-FKBP12 complex inhibits the mTOR ( ... Sirolimus has complex effects on the immune system-while IL-12 goes up and IL-10 decreases, which suggests an immunostimulatory ... LAM involves lung tissue infiltration with smooth muscle-like cells with mutations of the tuberous sclerosis complex gene (TSC2 ...

https://en.wikipedia.org/wiki/Sirolimus

1991). "Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a ... The branched-chain α-ketoacid dehydrogenase complex (BCKDC or BCKDH complex) is a multi-subunit complex of enzymes that is ... H+ A deficiency in any of the enzymes of this complex as well as an inhibition of the complex as a whole leads to a buildup of ... "Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in ...

https://en.wikipedia.org/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex

They introduced an iron-sulfur complex into the layered arrangement, which when submerged in water and irradiated with light ... is the fermentative conversion of organic substrate to biohydrogen manifested by a diverse group of bacteria using multi enzyme ...

https://en.wikipedia.org/wiki/Hydrogen_economy

... this enzyme forms a complex composed of three components: Three classes of these multienzyme complexes have been characterized ... The oxoglutarate dehydrogenase complex (OGDC) or α-ketoglutarate dehydrogenase complex is an enzyme complex, most commonly ... Many of these allosteric regulators act at the E1 domain of the enzyme complex, but all three domains of the enzyme complex can ... The activity of the enzyme complex is upregulated with high levels of ADP and Pi, Ca2+, and CoA-SH. The enzyme is inhibited by ...

https://en.wikipedia.org/wiki/Oxoglutarate_dehydrogenase_complex

It is not known if the HgcA and HgcB proteins create a multienzyme complex or work sequentially. It has also been shown that ... Similar to the pH effects, different concentrations of available mercury ion lead to different products and complexes of ...

https://en.wikipedia.org/wiki/Mercury_methylation

"Kinetic studies of a soluble alpha beta complex of nitrate reductase A from Escherichia coli. Use of various alpha beta mutants ... Proteins Kinetics of nitrite reductase Kinetics of nitrate reductase The evolution of macromolecules Properties of multienzyme ...

https://en.wikipedia.org/wiki/Athel_Cornish-Bowden

These guidelines enable multi-enzyme cascades to be designed and developed for the conversion of simple, sustainable feedstocks ... to more complex, target molecules." RSC Carbohydrate Chemistry Award (1992) Corday-Morgan Prize (1996) RSC Industrial Organic ...

https://en.wikipedia.org/wiki/Nicholas_Turner_(chemist)

His PhD thesis, titled "Multienzyme organization of encephalomyocarditis virus replication complexes", was supervised by Vadim ...

https://en.wikipedia.org/wiki/Eugene_Koonin

Pyruvate undergoes decarboxylation using the multi-enzyme complex to form acetyl coA which can readily be used in the TCA cycle ... The cell cycle is regulated in cell cycle checkpoints, by a series of signaling factors and complexes such as cyclins, cyclin- ...

https://en.wikipedia.org/wiki/Cell_biology

... since lipoic acid acts as an essential cofactor for several mitochondrial multienzyme complexes, such as pyruvate dehydrogenase ... The consequences of this are diminished oxidative phosphorylation and major alterations in complex lipids, such as increased ... complex (PDHC) and α-ketoglutarate dehydrogenase complex (α-KGDHC), among others. This diminished lipoylation also leads to a ... which has a competitive inhibitory effect on complex II, and also leads to a deficiency of malonyl-CoA. These deficiencies can ...

https://en.wikipedia.org/wiki/Combined_malonic_and_methylmalonic_aciduria

... both of which form multienzyme complexes. Hilbi H, Dehning I, Schink B, Dimroth P (July 1992). "Malonate decarboxylase of ...

https://en.wikipedia.org/wiki/Biotin-dependent_malonate_decarboxylase

... aminotransferase to transfer directly alpha-ketoglutarate to the alpha-ketoglutarate dehydrogenase complex in this multienzyme ... Formation of this ternary complex enables low levels of the alpha-ketoglutarate dehydrogenase complex, in the presence of the ... complex and that mitochondrial malate dehydrogenase can associate with this binary complex to form a ternary complex. ... A complex of the apoenzyme and citrate at 1.87 A resolution". Journal of Molecular Biology. 226 (3): 867-82. doi:10.1016/0022- ...

https://en.wikipedia.org/wiki/Malate_dehydrogenase_2

The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall ... In forming the entire PDH complex, the 289th beta residue, aspartic acid, interacts with the 276th residue of the E2 complex, a ... and is part of the pyruvate dehydrogenase multienzyme complex. Two of the mature PDHB proteins come together with two PDHA ... The entire human complex is 9.5 MDa in size, and has been described as 60-meric, meaning there are over 60 components that are ...

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(lipoamide)_beta

Many of the enzymes for the fatty acid synthesis are organized into a multienzyme complex called fatty acid synthase. The major ...

https://en.wikipedia.org/wiki/Lipogenesis

Spin-label study of the mobility of enzyme-bound lipoic acid in the pyruvate dehydrogenase multienzyme complex of Escherichia ... The role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.. scientific article ... The role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. (English) ... Kinetic analysis of the role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli ...

https://m.wikidata.org/wiki/Q43465585

Multienzyme Complexes / metabolism * Muscle Fibers, Fast-Twitch / chemistry * Muscle Fibers, Fast-Twitch / metabolism ...

https://pubmed.ncbi.nlm.nih.gov/15562249/?dopt=Abstract

The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. Learn ... hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha To use the sharing features on this page, please ... This enzyme complex functions in mitochondria, the energy-producing centers within cells. Mitochondrial trifunctional protein ... The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. ...

https://medlineplus.gov/genetics/gene/hadha/

Fu, J.; Yang, Y.R.; Johnson-Buck, A.; Liu, M.; Liu, Y.; Walter, N.G.; Woodbury, N.W.; Yan, H. Multi-enzyme complexes on DNA ... Wei, Q.; He, S.; Qu, J.; Xia, J. Synthetic multienzyme complexes assembled on virus-like particles for cascade biosynthesis in ... Cellulosomes are multienzyme complexes, produced extracellularly by some anaerobic cellulolytic bacteria species, that break ... Yan and co-workers refashioned DNA to mimic flexible "swinging arms" present in multi-enzyme complexes and multifunctional mega ...

https://www.mdpi.com/1420-3049/26/5/1389

hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha. IEA. KEGG. rno:00410. NCBI chr 6:26,187,969... ...

https://rgd.mcw.edu/rgdweb/ontology/annot.html?acc_id=PW:0000132

the SOS-box multi enzyme complex to launch the DNA-SOS repair ... complexes - S-nitrosothiols and dinitrosyl iron complexes (D ... and two cationic dinitrosyl iron complexes (DNICs) with thiourea - Fe(SС(NH2)2)2(NO)2]2SO4∙H2O (NO-29) and [Fe(SС(NH2)2)2(NO)2] ... complexes are the most abundant nitric oxide- derived cellular adduct: Biological parameters of assembly and disappearance. ... complexes with aliphatic ligands of natural origin cysteine - cisaconite: (CysA) - [Fe2(S(CH2)2NH3)2(NO)4]SO4 2.5 H2O and ...

https://www.researchgate.net/publication/311631607_Vitamin_Para-Aminobenzoic_Acid_PABA_Controls_Generation_of_Nitric_Oxide_NO_In_Vitro_and_its_Biological_Functions_in_the_Bacterial_Cells

Multienzyme Complexes - Preferred Concept UI. M0014188. Scope note. Systems of enzymes which function sequentially by ... MULTIPROTEIN COMPLEXES and MULTIFUNCTIONAL ENZYMES are also available. Allowable Qualifiers:. AD administration & dosage. AE ...

https://decs.bvsalud.org/en/ths/resource/?id=9290&filter=ths_exact_term&q=COMPLEJOS+MULTIENZIM%C3%81TICOS

RNA degrading enzymes and multi-enzyme complexes govern a variety of cellular processes. The role of these enzymes and multi- ... Structural and mechanistic studies on Staphylococcal RNA degrading enzymes and multienzyme complexes Raj, Rishi ... Biophysical Studies on Mycobacterium Tuberculosis σ Factor - Regulatory Protein Complexes Jamithireddy, Anil Kumar ... Protein homeostasis in all organisms is a complex process involving regulatory mechanisms that govern protein synthesis, post- ...

https://etd.iisc.ac.in/handle/2005/1/browse?type=advisor&value=Gopal%2C+B

This implies the involvement of a stably assembled multienzyme complex.. Assuntos. Expressão Gênica , Glucosídeos/análise , ... Forskolin is a unique structurally complex labdane-type diterpenoid used in the treatment of glaucoma and heart failure based ... We approached mAb production in a different way and immunised with a complex mixture of polysaccharides. The multiplexed ...

https://pesquisa.bvsalud.org/portal/?lang=pt&q=au:Motawia,+Mohammed+Saddik

Multi-Enzyme Nano-complexes. Not submitted. 8-1999 Min DJ PhD qualifying exam NSF proposal- Multi-Enzyme Nano-complexes. Not ...

http://www.joeandrade.org/everything/

Effects of adding multienzyme complex on the performance of broilers. Animal Production and Quality Control ...

https://teses.usp.br/index.php?option=com_jumi&fileid=9&Itemid=159&lang=en&id=74131&prog=74001&exp=0&pagina=51

Ingredients: vitalzym extra strength premium softgels are the original, Rutin, Papain, vegetarian multi enzyme complex. Small, ... Pure Encapsulations #ad - Muscular health: systemic Enzyme Complex is formulated to support the overall health of the ... Advanced, cardiovascular, broad spectrum caps promote wellness: our complex extract provides the optimal potency level of ... And Connective Tissue Health* , 180 Capsules, Pure Encapsulations Systemic Enzyme Complex , Supplement to Support Muscle, Joint ...

http://pohsili.com/top-10-systemic-enzymes-for-inflammation-multi-enzyme-nutritional-supplements/

Electron Transport Chain Complex Proteins. *Exosome Multienzyme Ribonuclease Complex. *Fatty Acid Synthase, Type II ... Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES ...

https://profiles.ucdenver.edu/display/219348

Complex:pyruvate dehydrogenase multienzyme complex. *Complex:PYRUVOXID-CPLX. *Complex:quinolinate phosphoribosyltransferase ( ... Protein complexes, mostly from EcoCyc Todo:many of the ones with all caps names or -CPLX are accessions, not complex names. ... Pages in category "E. coli complexes". This category contains only the following page. ... Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=Category:E._coli_complexes&oldid=658515" ...

https://ecoliwiki.org/colipedia/index.php/Category:E._coli_complexes

Component A3a is a multienzyme complex that includes the mcrC gene product, an Fe-protein homolog, an iron-sulfur flavoprotein ... It contains the hydroporphinoid nickel complex coenzyme F430 in its active site, and the Ni center has to be in its Ni(I) ... CODH/ACS complex and protein components involved in electron bifurcation. According to our postulated model of activation, ...

https://etd.auburn.edu/handle/10415/4463

Digeseb® (Multi Enzyme Complex) (1)‎. Vitamin B6 (1)‎. Chasteberry (1)‎. Lemon Balm Leaf (1)‎. ...

https://www.kallistia.com/en-hu/collections/skincare

Exosome Multienzyme Ribonuclease Complex 100% * Trichohepatoenteric Syndrome 76% * B-Lymphocytes 46% * B-Lymphoid Precursor ...

https://utsouthwestern.elsevierpure.com/en/organisations/rheumatology-2/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle&ordering=title&descending=false

Multienzyme Complexes. *Mutant Proteins. *Mycobacterium tuberculosis. *Nanofibers. *Nucleic Acid Conformation. *Oxazolone. * ...

https://connects.catalyst.harvard.edu/Profiles/display/Person/137864/Network/ResearchAreas

A feed specific synergistically acting multi-enzyme complex, produced by SSF technology.. * Energises feed by 100 to 140 kilo ... A feed specific synergistically acting multi-enzyme complex, produced by SSF technology. ... Due to the heterogeneity and complex chemical nature of Xylans, its complete break down requires a complex of several ... During the fermentation yeast peptides complex with minerals to form organic mineral proteinates.. The minerals-peptide complex ...

https://zeusbiotech.com/category/

This gene encodes component E2 of the multi-enzyme pyruvate dehydrogenase complex (PDC). PDC resides in the inner mitochondrial ... The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the ... This gene encodes component E2 of the multi-enzyme pyruvate dehydrogenase complex (PDC). PDC resides in the inner mitochondrial ... The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the ...

https://pharos.nih.gov/targets/ENSP00000280346

ENZIMETIN 5® capsules contain DigeZyme®, a clinically tested multienzyme complex of 5 di... ...

https://www.esensa.rs/en/namena/diarrhea-dehydration-constipation-indigestion/

Zverlov V.V., Schwarz W.H. The Clostridium thermocellum cellulosome - the paradigm of a multienzyme complex. In Ohmiya, K., K. ... Lic16A of Clostridium thermocellum, a non-cellulosomal, heighly complex endo-beta-1,3-glucanase bound to the outer cell surface ... These results were yielded in cooperation with researchers from the Russian Cardiological Research-and-Production Complex. ... an emerging concept for the regulation of bacterial protein complexes? Mol Microbiol. 2006. V. 60. P. 1323-1326. ...

https://img.ras.ru/en/labs/laboratory-protein-engineering

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. ... The four polypeptide chains are arranged nearly linearly in an alpha beta beta alpha order forming a complex 150 A long. The ... The three-dimensional structure of the alpha 2 beta 2 complex of tryptophan synthase from Salmonella typhimurium has been ...

http://bioinformatics.unipr.it/cgi-bin/bioinformatics/B6db/bib.pl/Show?3053720

The glycolytic enzymes (enzymes that oxidize sugars for energy) exemplify this type of multi-enzyme complex. One enzyme ... Two complexes of RNA and protein make up the ribosome, the 30S subunit, and the 50S subunit. (The S stands for Svedberg units, ... The amino acyl-tRNA synthetase complex. A molecular model of aminoacyl tRNA synthetase binding its tRNA. The tRNA is shown as ... The nucleoid is the cellular region that contains the DNA-protein complex that makes up the chromosome. It is not a set region ...

https://sixthedition.microbiologytext.com/book/displayarticle/665

5 formula is a multienzyme complex made up of 5 important enzymes to help with healthy digestion; the enzymes in this formula ... Our Digetox®5 formula is a multienzyme complex made up of 5 important enzymes to help with healthy digestion; the enzymes in ...

https://earthscreationshop.com/products/digetox-5

Each enzyme in this multi-enzyme complex formulation is of food grade and is non-GMO and gluten-free ... All the enzymes used in this multi-enzyme complex are safe in terms of their origin, quality, and efficacy ...

https://fabenol.com/fabenol/salient-features/

Electron Transport Complex II * Hemin * Mitochondria, Heart * Multienzyme Complexes * Oxidoreductases * Protein Binding ...

https://scholars.duke.edu/display/pub657825

Multienzyme Complexes. *Mutation. *Mutation Rate. *NF-kappa B. *Oligonucleotide Array Sequence Analysis ...

https://profiles.umassmed.edu/display/132805/Network/ResearchAreas

Developing multi-enzyme cocktails is one strategy being explored for industrial processing. Free-Living Lignocellulose ... Eukaryotes also use lignocellulose as a carbon source but cannot do so without associations with complex communities of ... Lignocellulose serves as a highly abundant, yet highly complex, carbon source for many diverse microorganisms, and its ...

https://asm.org/Articles/2022/March/Lignocellulose-Degrading-Microbes-Give-Plants-New

... produces death of dopaminergic substantia nigral cells by inhibiting the mitochondrial NADH dehydrogenase multienzyme complex, ... produces death of dopaminergic substantia nigral cells by inhibiting the mitochondrial NADH dehydrogenase multienzyme complex, ...

https://www.dpag.ox.ac.uk/publications/106590

Enzymes Pyruvate Subunit Enzyme complex DigeZyme Protein Molecular Alpha Pathways Dehydrogenase Enzyme Tree Assembly

Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides. (ucdenver.edu)
Advanced, cardiovascular, broad spectrum caps promote wellness: our complex extract provides the optimal potency level of proteolytic enzymes that may assist with IBS, gastrointestinal, & support the return of blood volume & flow. (pohsili.com)

The role of lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. (wikidata.org)
Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources. (wikidata.org)
Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. (wikidata.org)
Escherichia coli pyruvate dehydrogenase complex. (wikidata.org)
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. (nih.gov)
This gene encodes component E2 of the multi-enzyme pyruvate dehydrogenase complex (PDC). (nih.gov)

The subunit molecular weights of the alpha-ketoacid dehydrogenase multienzyme complexes from E. coli. (wikidata.org)
Other mutations replace one amino acid with another amino acid in the alpha subunit, which probably alters the subunit's structure and disrupts all three functions of the enzyme complex. (medlineplus.gov)

The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. (medlineplus.gov)
This enzyme complex functions in mitochondria, the energy-producing centers within cells. (medlineplus.gov)
Ingredients: vitalzym extra strength premium softgels are the original, Rutin, Papain, vegetarian multi enzyme complex. (pohsili.com)

ENZIMETIN 5® capsules contain DigeZyme®, a clinically tested multienzyme complex of 5 di. (esensa.rs)

Component A3a is a multienzyme complex that includes the mcrC gene product, an Fe-protein homolog, an iron-sulfur flavoprotein, CODH/ACS complex and protein components involved in electron bifurcation. (auburn.edu)

Proteins associated with metabolic pathways have received considerable attention in an effort to understand the molecular details of the complex reactions catalyzed in vivo. (iisc.ac.in)

The three-dimensional structure of the alpha 2 beta 2 complex of tryptophan synthase from Salmonella typhimurium has been determined by x-ray crystallography at 2.5 A resolution. (unipr.it)
The four polypeptide chains are arranged nearly linearly in an alpha beta beta alpha order forming a complex 150 A long. (unipr.it)

The minerals-peptide complex of ORGANOMIN-Forte is absorbed intact to the blood stream by peptide or amino acid uptake pathways rather than the normal metal ion uptake mechanism. (zeusbiotech.com)

Icosahedral pyruvate dehydrogenase (PDH) enzyme complexes are molecular machines consisting of a central E2 core decorated by a shell of peripheral enzymes (E1 and E3) found localized at a distance of approximately 75-90 A from the core. (nih.gov)
Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit. (nih.gov)
The three-dimensional solution structure of a 51-residue synthetic peptide comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli has been determined by nuclear magnetic resonance spectroscopy and hybrid distance geometry-dynamical simulated annealing calculations. (nih.gov)
In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. (nih.gov)

This catalytic machinery explains the existence of lysosomal enzyme complexes that can be dynamically assembled and disassembled to efficiently and quickly adapt to the pool of substrates to be processed or degraded, adding extra tiers to the regulation of the individual protein components. (nih.gov)
The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. (medlineplus.gov)
This enzyme complex functions in mitochondria, the energy-producing centers within cells. (medlineplus.gov)
Other mutations replace one amino acid with another amino acid in the alpha subunit, which probably alters the subunit's structure and disrupts all three functions of the enzyme complex. (medlineplus.gov)
Dr. Neuman is extending the use of single-molecule techniques to dissect multi-enzyme complex formation and activity. (nih.gov)

A technique or tool used to analyze choices for complex decisions, by organizing them, for analysis, into a tree structure. (nih.gov)

15. Hypoxia drives the assembly of the multienzyme purinosome complex. (nih.gov)

Anatomy4

Organisms12

Diseases1

Chemicals and Drugs65

Analytical, Diagnostic and Therapeutic Techniques and Equipment13

Phenomena and Processes24

Technology, Industry, Agriculture1

Information Science3

Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. (1/7511)

Cloning and characterisation of a novel ompB operon from Vibrio cholerae 569B. (2/7511)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (3/7511)

AMP-activated protein kinase phosphorylation of endothelial NO synthase. (4/7511)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (5/7511)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (6/7511)

Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. (7/7511)

Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. (8/7511)

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Multienzyme Complexes

Pyruvate Dehydrogenase Complex

Dihydrolipoyllysine-Residue Acetyltransferase

Dihydrolipoamide Dehydrogenase

Ketone Oxidoreductases

Thioctic Acid

Geobacillus stearothermophilus

Ketoglutarate Dehydrogenase Complex

Mitochondrial Trifunctional Protein

Enoyl-CoA Hydratase

Acetyl-CoA C-Acyltransferase

Glycine Dehydrogenase (Decarboxylating)

Thermoanaerobacterium

Pyruvate Dehydrogenase (Lipoamide)

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)

Cellulases

Racemases and Epimerases

Clostridium thermocellum

Cellulosomes

Glycine Decarboxylase Complex H-Protein

3-Hydroxyacyl CoA Dehydrogenases

Acetyltransferases

Aminomethyltransferase

Escherichia coli

Caloric Restriction

Cathepsin A

Thiamine Pyrophosphate

Hydroxymethyl and Formyl Transferases

Amino Acyl-tRNA Synthetases

Fatty Acid Synthases

Molecular Sequence Data

Rhodotorula

Ethylmaleimide

Amino Acid Sequence

Dodecenoyl-CoA Isomerase

Kinetics

Aspartate-tRNA Ligase

Cellulase

Maple Syrup Urine Disease

Xylans

Acetyl Coenzyme A

Methanosarcina

Isomerases

Chromatography, Gel

Protein Conformation

Molecular Weight

Binding Sites

Electrophoresis, Polyacrylamide Gel

Pyruvates

Models, Molecular

Peptide Synthases

Cellulose

Amino Acid Oxidoreductases

Acyltransferases

Malate Dehydrogenase

NAD

Saccharopolyspora

Catalysis

Coenzyme A

Substrate Specificity

Catalytic Domain

Base Sequence

Pyruvic Acid

Transferases

Cloning, Molecular

Ultracentrifugation

Glycine Decarboxylase Complex

Pseudomonas

Sequence Homology, Amino Acid

Protein Structure, Quaternary

Fatty Acids

Crystallography, X-Ray

Bacterial Proteins

Ligases

Operon

Protein Binding

Oxidation-Reduction

Mutation

Protein Structure, Secondary

Genes, Bacterial