A species of gram-positive, thermophilic, cellulolytic bacteria in the family Clostridaceae. It degrades and ferments CELLOBIOSE and CELLULOSE to ETHANOL in the CELLULOSOME.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.
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.
Extracellular structures found in a variety of microorganisms. They contain CELLULASES and play an important role in the digestion of CELLULOSE.
A disaccharide consisting of two glucose units in beta (1-4) glycosidic linkage. Obtained from the partial hydrolysis of cellulose.
An exocellulase with specificity for the hydrolysis of 1,4-beta-D-glucosidic linkages in CELLULOSE and cellotetraose. It catalyzes the hydrolysis of terminal non-reducing ends of beta-D-glucosides with release of CELLOBIOSE.
A common inhabitant of the colon flora in human infants and sometimes in adults. It produces a toxin that causes pseudomembranous enterocolitis (ENTEROCOLITIS, PSEUDOMEMBRANOUS) in patients receiving antibiotic therapy.
A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.
Infections with bacteria of the genus CLOSTRIDIUM.
A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans.
Polysaccharides consisting of xylose units.
An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.
A species of anaerobic, gram-positive, rod-shaped bacteria in the family Clostridiaceae that produces proteins with characteristic neurotoxicity. It is the etiologic agent of BOTULISM in humans, wild fowl, HORSES; and CATTLE. Seven subtypes (sometimes called antigenic types, or strains) exist, each producing a different botulinum toxin (BOTULINUM TOXINS). The organism and its spores are widely distributed in nature.
Dextrins are a group of partially degraded and digestible starches, formed through the hydrolysis of starch by heat, acids, or enzymes, consisting of shorter chain polymers of D-glucose units linked mainly by α-(1→4) and α-(1→6) glycosidic bonds.
Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.
Proteins found in any species of bacterium.
Tetroses are uncommon sugars (monosaccharides) with four carbon atoms, having an aldehyde functional group at the first carbon atom, and forming ring structures in their cyclic forms, primarily found in complex carbohydrates and certain natural products.
Glycoside Hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds, resulting in the breakdown of complex carbohydrates and oligosaccharides into simpler sugars.
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.
An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.
An enzyme that catalyzes the transfer of a phosphate group to the 5'-terminal hydroxyl groups of DNA and RNA. EC 2.7.1.78.
Polysaccharides composed of repeating glucose units. They can consist of branched or unbranched chains in any linkages.
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.
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 process of cleaving a chemical compound by the addition of a molecule of water.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
An acute inflammation of the INTESTINAL MUCOSA that is characterized by the presence of pseudomembranes or plaques in the SMALL INTESTINE (pseudomembranous enteritis) and the LARGE INTESTINE (pseudomembranous colitis). It is commonly associated with antibiotic therapy and CLOSTRIDIUM DIFFICILE colonization.
An exocellulase with specificity for 1,3-beta-D-glucasidic linkages. It catalyzes hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing GLUCOSE.
The functional hereditary units of BACTERIA.
A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.
An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.
A species of gram-positive bacteria in the family Clostridiaceae, used for the industrial production of SOLVENTS.
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.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
The cause of TETANUS in humans and domestic animals. It is a common inhabitant of human and horse intestines as well as soil. Two components make up its potent exotoxin activity, a neurotoxin and a hemolytic toxin.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
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.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
A species of gram-positive bacteria in the family Clostridiaceae. It is a cellulolytic, mesophilic species isolated from decayed GRASS.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.
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.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
A species of gram-positive bacteria in the family Clostridiaceae, found in INTESTINES and SOIL.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Structural insights into the mechanism of formation of cellulosomes probed by small angle X-ray scattering. (1/130)

Exploring the mechanism by which the multiprotein complexes of cellulolytic organisms, the cellulosomes, attain their exceptional synergy is a challenge for biologists. We have studied the solution structures of the Clostridium cellulolyticum cellulosomal enzyme Cel48F in the free and complexed states with cohesins from Clostridium thermocellum and Clostridium cellulolyticum by small angle x-ray scattering in order to investigate the conformational events likely to occur upon complexation. The solution structure of the free cellulase indicates that the dockerin module is folded, whereas the linker connecting the catalytic module to the dockerin is extended and flexible. Remarkably, the docking of the different cohesins onto Cel48F leads to a pleating of the linker. The global structure determined here allowed modeling of the atomic structure of the C. cellulolyticum dockerin-cohesin interface, highlighting the local differences between both organisms responsible for the species specificity.  (+info)

Design and production in Aspergillus niger of a chimeric protein associating a fungal feruloyl esterase and a clostridial dockerin domain. (2/130)

A chimeric enzyme associating feruloyl esterase A (FAEA) from Aspergillus niger and dockerin from Clostridium thermocellum was produced in A. niger. A completely truncated form was produced when the dockerin domain was located downstream of the FAEA (FAEA-Doc), whereas no chimeric protein was produced when the bacterial dockerin domain was located upstream of the FAEA (Doc-FAEA). Northern blot analysis showed similar transcript levels for the two constructs, indicating a posttranscriptional bottleneck for Doc-FAEA production. The sequence encoding the first 514 amino acids from A. niger glucoamylase and a dibasic proteolytic processing site (kex-2) were fused upstream of the Doc-FAEA sequence. By using this fusion strategy, the esterase activity found in the extracellular medium was 20-fold-higher than that of the wild-type reference strain, and the production yield was estimated to be about 100 mg of chimeric protein/liter. Intracellular and extracellular production was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, dockerin-cohesin interaction assays, and Western blotting. Labeled cohesins detected an intact extracellular Doc-FAEA of about 43 kDa and a cleaved-off dockerin domain of about 8 kDa. In addition, an intracellular 120-kDa protein was recognized by using labeled cohesins and antibodies raised against FAEA. This protein corresponded to the unprocessed Doc-FAEA form fused to glucoamylase. In conclusion, these results indicated that translational fusion to glucoamylase improved the secretion efficiency of a chimeric Doc-FAEA protein and allowed production of the first functional fungal enzyme joined to a bacterial dockerin.  (+info)

Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA. (3/130)

Cellobiohydrolase CbhA from Clostridium thermocellum cellulosome is a multi-modular protein composed starting from the N-terminus of a carbohydrate-binding module (CBM) of family 4, an immunoglobulin(Ig)-like module, a catalytic module of family 9 glycoside hydrolases (GH9), X1(1) and X1(2) modules, a CBM of family 3 and a dockerin module. Deletion of the Ig-like module from the Ig-GH9 construct results in complete inactivation of the GH9 module. The crystal structure of the Ig-GH9 module pair reveals the existence of an extensive module interface composed of over 40 amino acid residues of both modules and maintained through a large number of hydrophilic and hydrophobic interactions. To investigate the importance of these interactions between the two modules, we compared the secondary and tertiary structures and thermostabilities of the individual Ig-like and GH9 modules and the Ig-GH9 module pair using both circular dichroism (CD) spectroscopy and differential scanning calorimetry (DSC). Thr230, Asp262 and Asp264 of the Ig-like module are located in the module interface of the Ig-GH9 module pair and are suggested to be important in 'communication' between the modules. These residues were mutated to alanyl residues. The structure, stability and catalytic properties of the native Ig-GH9 and its D264A and T230A/D262A mutants were compared. The results indicate that despite being able to fold relatively independently, the Ig-like and GH9 modules interact and these interactions affect the final fold and stability of each module. Mutations of one or two amino acid residues lead to destabilization and change of the mechanism of thermal unfolding of the polypeptides. The enzymatic properties of native Ig-GH9, D264A and T230A/D262A mutants are similar. The results indicate that inactivation of the GH9 module occurs as a result of multiple structural disturbances finally affecting the topology of the catalytic center.  (+info)

Regulation of cellulase synthesis in batch and continuous cultures of Clostridium thermocellum. (4/130)

Regulation of cell-specific cellulase synthesis (expressed in milligrams of cellulase per gram [dry weight] of cells) by Clostridium thermocellum was investigated using an enzyme-linked immunosorbent assay protocol based on antibody raised against a peptide sequence from the scaffoldin protein of the cellulosome (Zhang and Lynd, Anal. Chem. 75:219-227, 2003). The cellulase synthesis in Avicel-grown batch cultures was ninefold greater than that in cellobiose-grown batch cultures. In substrate-limited continuous cultures, however, the cellulase synthesis with Avicel-grown cultures was 1.3- to 2.4-fold greater than that in cellobiose-grown cultures, depending on the dilution rate. The differences between the cellulase yields observed during carbon-limited growth on cellulose and the cellulase yields observed during carbon-limited growth on cellobiose at the same dilution rate suggest that hydrolysis products other than cellobiose affect cellulase synthesis during growth on cellulose and/or that the presence of insoluble cellulose triggers an increase in cellulase synthesis. Continuous cellobiose-grown cultures maintained either at high dilution rates or with a high feed substrate concentration exhibited decreased cellulase synthesis; there was a large (sevenfold) decrease between 0 and 0.2 g of cellobiose per liter, and there was a much more gradual further decrease for cellobiose concentrations >0.2 g/liter. Several factors suggest that cellulase synthesis in C. thermocellum is regulated by catabolite repression. These factors include: (i) substantially higher cellulase yields observed during batch growth on Avicel than during batch growth on cellobiose, (ii) a strong negative correlation between the cellobiose concentration and the cellulase yield in continuous cultures with varied dilution rates at a constant feed substrate concentration and also with varied feed substrate concentrations at a constant dilution rate, and (iii) the presence of sequences corresponding to key elements of catabolite repression systems in the C. thermocellum genome.  (+info)

Functions of family-22 carbohydrate-binding module in Clostridium thermocellum Xyn10C. (5/130)

Clostridium thermocellum xylanase Xyn10C (formerly XynC) is a modular enzyme, comprising a family-22 carbohydrate-binding module (CBM), a family-10 catalytic module of the glycoside hydrolases, and a dockerin module responsible for cellulosome assembly consecutively from the N-terminus. To study the functions of the CBM, truncated derivatives of Xyn10C were constructed: a recombinant catalytic module polypeptide (rCM), a family-22 CBM polypeptide (rCBM), and a polypeptide composed of the family-22 CBM and CM (rCBM-CM). The recombinant proteins were characterized by enzyme and binding assays. Although the catalytic activity of rCBM-CM toward insoluble xylan was four times higher than that of rCM toward the same substrate, removal of the CBM did not severely affect catalytic activity toward soluble xylan or beta-1,3-1,4-glucan. rCBM showed an affinity for amorphous celluloses and insoluble and soluble xylan in qualitative binding assays. The optimum temperature of rCBM-CM was 80 degrees C and that of rCM was 60 degrees C. These results indicate that the family-22 CBM of C. thermocellum Xyn10C not only was responsible for the binding of the enzyme to the substrates, but also contributes to the stability of the CM in the presence of the substrate at high temperatures.  (+info)

Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin. (6/130)

In recent work, we reported the self-assembly of a comprehensive set of defined "bifunctional" chimeric cellulosomes. Each complex contained the following: (i) a chimeric scaffoldin possessing a cellulose-binding module and two cohesins of divergent specificity and (ii) two cellulases, each bearing a dockerin complementary to one of the divergent cohesins. This approach allowed the controlled integration of desired enzymes into a multiprotein complex of predetermined stoichiometry and topology. The observed enhanced synergy on recalcitrant substrates by the bifunctional designer cellulosomes was ascribed to two major factors: substrate targeting and proximity of the two catalytic components. In the present work, the capacity of the previously described chimeric cellulosomes was amplified by developing a third divergent cohesin-dockerin device. The resultant trifunctional designer cellulosomes were assayed on homogeneous and complex substrates (microcrystalline cellulose and straw, respectively) and found to be considerably more active than the corresponding free enzyme or bifunctional systems. The results indicate that the synergy between two prominent cellulosomal enzymes (from the family-48 and -9 glycoside hydrolases) plays a crucial role during the degradation of cellulose by cellulosomes and that one dominant family-48 processive endoglucanase per complex is sufficient to achieve optimal levels of synergistic activity. Furthermore cooperation within a cellulosome chimera between cellulases and a hemicellulase from different microorganisms was achieved, leading to a trifunctional complex with enhanced activity on a complex substrate.  (+info)

Cellulase, clostridia, and ethanol. (7/130)

Biomass conversion to ethanol as a liquid fuel by the thermophilic and anaerobic clostridia offers a potential partial solution to the problem of the world's dependence on petroleum for energy. Coculture of a cellulolytic strain and a saccharolytic strain of Clostridium on agricultural resources, as well as on urban and industrial cellulosic wastes, is a promising approach to an alternate energy source from an economic viewpoint. This review discusses the need for such a process, the cellulases of clostridia, their presence in extracellular complexes or organelles (the cellulosomes), the binding of the cellulosomes to cellulose and to the cell surface, cellulase genetics, regulation of their synthesis, cocultures, ethanol tolerance, and metabolic pathway engineering for maximizing ethanol yield.  (+info)

Regulation of major cellulosomal endoglucanases of Clostridium thermocellum differs from that of a prominent cellulosomal xylanase. (8/130)

The expression of scaffoldin-anchoring genes and one of the major processive endoglucanases (CelS) from the cellulosome of Clostridium thermocellum has been shown to be dependent on the growth rate. For the present work, we studied the gene regulation of selected cellulosomal endoglucanases and a major xylanase in order to examine the previously observed substrate-linked alterations in cellulosome composition. For this purpose, the transcript levels of genes encoding endoglucanases CelB, CelG, and CelD and the family 10 xylanase XynC were determined in batch cultures, grown on either cellobiose or cellulose, and in carbon-limited continuous cultures at different dilution rates. Under all conditions tested, the transcript levels of celB and celG were at least 10-fold higher than that of celD. Like the major processive endoglucanase CelS, the transcript levels of these endoglucanase genes were also dependent on the growth rate. Thus, at a rate of 0.04 h(-1), the levels of celB, celG, and celD were threefold higher than those obtained in cultures grown at maximal rates (0.35 h(-1)) on cellobiose. In contrast, no clear correlation was observed between the transcript level of xynC and the growth rate-the levels remained relatively high, fluctuating between 30 and 50 transcripts per cell. The results suggest that the regulation of C. thermocellum endoglucanases is similar to that of the processive endoglucanase celS but differs from that of a major cellulosomal xylanase in that expression of the latter enzyme is independent of the growth rate.  (+info)

'Clostridium thermocellum' is a type of anaerobic, gram-positive bacterium that is known for its ability to produce cellulases and break down cellulose. It is thermophilic, meaning it grows optimally at higher temperatures, typically between 55-70°C. This organism is of interest in the field of bioenergy because of its potential to convert plant biomass into useful products such as biofuels. However, it's important to note that this bacterium can also produce harmful metabolic byproducts and can be potentially pathogenic to humans.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

Cellulase is a type of enzyme that breaks down cellulose, which is a complex carbohydrate and the main structural component of plant cell walls. Cellulases are produced by certain bacteria, fungi, and protozoans, and are used in various industrial applications such as biofuel production, food processing, and textile manufacturing. In the human body, there are no known physiological roles for cellulases, as humans do not produce these enzymes and cannot digest cellulose.

Cellulose is a complex carbohydrate that is the main structural component of the cell walls of green plants, many algae, and some fungi. It is a polysaccharide consisting of long chains of beta-glucose molecules linked together by beta-1,4 glycosidic bonds. Cellulose is insoluble in water and most organic solvents, and it is resistant to digestion by humans and non-ruminant animals due to the lack of cellulase enzymes in their digestive systems. However, ruminants such as cows and sheep can digest cellulose with the help of microbes in their rumen that produce cellulase.

Cellulose has many industrial applications, including the production of paper, textiles, and building materials. It is also used as a source of dietary fiber in human food and animal feed. Cellulose-based materials are being explored for use in biomedical applications such as tissue engineering and drug delivery due to their biocompatibility and mechanical properties.

Cellulosomes are large, complex enzymatic structures produced by certain anaerobic bacteria that allow them to break down and consume cellulose, a major component of plant biomass. These structures are composed of multiple enzymes that work together in a coordinated manner to degrade cellulose into simpler sugars, which the bacteria can then use as a source of energy and carbon.

The individual enzymes in a cellulosome are non-covalently associated with a central scaffoldin protein, forming a multi-enzyme complex. The scaffoldin protein contains cohesin modules that bind to dockerin modules on the enzyme subunits, creating a highly organized and stable structure.

Cellulosomes have been identified in several species of anaerobic bacteria, including members of the genera Clostridium and Ruminococcus. They are thought to play a key role in the global carbon cycle by breaking down plant material and releasing carbon dioxide back into the atmosphere.

Cellobiose is a disaccharide made up of two molecules of glucose joined by a β-1,4-glycosidic bond. It is formed when cellulose or beta-glucans are hydrolyzed, and it can be further broken down into its component glucose molecules by the action of the enzyme beta-glucosidase. Cellobiose has a sweet taste, but it is not as sweet as sucrose (table sugar). It is used in some industrial processes and may have potential applications in the food industry.

Cellulose 1,4-beta-Cellobiosidase is an enzyme that catalyzes the hydrolysis of cellulose, a complex carbohydrate and the main structural component of plant cell walls, into simpler sugars. Specifically, this enzyme breaks down cellulose by cleaving the 1,4-beta-glycosidic bonds between the cellobiose units that make up the cellulose polymer, releasing individual cellobiose molecules (disaccharides consisting of two glucose molecules). This enzyme is also known as cellobiohydrolase or beta-1,4-D-glucan cellobiohydrolase. It plays a crucial role in the natural breakdown of plant material and is widely used in various industrial applications, such as biofuel production and pulp and paper manufacturing.

'Clostridium difficile' (also known as 'C. difficile' or 'C. diff') is a type of Gram-positive, spore-forming bacterium that can be found in the environment, including in soil, water, and human and animal feces. It is a common cause of healthcare-associated infections, particularly in individuals who have recently received antibiotics or have other underlying health conditions that weaken their immune system.

C. difficile produces toxins that can cause a range of symptoms, from mild diarrhea to severe colitis (inflammation of the colon) and potentially life-threatening complications such as sepsis and toxic megacolon. The most common toxins produced by C. difficile are called TcdA and TcdB, which damage the lining of the intestine and cause inflammation.

C. difficile infections (CDIs) can be difficult to treat, particularly in severe cases or in patients who have recurrent infections. Treatment typically involves discontinuing any unnecessary antibiotics, if possible, and administering specific antibiotics that are effective against C. difficile, such as metronidazole, vancomycin, or fidaxomicin. In some cases, fecal microbiota transplantation (FMT) may be recommended as a last resort for patients with recurrent or severe CDIs who have not responded to other treatments.

Preventing the spread of C. difficile is critical in healthcare settings, and includes measures such as hand hygiene, contact precautions, environmental cleaning, and antibiotic stewardship programs that promote the appropriate use of antibiotics.

Xylosidases are a group of enzymes that catalyze the hydrolysis of xylosides, which are glycosides with a xylose sugar. Specifically, they cleave the terminal β-1,4-linked D-xylopyranoside residues from various substrates such as xylooligosaccharides and xylan. These enzymes play an important role in the breakdown and metabolism of plant-derived polysaccharides, particularly hemicelluloses, which are a major component of plant biomass. Xylosidases have potential applications in various industrial processes, including biofuel production and animal feed manufacturing.

Clostridium infections are caused by bacteria of the genus Clostridium, which are gram-positive, rod-shaped, spore-forming, and often anaerobic organisms. These bacteria can be found in various environments, including soil, water, and the human gastrointestinal tract. Some Clostridium species can cause severe and potentially life-threatening infections in humans. Here are some of the most common Clostridium infections with their medical definitions:

1. Clostridioides difficile infection (CDI): An infection caused by the bacterium Clostridioides difficile, previously known as Clostridium difficile. It typically occurs after antibiotic use disrupts the normal gut microbiota, allowing C. difficile to overgrow and produce toxins that cause diarrhea, colitis, and other gastrointestinal symptoms. Severe cases can lead to sepsis, toxic megacolon, or even death.
2. Clostridium tetani infection: Also known as tetanus, this infection is caused by the bacterium Clostridium tetani. The spores of this bacterium are commonly found in soil and animal feces. They can enter the body through wounds, cuts, or punctures, germinate, and produce a potent exotoxin called tetanospasmin. This toxin causes muscle stiffness and spasms, particularly in the neck and jaw (lockjaw), which can lead to difficulty swallowing, breathing, and potentially fatal complications.
3. Clostridium botulinum infection: This infection is caused by the bacterium Clostridium botulinum and results in botulism, a rare but severe paralytic illness. The bacteria produce neurotoxins (botulinum toxins) that affect the nervous system, causing symptoms such as double vision, drooping eyelids, slurred speech, difficulty swallowing, dry mouth, and muscle weakness. In severe cases, botulism can lead to respiratory failure and death.
4. Gas gangrene (Clostridium perfringens infection): A rapidly progressing soft tissue infection caused by Clostridium perfringens or other clostridial species. The bacteria produce potent exotoxins that cause tissue destruction, gas production, and widespread necrosis. Gas gangrene is characterized by severe pain, swelling, discoloration, and a foul-smelling discharge. If left untreated, it can lead to sepsis, multi-organ failure, and death.
5. Clostridioides difficile infection (C. difficile infection): Although not caused by a typical clostridial species, C. difficile is a gram-positive, spore-forming bacterium that can cause severe diarrhea and colitis, particularly in hospitalized patients or those who have recently taken antibiotics. The bacteria produce toxins A and B, which damage the intestinal lining and contribute to inflammation and diarrhea. C. difficile infection can range from mild to life-threatening, with complications such as sepsis, toxic megacolon, and bowel perforation.

Xylan Endo-1,3-beta-Xylosidase is an enzyme that breaks down xylan, which is a major component of hemicellulose in plant cell walls. This enzyme specifically catalyzes the hydrolysis of 1,3-beta-D-xylosidic linkages in xylans, resulting in the release of xylose units from the xylan backbone. It is involved in the process of breaking down plant material for various industrial applications and in the natural decomposition of plants by microorganisms.

Xylans are a type of complex carbohydrate, specifically a hemicellulose, that are found in the cell walls of many plants. They are made up of a backbone of beta-1,4-linked xylose sugar molecules and can be substituted with various side groups such as arabinose, glucuronic acid, and acetyl groups. Xylans are indigestible by humans, but they can be broken down by certain microorganisms in the gut through a process called fermentation, which can produce short-chain fatty acids that have beneficial effects on health.

Beta-glucosidase is an enzyme that breaks down certain types of complex sugars, specifically those that contain a beta-glycosidic bond. This enzyme is found in various organisms, including humans, and plays a role in the digestion of some carbohydrates, such as cellulose and other plant-based materials.

In the human body, beta-glucosidase is produced by the lysosomes, which are membrane-bound organelles found within cells that help break down and recycle various biological molecules. Beta-glucosidase is involved in the breakdown of glycolipids and gangliosides, which are complex lipids that contain sugar molecules.

Deficiencies in beta-glucosidase activity can lead to certain genetic disorders, such as Gaucher disease, in which there is an accumulation of glucocerebrosidase, a type of glycolipid, within the lysosomes. This can result in various symptoms, including enlargement of the liver and spleen, anemia, and bone pain.

'Clostridium botulinum' is a gram-positive, rod-shaped, anaerobic bacteria that produces one or more neurotoxins known as botulinum toxins. These toxins are among the most potent naturally occurring biological poisons and can cause a severe form of food poisoning called botulism in humans and animals. Botulism is characterized by symmetrical descending flaccid paralysis, which can lead to respiratory and cardiovascular failure, and ultimately death if not treated promptly.

The bacteria are widely distributed in nature, particularly in soil, sediments, and the intestinal tracts of some animals. They can form spores that are highly resistant to heat, chemicals, and other environmental stresses, allowing them to survive for long periods in adverse conditions. The spores can germinate and produce vegetative cells and toxins when they encounter favorable conditions, such as anaerobic environments with appropriate nutrients.

Human botulism can occur through three main routes of exposure: foodborne, wound, and infant botulism. Foodborne botulism results from consuming contaminated food containing preformed toxins, while wound botulism occurs when the bacteria infect a wound and produce toxins in situ. Infant botulism is caused by the ingestion of spores that colonize the intestines and produce toxins, mainly affecting infants under one year of age.

Prevention measures include proper food handling, storage, and preparation practices, such as cooking and canning foods at appropriate temperatures and for sufficient durations. Wound care and prompt medical attention are crucial in preventing wound botulism. Vaccines and antitoxins are available for prophylaxis and treatment of botulism in high-risk individuals or in cases of confirmed exposure.

Dextrins are a group of carbohydrates that are produced by the hydrolysis of starches. They are made up of shorter chains of glucose molecules than the original starch, and their molecular weight and physical properties can vary depending on the degree of hydrolysis. Dextrins are often used in food products as thickeners, stabilizers, and texturizers, and they also have applications in industry as adhesives and binders. In a medical context, dextrins may be used as a source of calories for patients who have difficulty digesting other types of carbohydrates.

Endo-1,4-beta Xylanases are a type of enzyme that catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans, which are complex polysaccharides made up of beta-1,4-linked xylose residues. Xylan is a major hemicellulose component found in the cell walls of plants, and endo-1,4-beta Xylanases play an important role in the breakdown and digestion of plant material by various organisms, including bacteria, fungi, and animals. These enzymes are widely used in industrial applications, such as biofuel production, food processing, and pulp and paper manufacturing, to break down xylans and improve the efficiency of various processes.

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.

Tetroses are a type of monosaccharides, which are simple sugars that cannot be broken down into simpler units by hydrolysis. Tetroses have four carbon atoms and are aldotetroses, meaning they contain an aldehyde functional group at the first carbon atom.

There are two naturally occurring tetroses: erythrose and threose. Erythrose has its hydroxyl groups on the second and fourth carbon atoms, while threose has its hydroxyl groups on the second and third carbon atoms. Tetroses can participate in various chemical reactions, including forming glycosidic bonds with other monosaccharides to create disaccharides or polysaccharides. However, tetroses are not as common as other monosaccharides, such as pentoses and hexoses.

Glycoside hydrolases are a class of enzymes that catalyze the hydrolysis of glycosidic bonds found in various substrates such as polysaccharides, oligosaccharides, and glycoproteins. These enzymes break down complex carbohydrates into simpler sugars by cleaving the glycosidic linkages that connect monosaccharide units.

Glycoside hydrolases are classified based on their mechanism of action and the type of glycosidic bond they hydrolyze. The classification system is maintained by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme in this class is assigned a unique Enzyme Commission (EC) number, which reflects its specificity towards the substrate and the type of reaction it catalyzes.

These enzymes have various applications in different industries, including food processing, biofuel production, pulp and paper manufacturing, and biomedical research. In medicine, glycoside hydrolases are used to diagnose and monitor certain medical conditions, such as carbohydrate-deficient glycoprotein syndrome, a rare inherited disorder affecting the structure of glycoproteins.

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.

Beta-Mannosidase is an enzyme that breaks down complex carbohydrates known as glycoproteins. It does this by catalyzing the hydrolysis of beta-mannosidic linkages, which are specific types of chemical bonds that connect mannose sugars within glycoproteins.

This enzyme plays an important role in the normal functioning of the body, particularly in the breakdown and recycling of glycoproteins. A deficiency in beta-mannosidase activity can lead to a rare genetic disorder known as beta-Mannosidosis, which is characterized by the accumulation of mannose-rich oligosaccharides in various tissues and organs, leading to progressive neurological deterioration and other symptoms.

Polynucleotide 5'-Hydroxyl-Kinase (PNK) is an enzyme that catalyzes the addition of a phosphate group to the 5'-hydroxyl end of a polynucleotide strand, such as DNA or RNA. This enzyme plays a crucial role in the repair and maintenance of DNA ends during various cellular processes, including DNA replication, recombination, and repair.

PNK has two distinct activities: 5'-kinase activity and 3'-phosphatase activity. The 5'-kinase activity adds a phosphate group to the 5'-hydroxyl end of a polynucleotide strand, while the 3'-phosphatase activity removes a phosphate group from the 3'-end of a strand. These activities enable PNK to process and repair DNA ends with missing or damaged phosphate groups, ensuring their proper alignment and ligation during DNA repair and recombination.

PNK is involved in several essential cellular pathways, including base excision repair (BER), nucleotide excision repair (NER), and double-strand break (DSB) repair. Dysregulation or mutations in PNK can lead to genomic instability and contribute to the development of various diseases, such as cancer and neurodegenerative disorders.

Glucans are polysaccharides (complex carbohydrates) that are made up of long chains of glucose molecules. They can be found in the cell walls of certain plants, fungi, and bacteria. In medicine, beta-glucans derived from yeast or mushrooms have been studied for their potential immune-enhancing effects. However, more research is needed to fully understand their role and effectiveness in human health.

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.

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.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Fermentation is a metabolic process in which an organism converts carbohydrates into alcohol or organic acids using enzymes. In the absence of oxygen, certain bacteria, yeasts, and fungi convert sugars into carbon dioxide, hydrogen, and various end products, such as alcohol, lactic acid, or acetic acid. This process is commonly used in food production, such as in making bread, wine, and beer, as well as in industrial applications for the production of biofuels and chemicals.

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.

Cellulases are a group of enzymes that break down cellulose, which is a complex carbohydrate and the main structural component of plant cell walls. These enzymes are produced by various organisms, including bacteria, fungi, and protozoa. They play an important role in the natural decomposition process and have various industrial applications, such as in the production of biofuels, paper, and textiles.

Cellulases work by hydrolyzing the beta-1,4 glycosidic bonds between the glucose molecules that make up cellulose, breaking it down into simpler sugars like glucose. This process is known as saccharification. The specific type of cellulase enzyme determines where on the cellulose molecule it will cleave the bond.

There are three main types of cellulases: endoglucanases, exoglucanases, and beta-glucosidases. Endoglucanases randomly attack internal bonds in the amorphous regions of cellulose, creating new chain ends for exoglucanases to act on. Exoglucanases (also known as cellobiohydrolases) cleave cellobiose units from the ends of the cellulose chains, releasing cellobiose or glucose. Beta-glucosidases convert cellobiose into two molecules of glucose, which can then be further metabolized by the organism.

In summary, cellulases are a group of enzymes that break down cellulose into simpler sugars through hydrolysis. They have various industrial applications and play an essential role in natural decomposition processes.

Pseudomembranous enterocolitis is a medical condition characterized by inflammation of the inner lining of the small intestine (enteritis) and large intestine (colitis), resulting in the formation of pseudomembranes – raised, yellowish-white plaques composed of fibrin, mucus, and inflammatory cells. The condition is most commonly caused by a toxin produced by the bacterium Clostridioides difficile (C. difficile), which can overgrow in the gut following disruption of the normal gut microbiota, often after antibiotic use. Symptoms may include diarrhea, abdominal cramps, fever, nausea, and dehydration. Severe cases can lead to complications such as sepsis, toxic megacolon, or even death if left untreated. Treatment typically involves discontinuing the offending antibiotic, administering oral metronidazole or vancomycin to eliminate C. difficile, and managing symptoms with supportive care. In some cases, fecal microbiota transplantation (FMT) may be considered as a treatment option.

Glucan 1,3-beta-Glucosidase is an enzyme that breaks down 1,3-beta-D-glucans, which are polysaccharides made up of chains of beta-D-glucose molecules linked together by 1,3-beta-glycosidic bonds. This enzyme catalyzes the hydrolysis of these glycosidic bonds, releasing individual glucose molecules or smaller oligosaccharides.

Glucan 1,3-beta-Glucosidase is found in various organisms, including bacteria, fungi, and higher plants. It has potential applications in biotechnology, such as in the production of biofuels and the degradation of plant material for use in animal feed. Additionally, it has been studied for its potential role in the treatment of certain medical conditions, such as fungal infections, where it can help to break down the cell walls of pathogenic fungi.

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.

Ethanol is the medical term for pure alcohol, which is a colorless, clear, volatile, flammable liquid with a characteristic odor and burning taste. It is the type of alcohol that is found in alcoholic beverages and is produced by the fermentation of sugars by yeasts.

In the medical field, ethanol is used as an antiseptic and disinfectant, and it is also used as a solvent for various medicinal preparations. It has central nervous system depressant properties and is sometimes used as a sedative or to induce sleep. However, excessive consumption of ethanol can lead to alcohol intoxication, which can cause a range of negative health effects, including impaired judgment, coordination, and memory, as well as an increased risk of accidents, injuries, and chronic diseases such as liver disease and addiction.

Acetylesterase is an enzyme that catalyzes the hydrolysis of acetyl esters into alcohol and acetic acid. This enzyme plays a role in the metabolism of various xenobiotics, including drugs and environmental toxins, by removing acetyl groups from these compounds. Acetylesterase is found in many tissues, including the liver, intestine, and blood. It belongs to the class of enzymes known as hydrolases, which act on ester bonds.

'Clostridium acetobutylicum' is a gram-positive, spore-forming, rod-shaped bacterium that is commonly found in soil and aquatic environments. It is a species of the genus Clostridium, which includes many bacteria capable of producing industrial chemicals through fermentation.

'Clostridium acetobutylicum' is particularly known for its ability to produce acetic acid and butyric acid, as well as solvents such as acetone and butanol, during the process of anaerobic respiration. This makes it a potential candidate for biotechnological applications in the production of biofuels and other industrial chemicals.

However, like many Clostridium species, 'Clostridium acetobutylicum' can also produce toxins and cause infections in humans and animals under certain circumstances. Therefore, it is important to handle this organism with care and follow appropriate safety protocols when working with it in a laboratory setting.

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.

Bacterial DNA refers to the genetic material found in bacteria. It is composed of a double-stranded helix containing four nucleotide bases - adenine (A), thymine (T), guanine (G), and cytosine (C) - that are linked together by phosphodiester bonds. The sequence of these bases in the DNA molecule carries the genetic information necessary for the growth, development, and reproduction of bacteria.

Bacterial DNA is circular in most bacterial species, although some have linear chromosomes. In addition to the main chromosome, many bacteria also contain small circular pieces of DNA called plasmids that can carry additional genes and provide resistance to antibiotics or other environmental stressors.

Unlike eukaryotic cells, which have their DNA enclosed within a nucleus, bacterial DNA is present in the cytoplasm of the cell, where it is in direct contact with the cell's metabolic machinery. This allows for rapid gene expression and regulation in response to changing environmental conditions.

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.

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.

Organelles are specialized structures within cells that perform specific functions essential for the cell's survival and proper functioning. They can be thought of as the "organs" of the cell, and they are typically membrane-bound to separate them from the rest of the cellular cytoplasm. Examples of organelles include the nucleus (which contains the genetic material), mitochondria (which generate energy for the cell), ribosomes (which synthesize proteins), endoplasmic reticulum (which is involved in protein and lipid synthesis), Golgi apparatus (which modifies, sorts, and packages proteins and lipids for transport), lysosomes (which break down waste materials and cellular debris), peroxisomes (which detoxify harmful substances and produce certain organic compounds), and vacuoles (which store nutrients and waste products). The specific organelles present in a cell can vary depending on the type of cell and its function.

'Clostridium tetani' is a gram-positive, spore-forming, anaerobic bacterium that is the causative agent of tetanus. The bacteria are commonly found in soil, dust, and manure, and can contaminate wounds, leading to the production of a potent neurotoxin called tetanospasmin. This toxin causes muscle spasms and stiffness, particularly in the jaw and neck muscles, as well as autonomic nervous system dysfunction, which can be life-threatening. Tetanus is preventable through vaccination with the tetanus toxoid vaccine.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

'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.

Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.

The most common disaccharides include:

* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.

Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.

Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.

'Clostridium cellulolyticum' is a species of gram-positive, rod-shaped, anaerobic bacteria found in soil and aquatic environments. It is known for its ability to break down complex carbohydrates such as cellulose and hemicellulose into simple sugars through the process of fermentation. This makes it a potential candidate for biofuel production from plant biomass.

The bacterium produces a range of enzymes that can degrade these polysaccharides, including cellulases and xylanases. These enzymes work together in a complex system to break down the cellulose and hemicellulose into monosaccharides, which can then be fermented by the bacterium to produce various end products such as acetate, ethanol, hydrogen, and carbon dioxide.

'Clostridium cellulolyticum' is also known to produce a number of other enzymes and metabolites that have potential applications in industry, including amylases, proteases, and lipases. However, further research is needed to fully understand the biology and potential uses of this organism.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

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.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

Chromosomal proteins, non-histone, are a diverse group of proteins that are associated with chromatin, the complex of DNA and histone proteins, but do not have the characteristic structure of histones. These proteins play important roles in various nuclear processes such as DNA replication, transcription, repair, recombination, and chromosome condensation and segregation during cell division. They can be broadly classified into several categories based on their functions, including architectural proteins, enzymes, transcription factors, and structural proteins. Examples of non-histone chromosomal proteins include high mobility group (HMG) proteins, poly(ADP-ribose) polymerases (PARPs), and condensins.

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.

Botulinum toxins are neurotoxic proteins produced by the bacterium Clostridium botulinum and related species. They are the most potent naturally occurring toxins, and are responsible for the paralytic illness known as botulism. There are seven distinct botulinum toxin serotypes (A-G), each of which targets specific proteins in the nervous system, leading to inhibition of neurotransmitter release and subsequent muscle paralysis.

In clinical settings, botulinum toxins have been used for therapeutic purposes due to their ability to cause temporary muscle relaxation. Botulinum toxin type A (Botox) is the most commonly used serotype in medical treatments, including management of dystonias, spasticity, migraines, and certain neurological disorders. Additionally, botulinum toxins are widely employed in aesthetic medicine for reducing wrinkles and fine lines by temporarily paralyzing facial muscles.

It is important to note that while botulinum toxins have therapeutic benefits when used appropriately, they can also pose significant health risks if misused or improperly handled. Proper medical training and supervision are essential for safe and effective utilization of these powerful toxins.

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.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

'Clostridium sordellii' is a gram-positive, spore-forming, anaerobic rod-shaped bacterium. It is part of the normal microbiota found in the human and animal gastrointestinal tract. However, it can cause severe and potentially fatal infections in humans, such as sepsis, myonecrosis (gas gangrene), and soft tissue infections. These infections are more commonly associated with contaminated wounds, surgical sites, or drug use (particularly black tar heroin). The bacterium produces powerful toxins that contribute to its virulence and can lead to rapid progression of the infection. Immediate medical attention is required for proper diagnosis and treatment, which typically involves antibiotics, surgical debridement, and supportive care.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

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.

Bacterial toxins are poisonous substances produced and released by bacteria. They can cause damage to the host organism's cells and tissues, leading to illness or disease. Bacterial toxins can be classified into two main types: exotoxins and endotoxins.

Exotoxins are proteins secreted by bacterial cells that can cause harm to the host. They often target specific cellular components or pathways, leading to tissue damage and inflammation. Some examples of exotoxins include botulinum toxin produced by Clostridium botulinum, which causes botulism; diphtheria toxin produced by Corynebacterium diphtheriae, which causes diphtheria; and tetanus toxin produced by Clostridium tetani, which causes tetanus.

Endotoxins, on the other hand, are components of the bacterial cell wall that are released when the bacteria die or divide. They consist of lipopolysaccharides (LPS) and can cause a generalized inflammatory response in the host. Endotoxins can be found in gram-negative bacteria such as Escherichia coli and Pseudomonas aeruginosa.

Bacterial toxins can cause a wide range of symptoms depending on the type of toxin, the dose, and the site of infection. They can lead to serious illnesses or even death if left untreated. Vaccines and antibiotics are often used to prevent or treat bacterial infections and reduce the risk of severe complications from bacterial toxins.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

Clostridium cellulovorans Clostridium clariflavum Clostridium josui Clostridium papyrosolvens Clostridium thermocellum (treated ... The scaffoldin of some cellulosomes, an example being that of Clostridium thermocellum, contains a carbohydrate-binding module ... Dockerin Organelle Bayer, EA; Kenig, R; Lamed, R (1983). "Adherence of Clostridium thermocellum to cellulose". J. Bacteriol. ... has been derived from the study of Clostridium thermocellum. In the early 1980s, Raphael Lamed and Ed Bayer met at Tel Aviv ...
Alexander JK (June 1968). "Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum". The Journal ...
"Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA". Journal of ...
"Chemoenzymatic Synthesis of β-D Glucosides using Cellobiose Phosphorylase from Clostridium thermocellum". Advanced Synthesis & ...
His research on Clostridium botulinum and Clostridium thermocellum improved understanding of clostridial metabolism, growth ... Furthermore, he developed a minimal chemically defined medium for the growth of Clostridium thermocellum, identifying specific ... Additionally, he investigated the cellulase system of Clostridium thermocellum, demonstrating comparable solubilization rates ... "Chemically Defined Minimal Medium for Growth of the Anaerobic Cellulolytic Thermophile Clostridium thermocellum". Applied and ...
... a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum". The Journal of Biological Chemistry. 282 (49): ...
... orthophosphate glucosyltransferase from Clostridium thermocellum". J. Biol. Chem. 244 (2): 457-64. PMID 5773308. Portal: ...
156, 828-36 (1983). Bayer, E. A., Kenig, R. & Lamed, R. Adherence of Clostridium thermocellum to cellulose. J. Bacteriol. 156, ... cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. ... Biotechnology for biofuels production of a functional cell wall anchored minicellulosome by recombinant Clostridium ...
The scaffolding component of the cellulolytic bacterium Clostridium thermocellum is a non-hydrolytic protein which organises ... "A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly". ...
One example is the CBM11 of Clostridium thermocellum Cel26A-Cel5E, this domain has been shown to bind both β-1,4-glucan and β-1 ... In anaerobic bacteria that degrade plant cell walls, exemplified by Clostridium thermocellum, the dockerin domains of the ... "The Family 11 Carbohydrate-binding Module of Clostridium thermocellum Lic26A-Cel5E Accommodates -1,4- and -1,3-1,4-Mixed Linked ... "Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS". FEMS Microbiol ...
Clostridium thermocellum, 1daq​). Among all the structures reported to date, the majority of EF-hand motifs are paired either ...
The precise role of most bacterial serpins remains obscure, although Clostridium thermocellum serpin localises to the ...
One example is Clostridium thermocellum, which uses a complex cellulosome to break down cellulose and synthesize ethanol. ... However, C. thermocellum also produces other products during cellulose metabolism, including acetate and lactate, in addition ... Demain AL, Newcomb M, Wu JH (March 2005). "Cellulase, clostridia, and ethanol". Microbiology and Molecular Biology Reviews. 69 ... Instead of sugar fermentation with yeast, this process uses Clostridium ljungdahlii bacteria. This microorganism will ingest ...
Bi-functional acetaldehyde/alcohol dehydrogenase genes from Clostridium thermocellum allow for the conversion of sugars to ...
The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. Barr BK, ...
Cellulose-Degrading Coculture with Clostridium thermocellum". Applied and Environmental Microbiology. 81 (16): 5567-5573. doi: ...
JGI: Archived 2007-12-21 at the Wayback Machine Clostridium thermocellum ATCC 27405 Cellulase, Clostridia, and Ethanol Ibid. ... Characterization of Clostridium thermocellum JW20 U.S. Department of Energy: Archived 2007-04-27 at the Wayback Machine ... Cellulosic Ethanol Type strain of Clostridium thermocellum at BacDive - the Bacterial Diversity Metadatabase v t e (Webarchive ...
Zverlov VV, Schantz N, Schwarz WH (August 2005). "A major new component in the cellulosome of Clostridium thermocellum is a ... For example, Clostridium cellulolyticum produces 13 GH9 modular cellulases containing a different number and arrangement of ... "Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium ...
"Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between ... "Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced ... "Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced ...
... butyricum converts glycerol to 1,3-propanediol. Genes from Clostridium thermocellum have been inserted into ... Mixtures of Clostridium species, such as Clostridium beijerinckii, Clostridium butyricum, and species from other genera have ... Clostridium tetani causes tetanus. Clostridium difficile, now placed in Clostridioides. Clostridium histolyticum, now placed in ... Clostridium welchii and Clostridium tetani respond to sulfonamides. Clostridia are also susceptible to tetracyclines, ...
This unique metabolism differs form other model cellulose degraders like Clostridium thermocellum and Trichoderma reesei which ...
The C-terminal domain belongs to this family shows similarity to a cellulase from Clostridium thermocellum (CelS), which acts ...
Clostridium aldrichii, C. alkalicellulosi, C. clariflavum, C. straminisolvens and C. thermocellum, reassigned in 2019. Genus ... Clostridium baratii Clostridium beihaiense Clostridium beijerinckii Clostridium diolis Clostridium bornimense Clostridium ... Clostridium aceticum Clostridium acetireducens Clostridium acetobutylicum Clostridium acidisoli Clostridium aciditolerans ... Clostridium aestuarii Clostridium akagii Clostridium algidicarnis Clostridium algifaecis Clostridium algoriphilum Clostridium ...
... kluyveri Clostridium novyi Clostridium perfringens Clostridium phytofermentans Clostridium tetani Clostridium thermocellum ... Pathema-Clostridium Clostridium acetobutylicum Clostridium botulinum Clostridium butyricum Clostridium difficile Clostridium ... Clostridium botulinum, Burkholderia mallei, Burkholderia pseudomallei, Clostridium perfringens, and Entamoeba histolytica) ...
Clostridium tetanomorphum MeSH B03.300.390.400.200.770 - Clostridium thermocellum MeSH B03.300.390.400.200.800 - Clostridium ... Clostridium tetanomorphum MeSH B03.510.415.400.200.770 - Clostridium thermocellum MeSH B03.510.415.400.200.800 - Clostridium ... Clostridium botulinum type G MeSH B03.300.390.400.200.180 - Clostridium butyricum MeSH B03.300.390.400.200.200 - Clostridium ... Clostridium botulinum type G MeSH B03.510.415.400.200.180 - Clostridium butyricum MeSH B03.510.415.400.200.200 - Clostridium ...
nov.; Reclassification of Thermoanaerobium brockii, Clostridium thermosulfurogenes, and Clostridium thermohydrosulfuricum E100- ... 2018, Hungateiclostridium thermocellum (Viljoen et al. 1926) Zhang et al. 2018, Hungateiclostridium cellulolyticum (Patel et al ... "Species: Clostridium thermosulfurigenes". lpsn.dsmz.de. Archived from the original on 2021-02-26. Retrieved 2021-03-22. Nogi, ... Originally described as Clostridium glycyrrhizinilyticum (31 letters) and later reclassified in genus Mediterraneibacter. Its ...
Carbohydrate Binding Module 42B (CBM42) is a Carbohydrate Binding Protein originating from Clostridium thermocellum. The ... is a Carbohydrate Binding Protein originating from Clostridium thermocellum. The recombinant CBM42, purified from Escherichia ...
The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. ...
Clostridium straminisolvens, Clostridium clariflavum, Acetivibrio cellulolyticus, and Clostridium sp. strain Bc-iso-3. ... Clostridium straminisolvens, Clostridium clariflavum, Acetivibrio cellulolyticus, and Clostridium sp. strain Bc-iso-3. ... Clostridium straminisolvens, Clostridium clariflavum, Acetivibrio cellulolyticus, and Clostridium sp. strain Bc-iso-3. ... Clostridium straminisolvens, Clostridium clariflavum, Acetivibrio cellulolyticus, and Clostridium sp. strain Bc-iso-3. ...
... including spore-forming Clostridia species Clostridium cellulovorans (Yang et al., 2015), C. thermocellum (Knutson et al., 1999 ... Clostridium thermocellum; Knutson et al., 1999), the effective partitioning of ethanol into the scCO2 phase (Guvenc et al., ... Effect of pressurized solvents on ethanol production by the thermophilic bacterium Clostridium thermocellum. J. Supercrit. ... Yang, X., Xu, M., and Yang, S. T. (2015). Metabolic and process engineering of Clostridium cellulovorans for biofuel production ...
Clostridium cellulovorans Clostridium clariflavum Clostridium josui Clostridium papyrosolvens Clostridium thermocellum (treated ... The scaffoldin of some cellulosomes, an example being that of Clostridium thermocellum, contains a carbohydrate-binding module ... Dockerin Organelle Bayer, EA; Kenig, R; Lamed, R (1983). "Adherence of Clostridium thermocellum to cellulose". J. Bacteriol. ... has been derived from the study of Clostridium thermocellum. In the early 1980s, Raphael Lamed and Ed Bayer met at Tel Aviv ...
Among the microorganisms that degrade polymers are the anaerobic bacteria Clostridium thermocellum [75], the genus Bacillus spp ... Clostridium thermocellum augmentation and microbial community analysis. Renew. Energy 2020, 148, 214-222. [Google Scholar] [ ... Clostridium sp.) and representatives of the Archea (archaeons), which produce methane as a result of respiration ( ...
Alternatively, Clostridium thermocellum is a thermophilic anerobe capable of both deconstruction and conversion of ... This work seeks to inform the deployment of cellulosic ethanol production by furthering our understanding of C.thermocellum ...
The crystal structure of a Fn3-like protein from Clostridium thermocellum. 3mtr. Crystal structure of the Ig5-FN1 tandem of ... cohesin and fibronectin type-III double module construct from the Clostridium perfringens glycoside hydrolase GH84C. ...
Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of the triphosphate tunnel metalloenzyme ... from the bacterium Clostridium thermocellum. CthTTM is a metal-dependent tripolyphosphatase and nucleoside triphosphatase; it ... as strong tripolyphosphatase activities similar to the triphosphate tunnel metalloenzyme proteins from Clostridium thermocellum ...
dash; Clostridium thermocellum *‐ Clostridium tyrobutyricum *‐ Clostridium xylanolyticum *‐ Clostridium ...
Clostridium thermocellum. AhpC like peroxiredoxin. complete. Achraf Jemmat. 4843. DacAhpC Betaproteobacteria. Delftia ... Clostridium beijerinckii. AhpC like peroxiredoxin. complete. Nicolas Rouhier. 4855. CcrAhpC (CC_2918) Alphaproteobacteria. ... Clostridium perfringens. AhpC like peroxiredoxin. complete. Nicolas Rouhier. 4876. CpsAhpC (CPS_4717) Gammaproteobacteria. ...
Clostridium thermocellum ATCC 27405 Bacteria hitchhiker 0.0000409658 n/a -. NC_009253 Dred_0614 putative endoribonuclease L-PSP ...
Clostridium thermocellum); NP_404421 (Yersinia pestis); DCDA_THEMA (Thermotoga maritima); Viridiplantae. BAD16980 (Oryza sativa ...
Clostridium thermocellum ATCC 27405, complete genome. basic membrane lipoprotein. 3e-33. 142. ... Clostridium novyi NT, complete genome. lipoprotein. 1e-40. 167. NC_014614:1259236:1269724. 1269724. 1270773. 1050. Clostridium ... Clostridium botulinum BKT015925 chromosome, complete genome. lipoprotein. 2e-38. 160. NC_014150:2399997:2402734. 2402734. ... Clostridium botulinum E3 str. Alaska E43, complete genome. putative basic membrane lipoprotein. 1e-12. 74.7. ...
Clostridium (Ruminiclostridium) thermocellum is a Gram-positive, thermophilic, anaerobic bacterium that is capable of ... Analysis of the alternative sigma factor system, σI5/RsgI5, in Clostridium thermocellum ...
Clostridium thermocellum [TaxId:203119] [194257] (4 PDB entries). *Domain for 3ul4: *. Domain d3ul4b_: 3ul4 B: [194258]. Other ... Clostridium thermocellum [TaxId:1249482] [332378] (1 PDB entry). *Domain for 5k39: *. Domain d5k39b2: 5k39 B:103-159 [332379]. ... Clostridium thermocellum [TaxId:1515] [256259] (1 PDB entry). *Domains for 4fl4: *. Domain d4fl4a1: 4fl4 A:23-88 [240137]. ... Clostridium thermocellum [TaxId:492476] [311325] (1 PDB entry). *Domains for 3p0d: *. Domain d3p0da1: 3p0d A:23-88 [306185]. ...
Celobiose/metabolismo , Clostridium thermocellum/genética , Clostridium thermocellum/metabolismo , Transcriptoma/genética , ... Clostridium thermocellum is a thermophilic bacterium recognized for its natural ability to effectively deconstruct cellulosic ... Clostridium (Ruminiclostridium) thermocellum is recognized for its ability to ferment cellulosic biomass directly, but it ... Clostridium thermocellum/genética , Regulação Bacteriana da Expressão Gênica/genética , Riboswitch/genética , Biologia ...
... acetyltransferase enables thermophilic isobutyl acetate production directly from cellulose by Clostridium thermocellum ...
p,The cellulose binding domain (CBD) of cellulosome-integrating protein A from Clostridium thermocellum NBRC 103400 was ...
Wilson CM, Yang SH, Rodriguez M, Ma Q, Johnson CM, Dice L, Xu Y, Brown SD: Clostridium thermocellum transcriptomic profiles ... mechanism of tolerance for the Populus hydrolysate-tolerant mutant strain of Clostridium thermocellum . Plos One 2013, 8(10):16 ... Venkataramanan KP, Jones SW, McCormick KP, Kunjeti SG, Ralston MT, Meyers BC, Papoutsakis ET: The Clostridium small RNome that ... Wang Y, Li XZ, Mao YJ, Blaschek HP: Genome-wide dynamic transcriptional profiling in Clostridium beijerinckii NCIMB 8052 using ...
C. thermocellum can utilize lignocellulosic waste and generate ethanol, making it a possible candidate for use in the ... The Clostridium genus includes common free-living bacteria as well as important pathogens. Some of the main species and how you ... This Quantum Formula antidotes the various species in the Clostridium genus as well as botulism toxin A-G, beta toxin, epsilon ... The toxic part of Clostridium is not the bacteria itself, but the toxins these bacteria produce. Seven types of neurotoxins ...
4-glucans by the family 11 carbohydrate-binding module from Clostridium thermocellum. ...
Clostridium thermoalcaliphilum * Clostridium thermoautotrophicum * Clostridium thermobutyricum * Clostridium thermocellum * ... Parent taxon: Clostridium Prazmowski 1880 (Approved Lists 1980) Assigned by: Lagier JC, Bibi F, Ramasamy D, Azhar EI, Robert C ... Clostridium jeddahense is the correct name instead if this species is regarded as a separate species (i.e., if its ... Non contiguous-finished genome sequence and description of Clostridium jeddahense sp. nov. Stand Genomic Sci 2014; 9:1003-1019 ...
3-glucans by the cellulosome of Clostridium thermocellum revealed by structure and function studies of a family 81 glycoside ... and the cellulosomal GH81 from Clostridium themocellum ATCC 27405 (CtLam81A) [6], however, the C-terminal domain is a CBM56 in ...
Clostridium thermocellum cloud point clover cmelina CNG Conversion kit co co-generation co-location Co-op Extension co- ...
Clostridium tetani B3.353.625.500.725 Clostridium tetanomorphum B3.353.625.500.740 Clostridium thermocellum B3.353.625.500.770 ... Clostridium B3.353.625.500 Clostridium acetobutylicum B3.353.625.500.25 Clostridium beijerinckii B3.353.625.500.100 Clostridium ... Clostridium botulinum type A B3.353.625.500.160.50 Clostridium botulinum type B B3.353.625.500.160.100 Clostridium botulinum ... Clostridium botulinum type E B3.353.625.500.160.250 Clostridium botulinum type F B3.353.625.500.160.300 Clostridium botulinum ...
Clostridium tetani B3.353.625.500.725 Clostridium tetanomorphum B3.353.625.500.740 Clostridium thermocellum B3.353.625.500.770 ... Clostridium B3.353.625.500 Clostridium acetobutylicum B3.353.625.500.25 Clostridium beijerinckii B3.353.625.500.100 Clostridium ... Clostridium botulinum type A B3.353.625.500.160.50 Clostridium botulinum type B B3.353.625.500.160.100 Clostridium botulinum ... Clostridium botulinum type E B3.353.625.500.160.250 Clostridium botulinum type F B3.353.625.500.160.300 Clostridium botulinum ...
Clostridium kluyveri(4) * Clostridium novyi(3) * Clostridium perfringens(16) * Clostridium thermocellum(1) ...
Clostridium thermocellum Clostridium thermocellum Clostridium thermocellum Clostridium tyrobutyricum Clostridium tyrobutyricum ... Clostridium chauvoei Clostridium chauvoei Clostridium chauvoei Clostridium histolyticum Clostridium histolyticum Clostridium ... Clostridium kluyveri Clostridium kluyveri Clostridium kluyveri Clostridium sordellii Clostridium sordellii Clostridium ... Clostridium tertium Clostridium tertium Clostridium tertium Clostridium tetanomorphum Clostridium tetanomorphum Clostridium ...
Clostridium thermocellum Clostridium thermocellum Clostridium thermocellum Clostridium tyrobutyricum Clostridium tyrobutyricum ... Clostridium chauvoei Clostridium chauvoei Clostridium chauvoei Clostridium histolyticum Clostridium histolyticum Clostridium ... Clostridium kluyveri Clostridium kluyveri Clostridium kluyveri Clostridium sordellii Clostridium sordellii Clostridium ... Clostridium tertium Clostridium tertium Clostridium tertium Clostridium tetanomorphum Clostridium tetanomorphum Clostridium ...
  • This architecture is largely conserved in the GH81 from Bacillus halodurans C-125 ( Bh GH81) [ 5 ], and the cellulosomal GH81 from Clostridium themocellum ATCC 27405 ( Ct Lam81A) [ 6 ], however, the C-terminal domain is a CBM56 in Bh GH81 and a cellulosomal dockerin in Ct Lam81A. (cazypedia.org)
  • By using comparative bioinformatic analysis, we have also identified highly conserved σ I and σ A -dependent promoters upstream of the primary scaffoldin-encoding genes of other clostridia, namely, Clostridium straminisolvens, Clostridium clariflavum, Acetivibrio cellulolyticus, and Clostridium sp. (tau.ac.il)
  • Interestingly, a previously identified TSS of the primary scaffoldin CbpA gene of Clostridium cellulovorans matches the predicted σ I -dependent promoter identified in the present work rather than the previously proposed σ A promoter. (tau.ac.il)
  • C. thermocellum, C. cellulolyticum, and C. cellulovorans) have greatly complicated efforts to probe cellulosome structure and function. (wikipedia.org)
  • Honey sometimes contains spores of Clostridium botulinum. (hcmionline.com)
  • They simply sought a 'cellulose-binding factor' or 'CBF' on the cell surface of the anaerobic thermophilic bacterium, C. thermocellum, which they inferred would account for the observation that the bacterium attaches strongly to the insoluble cellulose substrate prior to its degradation. (wikipedia.org)
  • Alternatively, Clostridium thermocellum is a thermophilic anerobe capable of both deconstruction and conversion of lignocellulose without thermochemical pretreatment. (dartmouth.edu)
  • The scaffoldin of some cellulosomes, an example being that of Clostridium thermocellum, contains a carbohydrate-binding module that adheres cellulose to the cellulosomal complex. (wikipedia.org)
  • Much of our understanding of its catalytic components, architecture, and mechanisms of attachment to the bacterial cell and to cellulose, has been derived from the study of Clostridium thermocellum. (wikipedia.org)
  • This Quantum Formula antidotes the various species in the Clostridium genus as well as botulism toxin A-G, beta toxin, epsilon toxin, perfringens type C and D and other neurotoxins, lignocellulosic waste, ethanol, endoglucanase, etc. (hcmionline.com)
  • The Clostridium genus includes common free-living bacteria as well as important pathogens. (hcmionline.com)
  • The toxic part of Clostridium is not the bacteria itself, but the toxins these bacteria produce. (hcmionline.com)
  • In the present report, we provide experimental evidence demonstrating that the C. thermocellum cipA gene, which encodes the primary cellulosomal scaffoldin, is regulated by several alternative σ I factors and by the vegetative σ A factor. (tau.ac.il)
  • Clostridium jeddahense is the correct name instead if this species is regarded as a separate species (i.e., if its nomenclatural type is not assigned to another species whose name is validly published, legitimate and not rejected and has priority) within a separate genus Clostridium . (dsmz.de)
  • Recently, the regulation of genes encoding certain cellulosomal components by multiple RNA polymerase alternative σ I factors has been demonstrated in Clostridium (Ruminiclostridium) thermocellum. (tau.ac.il)
  • The natural habitat for Clostridium species are soil, water and the gastrointestinal tract of animals and humans. (hcmionline.com)
  • Carbohydrate Binding Module 42B (CBM42) is a Carbohydrate Binding Protein originating from Clostridium thermocellum. (stratech.co.uk)
  • This work seeks to inform the deployment of cellulosic ethanol production by furthering our understanding of C.thermocellum mediated deconstruction. (dartmouth.edu)
  • C. thermocellum can utilize lignocellulosic waste and generate ethanol, making it a possible candidate for use in the production of ethanol fuel. (hcmionline.com)
  • Especie tipo del género CLOSTRIDIUM, bacteria grampositiva de la familia Clostridiaceae. (bvsalud.org)
  • Gram stain of Clostridium septicum , from culture growth of soft tissue infection. (idimages.org)
  • Clostridium septicum , from culture growth of soft tissue infection. (idimages.org)