Thermotoga maritima
Gram-Negative Anaerobic Bacteria
Thermotoga neapolitana
Gram-Negative Anaerobic Straight, Curved, and Helical Rods
Crystallography, X-Ray
Enzyme Stability
Molecular Sequence Data
Amino Acid Sequence
Models, Molecular
Structural Homology, Protein
Temperature
Sequence Homology, Amino Acid
Cloning, Molecular
Sequence Alignment
Protein Structure, Tertiary
Crystallization
Escherichia coli
Glycogen Debranching Enzyme System
Protein Structure, Quaternary
Protein Structure, Secondary
Cellulases
Catalytic Domain
Acetylesterase
Substrate Specificity
Protein Conformation
Binding Sites
Xylan Endo-1,3-beta-Xylosidase
Endo-1,4-beta Xylanases
Aminohydrolases
Glycoside Hydrolases
Xylosidases
Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima. (1/460)
Thermotoga maritima (Tm) expresses a 7 kDa monomeric protein whose 18 N-terminal amino acids show 81% identity to N-terminal sequences of cold shock proteins (Csps) from Bacillus caldolyticus and Bacillus stearothermophilus. There were only trace amounts of the protein in Thermotoga cells grown at 80 degrees C. Therefore, to perform physicochemical experiments, the gene was cloned in Escherichia coli. A DNA probe was produced by PCR from genomic Tm DNA with degenerated primers developed from the known N-terminus of TmCsp and the known C-terminus of CspB from Bacillus subtilis. Southern blot analysis of genomic Tm DNA allowed to produce a partial gene library, which was used as a template for PCRs with gene- and vector-specific primers to identify the complete DNA sequence. As reported for other csp genes, the 5' untranslated region of the mRNA was anomalously long; it contained the putative Shine-Dalgarno sequence. The coding part of the gene contained 198 bp, i.e., 66 amino acids. The sequence showed 61% identity to CspB from B. caldolyticus and high similarity to all other known Csps. Computer-based homology modeling allowed the conclusion that TmCsp represents a beta-barrel similar to CspB from B. subtilis and CspA from E. coli. As indicated by spectroscopic analysis, analytical gel permeation chromatography, and mass spectrometry, overexpression of the recombinant protein yielded authentic TmCsp with a molecular weight of 7,474 Da. This was in agreement with the results of analytical ultracentrifugation confirming the monomeric state of the protein. The temperature-induced equilibrium transition at 87 degrees C exceeds the maximum growth temperature of Tm and represents the maximal Tm-value reported for Csps so far. (+info)Allosteric control of three B12-dependent (class II) ribonucleotide reductases. Implications for the evolution of ribonucleotide reduction. (2/460)
Three separate classes of ribonucleotide reductases are known, each with a distinct protein structure. One common feature of all enzymes is that a single protein generates each of the four deoxyribonucleotides. Class I and III enzymes contain an allosteric substrate specificity site capable of binding effectors (ATP or various deoxyribonucleoside triphosphates) that direct enzyme specificity. Some (but not all) enzymes contain a second allosteric site that binds only ATP or dATP. Binding of dATP to this site inhibits the activity of these enzymes. X-ray crystallography has localized the two sites within the structure of the Escherichia coli class I enzyme and identified effector-binding amino acids. Here, we have studied the regulation of three class II enzymes, one from the archaebacterium Thermoplasma acidophilum and two from eubacteria (Lactobacillus leichmannii and Thermotoga maritima). Each enzyme has an allosteric site that binds ATP or various deoxyribonucleoside triphosphates and that regulates its substrate specificity according to the same rules as for class I and III enzymes. dATP does not inhibit enzyme activity, suggesting the absence of a second active allosteric site. For the L. leichmannii and T. maritima enzymes, binding experiments also indicate the presence of only one allosteric site. Their primary sequences suggest that these enzymes lack the structural requirements for a second site. In contrast, the T. acidophilum enzyme binds dATP at two separate sites, and its sequence contains putative effector-binding amino acids for a second site. The presence of a second site without apparent physiological function leads to the hypothesis that a functional site was present early during the evolution of ribonucleotide reductases, but that its function was lost from the T. acidophilum enzyme. The other two B12 enzymes lost not only the function, but also the structural basis for the site. Also a large subgroup (Ib) of class I enzymes, but none of the investigated class III enzymes, has lost this site. This is further indirect evidence that class II and I enzymes may have arisen by divergent evolution from class III enzymes. (+info)Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima. (3/460)
Phosphate acetyltransferase (PTA) and acetate kinase (AK) of the hyperthermophilic eubacterium Thermotoga maritima have been purified 1,500- and 250-fold, respectively, to apparent homogeneity. PTA had an apparent molecular mass of 170 kDa and was composed of one subunit with a molecular mass of 34 kDa, suggesting a homotetramer (alpha4) structure. The N-terminal amino acid sequence showed significant identity to that of phosphate butyryltransferases from Clostridium acetobutylicum rather than to those of known phosphate acetyltransferases. The kinetic constants of the reversible enzyme reaction (acetyl-CoA + Pi -->/<-- acetyl phosphate + CoA) were determined at the pH optimum of pH 6.5. The apparent Km values for acetyl-CoA, Pi, acetyl phosphate, and coenzyme A (CoA) were 23, 110, 24, and 30 microM, respectively; the apparent Vmax values (at 55 degrees C) were 260 U/mg (acetyl phosphate formation) and 570 U/mg (acetyl-CoA formation). In addition to acetyl-CoA (100%), the enzyme accepted propionyl-CoA (60%) and butyryl-CoA (30%). The enzyme had a temperature optimum at 90 degrees C and was not inactivated by heat upon incubation at 80 degrees C for more than 2 h. AK had an apparent molecular mass of 90 kDa and consisted of one 44-kDa subunit, indicating a homodimer (alpha2) structure. The N-terminal amino acid sequence showed significant similarity to those of all known acetate kinases from eubacteria as well that of the archaeon Methanosarcina thermophila. The kinetic constants of the reversible enzyme reaction (acetyl phosphate + ADP -->/<-- acetate + ATP) were determined at the pH optimum of pH 7.0. The apparent Km values for acetyl phosphate, ADP, acetate, and ATP were 0.44, 3, 40, and 0.7 mM, respectively; the apparent Vmax values (at 50 degrees C) were 2,600 U/mg (acetate formation) and 1,800 U/mg (acetyl phosphate formation). AK phosphorylated propionate (54%) in addition to acetate (100%) and used GTP (100%), ITP (163%), UTP (56%), and CTP (21%) as phosphoryl donors in addition to ATP (100%). Divalent cations were required for activity, with Mn2+ and Mg2+ being most effective. The enzyme had a temperature optimum at 90 degrees C and was stabilized against heat inactivation by salts. In the presence of (NH4)2SO4 (1 M), which was most effective, the enzyme did not lose activity upon incubation at 100 degrees C for 3 h. The temperature optimum at 90 degrees C and the high thermostability of both PTA and AK are in accordance with their physiological function under hyperthermophilic conditions. (+info)Location of translational initiation factor IF3 on the small ribosomal subunit. (4/460)
The location of translational initiation factor IF3 bound to the 30S subunit of the Thermus thermophilus ribosome has been determined by cryoelectron microscopy. Both the 30S.IF3 complex and control 30S subunit structures were determined to 27-A resolution. The difference map calculated from the two reconstructions reveals three prominent lobes of positive density. The previously solved crystal structure of IF3 fits very well into two of these lobes, whereas the third lobe probably arises from conformational changes induced in the 30S subunit as a result of IF3 binding. Our placement of IF3 on the 30S subunit allows an understanding in structural terms of the biochemical functions of this initiation factor, namely its ability to dissociate 70S ribosomes into 30S and 50S subunits and the preferential selection of initiator tRNA by IF3 during initiation. (+info)Purification and characterization of Thermotoga maritima endonuclease IV, a thermostable apurinic/apyrimidinic endonuclease and 3'-repair diesterase. (5/460)
An endonuclease IV homolog was identified as the product of a conceptual open reading frame in the genome of the hyperthermophilic bacterium Thermotoga maritima. The T. maritima endonuclease IV gene encodes a 287-amino-acid protein with 32% sequence identity to Escherichia coli endonuclease IV. The gene was cloned, and the expressed protein was purified and shown to have enzymatic activities that are characteristic of the endonuclease IV family of DNA repair enzymes, including apurinic/apyrimidinic endonuclease activity and repair activities on 3'-phosphates, 3'-phosphoglycolates, and 3'-trans-4-hydroxy-2-pentenal-5-phosphates. The T. maritima enzyme exhibits enzyme activity at both low and high temperatures. Circular dichroism spectroscopy indicates that T. maritima endonuclease IV has secondary structure similar to that of E. coli endonuclease IV and that the T. maritima endonuclease IV structure is more stable than E. coli endonuclease IV by almost 20 degrees C, beginning to rapidly denature only at temperatures approaching 90 degrees C. The presence of this enzyme, which is part of the DNA base excision repair pathway, suggests that thermophiles use a mechanism similar to that used by mesophiles to deal with the large number of abasic sites that arise in their chromosomes due to the increased rates of DNA damage at elevated temperatures. (+info)A detailed view of a ribosomal active site: the structure of the L11-RNA complex. (6/460)
We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors. (+info)Thermostable uracil-DNA glycosylase from Thermotoga maritima a member of a novel class of DNA repair enzymes. (7/460)
Uracil-DNA glycosylase (UDG) is a ubiquitous enzyme found in eukaryotes and prokaryotes [1][2][3]. This enzyme removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP [4] [5], and it is the primary activity in the DNA base excision repair pathway. Although UDG activities have been shown to be present in several thermophiles [6][7][8], no sequences have been found that are complementary to the Escherichia coli ung gene, which encodes UDG [9]. Here, we describe a UDG from the thermophile Thermotoga maritima. The T. maritima UDG gene has a low level of homology to the E. coli G-T/U mismatch-specific DNA glycosylase gene (mug). The expressed protein is capable of removing uracil from DNA containing either a U-A or a U-G base pair and is heat-stable up to 75 degrees C. The enzyme is also active on single-stranded DNA containing uracil. Analogous genes appear to be present in several prokaryotic organisms, including thermophilic and mesophilic eubacteria as well as archaebacteria, the human-disease pathogens Treponema palladium and Rickettsia prowazekii, and the extremely radioresistant organism Deinococcus radiodurans. These findings suggest that the T. maritima UDG is a member of a new class of DNA repair enzymes. (+info)A new member of the endonuclease III family of DNA repair enzymes that removes methylated purines from DNA. (8/460)
DNA is constantly exposed to endogenous andexogenous alkylating agents that can modify its bases,resulting in mutagenesis in the absence of DNA repair [1,2]. Alkylation damage is removed by the action of DNA glycosylases, which initiate the base excision repair pathway and protect the sequence information of the genome [3-5]. We have identified a new class of methylpurine DNA glycosylase, designated MpgII, that is a member of the endonuclease III family of DNA repair enzymes. We expressed and purified MpgII from Thermotoga maritima and found that the enzyme releases both 7-methylguanine and 3-methyladenine from DNA. We cloned the MpgII genes from T. maritima and from Aquifex aeolicus and found that both genes could restore methylmethanesulfonate (MMS) resistance to Escherichia coli alkA tagA double mutants, which are deficient in the repair of alkylated bases. Analogous genes are found in other Bacteria and Archaea and appear to be the only genes coding for methylpurine DNA glycosylase activity in these organisms. MpgII is the fifth member of the endonuclease III family of DNA repair enzymes, suggesting that the endonuclease III protein scaffold has been modified during evolution to recognize and repair a variety of DNA damage. (+info)"Thermotoga maritima" is not a medical term, but rather a scientific name for a specific type of bacterium. It belongs to the domain Archaea and is commonly found in marine environments with high temperatures, such as hydrothermal vents. The bacterium is known for its ability to survive in extreme conditions and has been studied for its potential industrial applications, including the production of biofuels and enzymes.
In a medical context, "Thermotoga maritima" may be relevant in research related to the development of new drugs or therapies, particularly those that involve extremophile organisms or their enzymes. However, it is not a term used to describe a specific medical condition or treatment.
Gram-negative anaerobic bacteria are a type of bacteria that do not require oxygen to grow and are characterized by their cell wall structure, which does not retain crystal violet dye in the Gram staining procedure. This is because they lack a thick peptidoglycan layer in their cell walls, which is typically stained dark purple in Gram-positive bacteria. Instead, gram-negative bacteria have an outer membrane that contains lipopolysaccharides (LPS), which can be toxic to human cells and contribute to the pathogenicity of these organisms.
Examples of gram-negative anaerobic bacteria include Bacteroides fragilis, Prevotella species, and Porphyromonas species. These bacteria are commonly found in the human mouth, gastrointestinal tract, and genitourinary tract, and can cause a variety of infections, including abscesses, wound infections, and bacteremia.
It's important to note that while gram-negative anaerobic bacteria do not require oxygen to grow, some may still tolerate or even prefer oxygen-rich environments. Therefore, the term "anaerobe" can be somewhat misleading when used to describe these organisms.
"Thermotoga neapolitana" is not a medical term, but rather a designation for a specific type of bacteria. It belongs to the genus "Thermotoga," which includes extremophile bacteria that thrive in extremely hot environments, such as hydrothermal vents and hot springs. The species "neapolitana" refers to the fact that this bacterium was first isolated from a hot water vent near Naples, Italy.
These bacteria are known for their ability to break down complex organic compounds into simpler molecules, which they use as a source of energy. They are also capable of surviving in temperatures up to 90°C (194°F) and have been studied for their potential applications in biotechnology, such as the production of biofuels and enzymes that can function at high temperatures.
While "Thermotoga neapolitana" itself is not a medical term, like other bacteria, it has the potential to cause infection under certain circumstances, particularly in individuals with weakened immune systems or exposed to contaminated equipment or environments. However, such cases are relatively rare and not well-studied.
'Gram-negative anaerobic straight, curved, and helical rods' are categories of bacteria that do not stain gram-positive during the Gram staining procedure, lack a outer layer of peptidoglycan, and do not require oxygen to grow. They can be further classified into different genera and species based on their shape and other microbiological and biochemical characteristics. Some examples of gram-negative anaerobic rods include Bacteroides, Prevotella, Porphyromonas, Fusobacterium, and Campylobacter. These bacteria are often found in the human oral cavity, gastrointestinal tract, and female genital tract and can cause a variety of infections such as abscesses, bacteremia, pneumonia, and meningitis.
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.
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.
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.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.
Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.
Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.
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.
'Structural homology' in the context of proteins refers to the similarity in the three-dimensional structure of proteins that are not necessarily related by sequence. This similarity arises due to the fact that these proteins have a common evolutionary ancestor or because they share a similar function and have independently evolved to adopt a similar structure. The structural homology is often identified using bioinformatics tools, such as fold recognition algorithms, that compare the three-dimensional structures of proteins to identify similarities. This concept is important in understanding protein function and evolution, as well as in the design of new drugs and therapeutic strategies.
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.
Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.
Molecular 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.
In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.
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.
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.
Ethacridine is an antiseptic and disinfectant agent that was previously used in medical and veterinary settings. It is a synthetic compound with the chemical formula C~14~H~15~ClN~3~O. Ethacridine has been used as a topical treatment for wounds, burns, and skin infections due to its ability to kill bacteria, fungi, and viruses. However, its use has declined over the years due to concerns about its potential toxicity and side effects.
Ethacridine works by interfering with the metabolic processes of microorganisms, which ultimately leads to their death. It is particularly effective against gram-negative bacteria, such as Escherichia coli and Pseudomonas aeruginosa. However, it has limited activity against gram-positive bacteria, such as Staphylococcus aureus.
Despite its antimicrobial properties, ethacridine is not commonly used in clinical practice today due to its potential toxicity. It can cause skin irritation, allergic reactions, and damage to the eyes and mucous membranes. Additionally, there are concerns that ethacridine may be absorbed into the body and cause harm to internal organs, such as the liver and kidneys.
Overall, while ethacridine has been a useful antiseptic and disinfectant in the past, its use is now limited due to concerns about its safety and efficacy.
Aldose-ketose isomerases are a group of enzymes that catalyze the interconversion between aldoses and ketoses, which are different forms of sugars. These enzymes play an essential role in carbohydrate metabolism by facilitating the reversible conversion of aldoses to ketoses and vice versa.
Aldoses are sugars that contain a carbonyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom) at the end of the carbon chain, while ketoses have their carbonyl group located in the middle of the chain. The isomerization process catalyzed by aldose-ketose isomerases helps maintain the balance between these two forms of sugars and enables cells to utilize them more efficiently for energy production and other metabolic processes.
There are several types of aldose-ketose isomerases, including:
1. Triose phosphate isomerase (TPI): This enzyme catalyzes the interconversion between dihydroxyacetone phosphate (a ketose) and D-glyceraldehyde 3-phosphate (an aldose), which are both trioses (three-carbon sugars). TPI plays a crucial role in glycolysis, the metabolic pathway that breaks down glucose to produce energy.
2. Xylulose kinase: This enzyme is involved in the pentose phosphate pathway, which is a metabolic route that generates reducing equivalents (NADPH) and pentoses for nucleic acid synthesis. Xylulose kinase catalyzes the conversion of D-xylulose (a ketose) to D-xylulose 5-phosphate, an important intermediate in the pentose phosphate pathway.
3. Ribulose-5-phosphate 3-epimerase: This enzyme is also part of the pentose phosphate pathway and catalyzes the interconversion between D-ribulose 5-phosphate (an aldose) and D-xylulose 5-phosphate (a ketose).
4. Phosphoglucomutase: This enzyme catalyzes the reversible conversion of glucose 1-phosphate (an aldose) to glucose 6-phosphate (an aldose), which is an important intermediate in both glycolysis and gluconeogenesis.
5. Phosphomannomutase: This enzyme catalyzes the reversible conversion of mannose 1-phosphate (a ketose) to mannose 6-phosphate (an aldose), which is involved in the biosynthesis of complex carbohydrates.
These are just a few examples of enzymes that catalyze the interconversion between aldoses and ketoses, highlighting their importance in various metabolic pathways.
'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.
The Glycogen Debranching Enzyme System, also known as glycogen debranching enzyme or Amy-1, is a crucial enzyme complex in human biochemistry. It plays an essential role in the metabolism of glycogen, which is a large, branched polymer of glucose that serves as the primary form of energy storage in animals and fungi.
The Glycogen Debranching Enzyme System consists of two enzymatic activities: a transferase and an exo-glucosidase. The transferase activity transfers a segment of a branched glucose chain to another part of the same or another glycogen molecule, while the exo-glucosidase activity cleaves the remaining single glucose units from the outer branches of the glycogen molecule.
This enzyme system is responsible for removing the branched structures of glycogen, allowing the linear chains to be further degraded by other enzymes into glucose molecules that can be used for energy production or stored for later use. Defects in this enzyme complex can lead to several genetic disorders, such as Glycogen Storage Disease Type III (Cori's disease) and Type IV (Andersen's disease), which are characterized by the accumulation of abnormal glycogen molecules in various tissues.
Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.
Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.
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.
A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.
In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.
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.
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.
Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.
Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.
Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.
In the context of 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.
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.
Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.
Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.
The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.
Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.
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.
Aminohydrolases are a class of enzymes that catalyze the hydrolysis of amide bonds and the breakdown of urea, converting it into ammonia and carbon dioxide. They are also known as amidases or urease. These enzymes play an essential role in various biological processes, including nitrogen metabolism and the detoxification of xenobiotics.
Aminohydrolases can be further classified into several subclasses based on their specificity for different types of amide bonds. For example, peptidases are a type of aminohydrolase that specifically hydrolyze peptide bonds in proteins and peptides. Other examples include ureases, which hydrolyze urea, and acylamidases, which hydrolyze acylamides.
Aminohydrolases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They have important applications in biotechnology and medicine, such as in the production of pharmaceuticals, the treatment of wastewater, and the diagnosis of genetic disorders.
Indole-3-glycerol-phosphate synthase (IGPS) is an enzyme that catalyzes the conversion of tryptophan into indole-3-glycerol phosphate, which is a key intermediate in the biosynthesis of various physiologically important compounds such as auxins (a type of plant hormone). In humans, defects in the IGPS enzyme have been associated with the disorder phenylketonuria (PKU), which is characterized by an inability to metabolize the amino acid phenylalanine. However, it's worth noting that IGPS primarily functions in the context of plant and microbial metabolism.
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.
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.
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.
Dimerization is a process in which two molecules, usually proteins or similar structures, bind together to form a larger complex. This can occur through various mechanisms, such as the formation of disulfide bonds, hydrogen bonding, or other non-covalent interactions. Dimerization can play important roles in cell signaling, enzyme function, and the regulation of gene expression.
In the context of medical research and therapy, dimerization is often studied in relation to specific proteins that are involved in diseases such as cancer. For example, some drugs have been developed to target and inhibit the dimerization of certain proteins, with the goal of disrupting their function and slowing or stopping the progression of the disease.
Thermotoga maritima
Thermotoga naphthophila
Thermotoga
Dicarboxylic acid
Sulfur-reducing bacteria
Glycoside hydrolase family 29
List of sequenced bacterial genomes
Phosphoribosylanthranilate isomerase
Ferredoxin
FtsA
Tryptophan synthase (indole-salvaging)
Ribosome recycling factor
Cellulase
Inferring horizontal gene transfer
TM0436
H+, Na+-translocating pyrophosphatase family
SurE, survival protein E
3H domain
Shikimate dehydrogenase
Thermotoga elfii
Structural genomics
Butyrate kinase
Jonathan Eisen
Muramyl ligase
Archaea
Fluorescent glucose biosensor
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-D-lysine ligase
Hyperthermophile
Thermotoga neapolitana
Non-proteinogenic amino acids
Thermotoga maritima - Wikipedia
6N9A: Crystal Structure of Thermotoga maritima threonylcarbamoyladenosine biosynthesis complex TsaB2D2E2 bound to ATP and...
RCSB PDB - 1TTY: Solution structure of sigma A region 4 from Thermotoga maritima
SCOPe 2.08: Species: Thermotoga maritima [TaxId: 2336]
SCOPe 2.08: Species: Thermotoga maritima [TaxId: 2336]
6OZF: Crystal structure of Thermotoga maritima (Tm) Endonuclease V (D110N) in complex with a 12mer DNA containing an inosine...
Structural Insights into Thermotoga maritima FtsH Periplasmic Domain on Substrate Recognition[v1] | Preprints.org
Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image...
Thermotoga maritima - Encyclopedia of Life
Regulon of ManR in Thermotoga maritima MSB8
a-(1-2,3,4,6)-D-Mannosidase (Thermotoga maritima)
beta-Glucosidase 1A from Thermotoga maritima, NX73725 - INNEX Scientific
Charakterisierung thermophiler Cellulasen aus Sulfolobus solfataricus und Thermotoga maritima - EPub Bayreuth
Biochemical Analysis of Thermotoga maritima Ribonuclease III and its Ribosomal RNA Substrates
PDB 5GVH | Chain STRUCTURE OF FABK FROM THERMOTOGA MARITIMA | 5GVH A | 3D Structure | canSARS
Uranium in PDB 3l0o: Structure of Rna-Free Rho Transcription Termination Factor From Thermotoga Maritima
Genes search | AnalogYeast
Genes search | AnalogYeast
Structural basis of laminin binding to the LARGE glycans on dystroglycan | Nature Chemical Biology
Crystal structure of a novel manganese-containing cupin (TM1459) from Thermotoga maritima at 1.65 Ã… resolution - Nuffield...
Crystal structure of a glycerophosphodiester phosphodiesterase (GDPD) from Thermotoga maritima (TM1621) at 1.60 Ã… resolution -...
New genital herpes web site launches!
Addgene
Capsid Mathematical Art - Shapeways Art
1j5u.1 | SWISS-MODEL Template Library
STRUCTURE-FUNCTION RELATIONSHIPS IN ALLOSTERIC CARBAMOYLTRANSFERASES FROM MESOPHILES AND EXTREME THERMOPHILES | | Project |...
CATH Domain 4p6yD01
MurD enzymes: some recent developments
Bacterium6
- T. maritima is well known for its ability to produce hydrogen (clean energy) and it is the only fermentative bacterium that has been shown to produce Hydrogen more than the Thauer limit (>4 mol H2 /mol glucose). (wikipedia.org)
- Thermotoga maritima is a non-sporulating, rod shaped, gram-negative bacterium. (wikipedia.org)
- Metabolic engineering in this bacterium led to development of strains of T. maritima that surpassed the Thauer limit of hydrogen production. (wikipedia.org)
- Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. (uni-regensburg.de)
- EC 4.2.1.11) from the hyperthermophilic bacterium Thermotoga maritima was purified to homogeneity. (uni-regensburg.de)
- The biochemical behavior of RNase III of the hyperthermophilic bacterium Thermotoga maritima is analyzed using purified recombinant enzyme and the cognate pre-ribosomal RNAs as substrates. (temple.edu)
Hyperthermophilic2
- Thermotoga maritima is a hyperthermophilic, anaerobic organism that is a member of the order Thermotogales. (wikipedia.org)
- The hyperthermophilic abilities of T. maritima, along with its deep lineage, suggests that it is potentially a very ancient organism. (wikipedia.org)
Species1
- Thermotoga maritima is a species of Bacteria in the family Thermotogaceae . (eol.org)
FeFe1
- A Group C [FeFe]-hydrogenase from Thermotoga maritima (TmHydS) has showed modest hydrogen conversion activity and reduced sensitivity to the enzyme's inhibitor, CO, in comparison to Group A prototypical and bifurcating [FeFe]-hydrogenases. (wikipedia.org)
Escherichia1
- This same basic mechanism applied to CheA from Escherichia coli and from Thermotoga maritima. (umd.edu)
Protein3
- The greatest degree of conservation between homologues is found in TMSs 1 and 2 of the Thermotoga maritima protein. (tcdb.org)
- The crystal structure of the CorA homologue from Thermotoga maritima has been solved at 3.9 Ã… resolution for the full-length protein and at 1.85 Ã… resolution for the cytoplasmic domain ( Lunin et al . (tcdb.org)
- Following plenary lectures on data collection, evaluation and interpretation (James Hester, Loes Kroon-Batenburg), symmetry (Mois I. Aroyo) and the CIF paradigm (Brian McMahon, James Hester), the students split into two groups for tutorial sessions, one looking at a zinc coordination polymer, the other at conformational aspects of Thermotoga maritima arginine-binding protein (TmArgBP). (iucr.org)
Organism1
- As an anaerobic fermentative chemoorganotrophic organism, T. maritima catabolizes sugars and polymers and produces carbon dioxide (CO2) and hydrogen (H2) gas as by-products of fermentation. (wikipedia.org)
Crystal2
- Here, we report the crystal structures of the Thermotoga maritima FtsH periplasmic domain (PD) in an associative trimeric state at a 1.5-1.95 Ã… resolution. (preprints.org)
- Joint Center for Structural Genomics (JCSG), Crystal structure of archease, possible chaperone (TM1083) from Thermotoga maritima at 2.0 A resolution. (expasy.org)
Genome2
- The genome of T. maritima consists of a single circular 1.8 megabase chromosome encoding for 1877 proteins. (wikipedia.org)
- The T. maritima genome encodes a ~5,000 nucleotide (nt) transcript, expressed from the single ribosomal RNA (rRNA) operon. (temple.edu)
Bacteria1
- T. maritima is one of fermentative bacteria that produces hydrogen to levels that approach the thermodynamic limit (4 mol H2/ mol glucose). (wikipedia.org)
Structure1
- That AsiA induces, rather than merely stabilizes, this rearrangement can be realized by comparison to the homologous structures of region 4 solved in a variety of contexts, including the structure of Thermotoga maritima sigmaA region 4 described herein. (rcsb.org)
Eubacterium Thermotoga maritima2
- Omp alpha is an outer-membrane protein that spans the periplasmic space of the hyperthermophilic eubacterium Thermotoga maritima. (unboundmedicine.com)
- TY - JOUR T1 - Model structure of the Omp alpha rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima. (unboundmedicine.com)
Cellulase 12A2
- Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. (tmu.edu.tw)
- Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop. (sinica.edu.tw)
Protein1
- The NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima represents an alpha/beta-topology formed by the regular secondary structures alpha1-beta1-beta2-alpha2-beta3-beta4-alpha3- beta5-3(10)-alpha4, with a small anti-parallel beta-sheet of beta-strands 1 and 2, and a mixed parallel/anti-parallel beta-sheet of beta-strands 3-5. (rcsb.org)
TRNA1
- Thermotoga maritima TruB, an enzyme responsible for the formation of pseudouridine in tRNA, has been purified and crystallized by the hanging-drop vapour-diffusion method in 100 mM citrate pH 3.5, 200 mM Li(2)SO(4), 20% glycerol, 13% PEG 8000. (ac.be)
Archaea1
- This similarity suggests horizontal gene transfer between Archaea and ancestors of T. maritima and could help to explain why T. maritima is capable of surviving in such extreme temperatures and conditions. (wikipedia.org)
Bacillus1
- 19. Role of N-terminal extension of Bacillus stearothermophilus RNase H2 and C-terminal extension of Thermotoga maritima RNase H2. (nih.gov)
Source1
- T. maritima is also capable of metabolizing cellulose as well as xylan, yielding H2 that could potentially be utilized as an alternative energy source to fossil fuels. (wikipedia.org)
Domain1
- 16. The N-terminal hybrid binding domain of RNase HI from Thermotoga maritima is important for substrate binding and Mg2+-dependent activity. (nih.gov)
Activity1
- A Group C [FeFe]-hydrogenase from Thermotoga maritima (TmHydS) has showed modest hydrogen conversion activity and reduced sensitivity to the enzyme's inhibitor, CO, in comparison to Group A prototypical and bifurcating [FeFe]-hydrogenases. (wikipedia.org)