A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
A genus of zygomycetous fungi of the family Mucoraceae, order MUCORALES, a common saprophyte and facultative parasite of mature fruits and vegetables. It may cause cerebral mycoses in diabetes and cutaneous infection in severely burned patients.
A genus of zygomycetous fungi of the family Mucoraceae, order Mucorales. It is primarily saprophytic, but may cause MUCORMYCOSIS in man from spores germinating in the lungs.
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.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.
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.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
The predominant milk-clotting enzyme from the true stomach or abomasum of the suckling calf. It is secreted as an inactive precursor called prorennin and converted in the acid environment of the stomach to the active enzyme. EC 3.4.23.4.
A large and heterogenous group of fungi whose common characteristic is the absence of a sexual state. Many of the pathogenic fungi in humans belong to this group.
Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.
Yeast-like ascomycetous fungi of the family Saccharomycopsidaceae, order SACCHAROMYCETALES, isolated from the stomach of rabbits and some other animals.
Nitrophenols are organic compounds characterized by the presence of a nitro group (-NO2) attached to a phenol molecule, known for their potential use in chemical and pharmaceutical industries, but also recognized as environmental pollutants due to their toxicity and potential carcinogenicity.
Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pepsinogen I or pepsinogen) and PEPSINOGEN C (formerly pepsinogen II or progastricsin). Pepsinogen B is the name of a pepsinogen from pigs.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.
Diazonium compounds are organic derivatives containing the general formula R-N2+X-, where R represents an aryl or alkyl group, and X- is an anion such as bromide or chloride, formed by the reaction of amines with nitrous acid in an acidic medium.
A mitosporic Loculoascomycetes fungal genus including some economically important plant parasites. Teleomorphs include Mycosphaerella and Venturia.
A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.
Azo compounds are organic compounds characterized by the presence of one or more azo groups, -N=N-, linking two aromatic rings, which can impart various colors and are used in dyes, pharmaceuticals, and chemical research.
An order of ascomycetous FUNGI which includes many economically important plant parasites as well as saprophytes.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The rate dynamics in chemical or physical systems.
The sum of the weight of all the atoms in a molecule.

Cloning of the SAP6 gene of Metschnikowia reukaufii and its heterologous expression and characterization in Escherichia coli. (1/51)

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Criteria for the differentiation between young and old Onchocerca volvulus filariae. (2/51)

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Recognition of fungal protease activities induces cellular activation and eosinophil-derived neurotoxin release in human eosinophils. (3/51)

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Identification of novel aspartic proteases from Strongyloides ratti and characterisation of their evolutionary relationships, stage-specific expression and molecular structure. (4/51)

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A novel bifunctional peptidic aspartic protease inhibitor inhibits chitinase A from Serratia marcescens: Kinetic analysis of inhibition and binding affinity. (5/51)

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Feline immunodeficiency virus (FIV) as a model for study of lentivirus infections: parallels with HIV. (6/51)

FIV is a significant pathogen in the cat and is, in addition, the smallest available natural model for the study of lentivirus infections. Although divergent at the amino acid level, the cat lentivirus has an abundance of structural and pathophysiological commonalities with HIV and thus serves well as a model for development of intervention strategies relevant to infection in both cats and man. The following review highlights both the strengths and shortcomings of the FIV/cat model, particular as regards development of antiviral drugs.  (+info)

Neutralizing antibodies to the hookworm hemoglobinase Na-APR-1: implications for a multivalent vaccine against hookworm infection and schistosomiasis. (7/51)

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Differences in exoenzyme production and adherence ability of Candida spp. isolates from catheter, blood and oral cavity. (8/51)

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Aspartic acid proteases are a type of enzyme that cleaves peptide bonds in proteins. They are called "aspartic" proteases because they contain two aspartic acid residues in their active site, which are essential for their catalytic function. These enzymes work by bringing the two carboxyl groups of the adjacent aspartic acids into close proximity, allowing them to act as a catalyst for the hydrolysis of peptide bonds.

Aspartic acid proteases play important roles in various biological processes, including protein degradation, cell signaling, and viral infection. Some examples of aspartic acid proteases include pepsin, cathepsin D, and HIV-1 protease. These enzymes are often targeted by drugs for the treatment of diseases such as cancer, arthritis, and AIDS.

Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.

Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.

In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.

Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.

Pepstatins are a group of naturally occurring cyclic peptides that inhibit aspartic proteases, a type of enzyme that breaks down proteins. They are isolated from various actinomycete species of Streptomyces and Actinosynnema. Pepstatins are often used in laboratory research to study the function of aspartic proteases and as tools to probe the mechanism of action of these enzymes. In addition, pepstatins have been explored for their potential therapeutic use in various diseases, including cancer, viral infections, and cardiovascular disease. However, they have not yet been approved for clinical use.

Aspartic acid endopeptidases are a type of enzyme that cleave peptide bonds within proteins. They are also known as aspartyl proteases or aspartic proteinases. These enzymes contain two catalytic aspartic acid residues in their active site, which work together to hydrolyze the peptide bond.

Aspartic acid endopeptidases play important roles in various biological processes, including protein degradation, processing, and activation. They are found in many organisms, including viruses, bacteria, fungi, plants, and animals. Some well-known examples of aspartic acid endopeptidases include pepsin, cathepsin D, and HIV protease.

Pepsin is a digestive enzyme found in the stomach that helps break down proteins in food. Cathepsin D is a lysosomal enzyme that plays a role in protein turnover and degradation within cells. HIV protease is an essential enzyme for the replication of the human immunodeficiency virus (HIV), which causes AIDS. Inhibitors of HIV protease are used as antiretroviral drugs to treat HIV infection.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Norleucine is not typically defined in a medical context, but it is a chemical compound used in research and biochemistry. It is an unnatural amino acid that is sometimes used as a substitute for the naturally occurring amino acid methionine in scientific studies. Norleucine has a different side chain than methionine, which can affect the properties of proteins when it is substituted for methionine.

In terms of its chemical structure, norleucine is a straight-chain aliphatic amino acid with a four-carbon backbone and a carboxyl group at one end and an amino group at the other end. It has a branched side chain consisting of a methyl group and an ethyl group.

While norleucine is not typically used as a therapeutic agent in medicine, it may have potential applications in the development of new drugs or in understanding the functions of proteins in the body.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Rhizopus is a genus of saprophytic fungi that belong to the family Mucoraceae. These fungi are commonly found in soil, decaying vegetation, and fruits. They are characterized by the presence of rhizoids, which are multicellular filaments that anchor the fungus to its substrate.

Rhizopus species are known to produce spores in large numbers, which can be dispersed through the air and cause infections in humans, particularly in individuals with weakened immune systems. One of the most common diseases caused by Rhizopus is mucormycosis, a serious and often life-threatening fungal infection that can affect various organs, including the sinuses, lungs, brain, and skin.

It's worth noting that while Rhizopus species are important pathogens in certain populations, they also have beneficial uses. For example, some species of Rhizopus are used in the production of tempeh, a traditional Indonesian food made from fermented soybeans.

"Mucor" is a genus of fungi that belongs to the order Mucorales. These fungi are commonly found in soil, decaying organic matter, and sometimes on fruits and vegetables. Some species of Mucor can cause mucormycosis, a rare but serious invasive fungal infection that primarily affects people with weakened immune systems, such as those with uncontrolled diabetes, cancer, organ transplant recipients, and those using high-dose corticosteroids.

Mucormycosis can affect various parts of the body, including the sinuses, lungs, skin, and gastrointestinal tract. The infection can quickly spread through the bloodstream and cause severe damage to tissues and organs. Early diagnosis and prompt treatment with antifungal medications and surgical debridement are crucial for managing mucormycosis and improving outcomes.

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.

Cathepsin D is a lysosomal aspartic protease that plays a role in intracellular protein degradation and turnover. It is produced as an inactive precursor and is activated by cleavage into two subunits within the acidic environment of the lysosome. Cathepsin D is also known to be secreted by certain cells, where it can contribute to extracellular matrix remodeling and tissue degradation. In addition, abnormal levels or activity of cathepsin D have been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

'Aspergillus oryzae' is a species of filamentous fungi belonging to the family Trichocomaceae. It is commonly known as koji mold and is widely used in the fermentation industry, particularly in Asian countries, for the production of various traditional foods and beverages such as soy sauce, miso, sake, and shochu. The fungus has the ability to produce a variety of enzymes, including amylases, proteases, and lipases, which make it useful in the breakdown and conversion of carbohydrates, proteins, and fats in food substrates.

In addition to its industrial applications, 'Aspergillus oryzae' has also been studied for its potential medicinal properties. Some research suggests that certain compounds produced by the fungus may have antimicrobial, antioxidant, and anti-inflammatory effects. However, more studies are needed to confirm these findings and determine the safety and efficacy of using 'Aspergillus oryzae' for medicinal purposes.

It is worth noting that while 'Aspergillus oryzae' is generally considered safe for food use, it can cause infections in people with weakened immune systems. Therefore, individuals who are at risk of invasive aspergillosis should avoid exposure to this and other species of Aspergillus.

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.

Pepsin A is defined as a digestive enzyme that is primarily secreted by the chief cells in the stomach's fundic glands. It plays a crucial role in protein catabolism, helping to break down food proteins into smaller peptides during the digestive process. Pepsin A has an optimal pH range of 1.5-2.5 for its enzymatic activity and is activated from its inactive precursor, pepsinogen, upon exposure to acidic conditions in the stomach.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Cathepsin E is a type of proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily located in the lysosomes of cells and plays a role in intracellular protein degradation. Cathepsin E is unique among the cathepsins because it is predominantly expressed in immune cells, such as macrophages and dendritic cells, where it functions as a protease involved in antigen presentation.

The enzyme has a molecular weight of approximately 42 kDa and is synthesized as an inactive precursor that undergoes proteolytic processing to generate the mature, active enzyme. Cathepsin E can cleave various substrates, including peptides and proteins, and has been implicated in several physiological and pathological processes, such as inflammation, immune response, and cancer.

In summary, Cathepsin E is a lysosomal cysteine protease that plays a crucial role in antigen presentation and protein degradation, primarily expressed in immune cells.

Chymosin, also known as rennin or rennet, is a proteolytic enzyme that is naturally present in the stomachs of ruminant animals such as cows, goats, and sheep. It plays an essential role in the digestion of milk in these animals by curdling or coagulating the milk protein casein, which helps in the separation of solid curds from liquid whey during the process of stomach digestion.

In the context of food production, chymosin is often used as a coagulant in the manufacturing of cheese and other dairy products. Traditionally, rennet was obtained by extracting it from the fourth stomach chamber (abomasum) of young calves, but nowadays, most commercial chymosin is produced through microbial fermentation using genetically modified bacteria or yeast that have been engineered to produce this enzyme. This method of production allows for a more consistent and animal-friendly source of chymosin for industrial applications.

The primary function of chymosin in cheese making is to catalyze the coagulation of casein, leading to the formation of a curd that can be further processed into various types of cheese. The enzyme specifically cleaves a bond in the casein protein called Phe105-Met106, resulting in the formation of para-κ-casein and paracaseinompholine, which then interact to form the curd. This reaction is crucial for initiating the cheese making process, as it allows for the separation of solid curds from liquid whey, which can then be pressed, aged, and transformed into a wide variety of cheese styles.

Mitosporic fungi, also known as asexual fungi or anamorphic fungi, are a group of fungi that produce mitospores (also called conidia) during their asexual reproduction. Mitospores are produced from the tip of specialized hyphae called conidiophores and are used for dispersal and survival of the fungi in various environments. These fungi do not have a sexual reproductive stage or it has not been observed, making their taxonomic classification challenging. They are commonly found in soil, decaying organic matter, and water, and some of them can cause diseases in humans, animals, and plants. Examples of mitosporic fungi include Aspergillus, Penicillium, and Fusarium species.

HIV Protease is a crucial enzyme that plays a significant role in the replication cycle of the Human Immunodeficiency Virus (HIV). It is responsible for cleaving or cutting specific long protein chains, produced during the translation of viral RNA, into smaller functional proteins. These proteins are essential for the formation of new virus particles.

The HIV Protease enzyme functions like a pair of molecular scissors, recognizing and cutting particular amino acid sequences in these polyprotein chains. By inhibiting this enzyme's activity with antiretroviral drugs known as protease inhibitors, the production of mature, infectious viral particles can be effectively prevented, which is a crucial component of highly active antiretroviral therapy (HAART) for managing HIV infection and reducing the risk of transmitting the virus to others.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

'Aspergillus niger' is a species of fungi that belongs to the genus Aspergillus. It is a ubiquitous microorganism that can be found in various environments, including soil, decaying vegetation, and indoor air. 'Aspergillus niger' is a black-colored mold that produces spores that are easily dispersed in the air.

This fungus is well known for its ability to produce a variety of enzymes and metabolites, some of which have industrial applications. For example, it is used in the production of citric acid, which is widely used as a food additive and preservative.

However, 'Aspergillus niger' can also cause health problems in humans, particularly in individuals with weakened immune systems or underlying lung conditions. It can cause allergic reactions, respiratory symptoms, and invasive aspergillosis, a serious infection that can spread to other organs in the body.

In addition, 'Aspergillus niger' can produce mycotoxins, which are toxic compounds that can contaminate food and feed and cause various health effects in humans and animals. Therefore, it is important to prevent the growth and proliferation of this fungus in indoor environments and food production facilities.

"Saccharomycopsis" is a genus of fungi in the family Saccharomycopsidaceae. These are typically aerobic, non-pathogenic yeasts that are commonly found in various environments such as soil, fruits, and insects. They have the ability to ferment sugars and produce alcohol, carbon dioxide, and other metabolic byproducts. Some species of Saccharomycopsis are used in industrial applications, including the production of fermented foods and beverages, while others are studied for their potential use in biotechnology and biofuel production. It's worth noting that Saccharomycopsis species are not typically associated with human diseases or infections.

Nitrophenols are organic compounds that contain a hydroxyl group (-OH) attached to a phenyl ring (aromatic hydrocarbon) and one or more nitro groups (-NO2). They have the general structure R-C6H4-NO2, where R represents the hydroxyl group.

Nitrophenols are known for their distinctive yellow to brown color and can be found in various natural sources such as plants and microorganisms. Some common nitrophenols include:

* p-Nitrophenol (4-nitrophenol)
* o-Nitrophenol (2-nitrophenol)
* m-Nitrophenol (3-nitrophenol)

These compounds are used in various industrial applications, including dyes, pharmaceuticals, and agrochemicals. However, they can also be harmful to human health and the environment, as some nitrophenols have been identified as potential environmental pollutants and may pose risks to human health upon exposure.

Pepsinogens are inactive precursor forms of the enzyme pepsin, which is produced in the stomach. They are composed of two types: Pepsinogen I (or gastric intrinsic factor) and Pepsinogen II. When exposed to acid in the stomach, these pepsinogens get converted into their active form, pepsin, which helps digest proteins in food. Measurement of pepsinogens in blood can be used as a diagnostic marker for certain stomach conditions, such as atrophic gastritis and gastric cancer.

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

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.

Epoxy compounds, also known as epoxy resins, are a type of thermosetting polymer characterized by the presence of epoxide groups in their molecular structure. An epoxide group is a chemical functional group consisting of an oxygen atom double-bonded to a carbon atom, which is itself bonded to another carbon atom.

Epoxy compounds are typically produced by reacting a mixture of epichlorohydrin and bisphenol-A or other similar chemicals under specific conditions. The resulting product is a two-part system consisting of a resin and a hardener, which must be mixed together before use.

Once the two parts are combined, a chemical reaction takes place that causes the mixture to cure or harden into a solid material. This curing process can be accelerated by heat, and once fully cured, epoxy compounds form a strong, durable, and chemically resistant material that is widely used in various industrial and commercial applications.

In the medical field, epoxy compounds are sometimes used as dental restorative materials or as adhesives for bonding medical devices or prosthetics. However, it's important to note that some people may have allergic reactions to certain components of epoxy compounds, so their use must be carefully evaluated and monitored in a medical context.

Diazonium compounds are a class of organic compounds that contain the functional group -N=N+E-, where E- represents a halide ion or an organic cation. They are typically prepared by treating an aromatic primary amine with nitrous acid (HNO2) in an acidic medium, which results in the formation of a diazonium ion.

The general reaction can be represented as follows:

R-NH2 + HNO2 + HX → R-N=N+X- + 2H2O

where R represents the aromatic ring and X- is a halide ion (Cl-, Br-, or I-).

Diazonium compounds are important intermediates in organic synthesis, particularly in the preparation of azo dyes and other colored compounds. They are also useful for introducing functional groups into aromatic rings through various chemical reactions such as sandmeyer reaction, gattermann reaction etc. However, diazonium salts are generally unstable and can decompose explosively if heated or subjected to strong shock or friction. Therefore, they must be handled with care.

'Cladosporium' is a genus of fungi that are widely distributed in the environment, particularly in soil, decaying plant material, and indoor air. These fungi are known for their dark-pigmented spores, which can be found in various shapes and sizes depending on the species. They are important causes of allergies and respiratory symptoms in humans, as well as plant diseases. Some species of Cladosporium can also produce toxins that may cause health problems in susceptible individuals. It is important to note that medical definitions typically refer to specific diseases or conditions that affect human health, so 'Cladosporium' itself would not be considered a medical definition.

"Aspergillus" is a genus of filamentous fungi (molds) that are widely distributed in the environment. These molds are commonly found in decaying organic matter such as leaf litter, compost piles, and rotting vegetation. They can also be found in indoor environments like air conditioning systems, dust, and building materials.

The medical relevance of Aspergillus comes from the fact that some species can cause a range of diseases in humans, particularly in individuals with weakened immune systems or underlying lung conditions. The most common disease caused by Aspergillus is called aspergillosis, which can manifest as allergic reactions, lung infections (like pneumonia), and invasive infections that can spread to other parts of the body.

Aspergillus species produce small, airborne spores called conidia, which can be inhaled into the lungs and cause infection. The severity of aspergillosis depends on various factors, including the individual's immune status, the specific Aspergillus species involved, and the extent of fungal invasion in the body.

Common Aspergillus species that can cause human disease include A. fumigatus, A. flavus, A. niger, and A. terreus. Preventing exposure to Aspergillus spores and maintaining a healthy immune system are crucial steps in minimizing the risk of aspergillosis.

Azo compounds are organic compounds characterized by the presence of one or more azo groups (-N=N-) in their molecular structure. The term "azo" is derived from the Greek word "azō," meaning "to boil" or "to sparkle," which refers to the brightly colored nature of many azo compounds.

These compounds are synthesized by the reaction between aromatic amines and nitrous acid or its derivatives, resulting in the formation of diazonium salts, which then react with another aromatic compound containing an active methylene group to form azo compounds.

Azo compounds have diverse applications across various industries, including dyes, pigments, pharmaceuticals, and agrochemicals. They are known for their vibrant colors, making them widely used as colorants in textiles, leather, paper, and food products. In addition, some azo compounds exhibit unique chemical properties, such as solubility, stability, and reactivity, which make them valuable intermediates in the synthesis of various organic compounds.

However, certain azo compounds have been found to pose health risks due to their potential carcinogenicity and mutagenicity. As a result, regulations have been imposed on their use in consumer products, particularly those intended for oral consumption or direct skin contact.

Xylariales is an order of fungi in the class Sordariomycetes, which are primarily wood-inhabiting species. This group includes both saprobic and pathogenic fungi, with some members known to cause various plant diseases. The order contains several families, including Xylariaceae, Amphisphaeriaceae, and Graphostromataceae, among others. Many species in Xylariales produce dark-colored, melanized structures called pycnidia or stromata, which contain the reproductive structures of the fungi. Some members of this order also have potential industrial applications, such as the production of enzymes and bioactive compounds.

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.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

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

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

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

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

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

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

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

LaPointe CF, Taylor RK (January 2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". The ... Aspartic proteases (also "aspartyl proteases", "aspartic endopeptidases") are a catalytic type of protease enzymes that use an ... Pepstatin is an inhibitor of aspartate proteases. Five superfamilies (clans) of aspartic proteases are known, each representing ... Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral ...
BACE is a transmembrane protein with an extracellular aspartic acid protease domain. γ-secretase is actually a protein complex ... Presenilin is believed to harbor the protease domain and represents an important example of an uncommon type of protease that ...
Caspases (cysteine-aspartic acid proteases) cleave at very specific amino acid residues. There are two types of caspases: ... Plaques are made up of small peptides, typically 39-43 amino acids in length, called amyloid beta (also written as A-beta or Aβ ... CAG codes for the amino acid glutamine. A repeat of CAG results in a polyglutamine (polyQ) tract. Diseases associated with such ... A current therapeutic target for the treatment of Alzheimer's disease is the protease β-secretase[non-primary source needed], ...
LaPointe CF, Taylor RK (January 2000). "The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases". The ...
... s are aspartic acid proteases, meaning their active site contains two aspartic acid residues. These two aspartic acid ... The name plasmepsin may come from Plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular ... Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C (1994). "Sequence, expression and modeled structure of an aspartic ... Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN (1999). "Crystal structure of the novel aspartic proteinase zymogen ...
The CASP14 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases ... Hu S, Snipas SJ, Vincenz C, Salvesen G, Dixit VM (Dec 1998). "Caspase-14 is a novel developmentally regulated protease". J Biol ... Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two ...
The CASP3 protein is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays ... This specificity allows caspases to be incredibly selective, with a 20,000-fold preference for aspartic acid over glutamic acid ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". ... cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid ...
The CASP8 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. ... Boldin MP, Goncharov TM, Goltsev YV, Wallach D (June 1996). "Involvement of MACH, a novel MORT1/FADD-interacting protease, in ...
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of ... The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... 1996). "Mch3, a novel human apoptotic cysteine protease highly related to CPP32". Cancer Res. 55 (24): 6045-52. PMID 8521391. ...
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of ... The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... Fernandes-Alnemri T, Litwack G, Alnemri ES (Aug 1995). "Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene ...
... (EC 3.4.23.21, Rhizopus aspartic proteinase, neurase, Rhizopus acid protease, Rhizopus acid proteinase) is an ... "Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419- ... Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (October 1987). "Binding of a reduced peptide inhibitor to the aspartic ... Kurono, Y.; Chidimatsu, M.; Horikoshi, K.; Ikeda, Y. (1971). "Isolation of a protease from a Rhizopus product". Agric. Biol. ...
BACE1 is an aspartic acid protease important in the formation of myelin sheaths in peripheral nerve cells: in mice the ... BACE1 is distantly related to the pathogenic aspartic-acid protease plasmepsin, which is a potential target for future anti- ... membrane-associated aspartic protease 2, memapsin-2, aspartyl protease 2, and ASP2, is an enzyme that in humans is encoded by ... "Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE". Science. 286 ( ...
Similar to other aspartic proteases, cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to ... The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and ... Cathepsin-D is an aspartic protease that depends critically on protonation of its active site Asp residue. Along with Asp- ...
Caspase stands for cysteine-aspartic acid protease and play an essential role in the apoptotic pathway of the cell. Protease 2A ... Picornain 3C are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Therefore, protease 3C depends on poliovirus 3CD protein for the translocation of 3C protease to carry out transcription ... Much testing will hopefully find an effective antiviral therapy targeting 3C protease. Targeting and inhibiting 3C protease ...
... (EC 3.4.23.20, peptidase A, Penicillium janthinellum aspartic proteinase, acid protease A, Penicillium citrinum ... acid proteinase, Penicillium cyclopium acid proteinase, Penicillium expansum acid proteinase, Penicillium janthinellum acid ... Penicillium roqueforti acid proteinase, Penicillium duponti aspartic proteinase, Penicillium citrinum aspartic proteinase) is ... Emi S, Myers DV, Iacobucci GA (February 1976). "Purification and properties of the thermostable acid protease of Penicillium ...
... (EC 3.4.23.26, Rhodotorula aspartic proteinase, Cladosporium acid protease, Cladosporium acid proteinase, ... Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on ... "Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of ... "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by ...
Mucor acid proteinase, Mucor acid protease, Mucor miehei aspartic proteinase, Mucor miehei aspartic protease, Mucor pusillus ... "Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic ... doi:10.1016/0076-6879(70)19033-1. Ottesen M, Rickert W (1970). "The acid protease of Mucor miehei". Methods Enzymol. 19: 459- ... Mucorpepsin (EC 3.4.23.23, Mucor rennin, Mucor aspartic proteinase, ...
Barkholt V (September 1987). "Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from ... Endothiapepsin (EC 3.4.23.22, Endothia aspartic proteinase, Endothia acid proteinase, Endothia parasitica acid proteinase, ... Hemmings AM, Foundling SI, Sibanda BL, Wood SP, Pearl LH, Blundell T (December 1985). "Energy calculations on aspartic ... Whitaker, J.R. (1970). "Protease of Endothia parasitica". Methods Enzymol. 19: 436-445. doi:10.1016/0076-6879(70)19032-x. ...
... using a threonine secondary alcohol Aspartic proteases - using an aspartate carboxylic acid Glutamic proteases - using a ... Alternatively, proteases may be classified by the optimal pH in which they are active: Acid proteases Neutral proteases ... Proteases are used throughout an organism for various metabolic processes. Acid proteases secreted into the stomach (such as ... Some proteases are less active after autolysis (e.g. TEV protease) whilst others are more active (e.g. trypsinogen). Proteases ...
The glutamine then returns the glutamic acid to its initial state. Aspartic protease Fujinaga M, Cherney MM, Oyama H, Oda K, ... These enzymes are acid proteases; eqolisin for example is most active at pH 2.0 when casein is used as substrate. Eqolosins ... Glutamic proteases are a group of proteolytic enzymes containing a glutamic acid residue within the active site. This type of ... belongs to subfamily of serine protease, serine-carboxyl protease (sedolisin) which was discovered in 2001. These proteases are ...
There are two classes of acidic proteases: Aspartic proteases - that use a catalytic aspartic acid in their active site ... Glutamic proteases - that use a catalytic glutamic acid in their active site (less common) This disambiguation page lists ... articles associated with the title Acidic protease. If an internal link led you here, you may wish to change the link to point ...
... is an enzyme that proteolytically cleaves other proteins at an aspartic acid residue, and belongs to a family of ... cysteine proteases called caspases. It is an inflammatory caspase, along with caspase 1, caspase 4 and the murine caspase 4 ...
Aspergillus acid protease, Aspergillus acid proteinase, Aspergillus aspartic proteinase, Aspergillus awamori acid proteinase, ... "The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from ... Aspergillus saitoi acid proteinase, pepsin-type aspartic proteinase, Aspergillus niger acid proteinase, sumizyme AP, proctase P ... aspartic proteinase from Aspergillus awamori. IV. Amino acid sequence of the enzyme". Bioorg. Khim. 12: 1030-1047. Yagi F, Fan ...
Enzymes in very low pH environments, like the aspartic protease pepsin in mammalian stomachs, may have catalytic aspartate or ... 2-Aminothiazoline-4-carboxylic acid is an intermediate in one industrial synthesis of L-cysteine for example. Aspartic acid is ... Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids ... As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react ...
... arginine-glycine-aspartic acid) motif. Most disintegrins contain this conserved RGD motif, but ADAM15 is the only member of the ... They include serine, aspartic, and cysteine-type proteases. A highly characterized example of the serine protease family is the ... while other proteases participate in the degradation and removal of the remaining cell debris. Proteases play numerous roles in ... Proteases not only facilitate angiogenesis, but they also have the ability to put the brakes on the process. One example of ...
... is an enzyme that proteolytically cleaves other proteins at an aspartic acid residue (LEVD-), and belongs to a family ... of cysteine proteases called caspases. The function of caspase 4 is not fully known, but it is believed to be an inflammatory ...
It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic ... the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. ... Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5, and caspase 9. It ... Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two ...
Each monomer contributes an aspartic acid residue that is essential for catalysis, Asp-25 and Asp-25´. The HIV protease has the ... HIV protease inhibitors fit the active site of the HIV aspartic protease and were rationally designed utilizing knowledge of ... In common usage HIV usually implies HIV-1. HIV-1 protease is one of the best known aspartic proteases, and an attractive target ... The mechanism of the HIV protease shares many features with the rest of the aspartic protease family although the full detailed ...
Proteases of this group hydrolyzes peptide bonds after the negatively charged glutamic acid or aspartic acid, with a higher ... "V8 protease". Other common references to this protease are staphylococcal serine protease, and SspA from its corresponding gene ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ... It has been shown that in spite of their similarities, the proteases from different species may differ in their efficiency in ...
Protease Serine protease Threonine protease Aspartic protease Metalloprotease Enzyme Proteolysis Catalytic triad Convergent ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and amino acids. ... Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common ... and the aspartic protease precursor pepsinogen. The protease is activated by removal of an inhibitory segment or protein. ...
An antisteatosis response regulated by oleic acid through lipid droplet-mediated ERAD enhancement. Castillo-Quan JI, Steinbaugh ... Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1 Nicolas J Lehrbach 1 2 , Gary Ruvkun 1 ... Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1 Nicolas J Lehrbach et al. Elife. 2016 ... Figure 5.. The DDI-1 aspartic protease is required for proteolytic activation of SKN-1A. (a) Schematic of the DDI-1 protein ...
Aspartic Acid Proteases Entry term(s). Acid Protease, Aspartic Acid Proteases, Aspartic Acid Proteinase, Aspartic Aspartic Acid ... Acid Protease, Aspartic. Acid Proteases, Aspartic. Acid Proteinase, Aspartic. Aspartic Acid Protease. Aspartic Acid Proteinase ... Aspartic Acid Protease, Aspartyl Proteases, Aspartic Acid Proteases, Aspartyl Proteinase, Aspartic Proteinase, Aspartic Acid ... Protease, Aspartic Acid. Protease, Aspartyl. Proteases, Aspartic Acid. Proteases, Aspartyl. Proteinase, Aspartic. Proteinase, ...
Aspartic Acid Protease Aspartic Acid Proteinase Aspartic Acid Proteinases Aspartic Proteinase Aspartic Proteinases Aspartyl ... Aspartic Acid Proteases [D08.811.277.656.074] * Aspartic Acid Endopeptidases [D08.811.277.656.074.500] ... A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.. Terms. Aspartic Acid Proteases ... 2010; see ASPARTIC ENDOPEPTIDASES 2000-2009, see ASPARTIC PROTEINASES 1991-1999. History Note. 2010; use ASPARTIC ACID ...
Aspartic Acid Protease Aspartic Acid Proteinase Aspartic Acid Proteinases Aspartic Proteinase Aspartic Proteinases Aspartyl ... Aspartic Acid Proteases [D08.811.277.656.074] * Aspartic Acid Endopeptidases [D08.811.277.656.074.500] ... A subclass of peptide hydrolases that depend on an ASPARTIC ACID residue for their activity.. Terms. Aspartic Acid Proteases ... 2010; see ASPARTIC ENDOPEPTIDASES 2000-2009, see ASPARTIC PROTEINASES 1991-1999. History Note. 2010; use ASPARTIC ACID ...
ß-secretase is a membrane-bound protease with motifs containing the highly conserved signature sequence of aspartic proteases, ... D(T/S)G(T/S), within which the aspartic acid residue is essential for proteolytic activity. The crystal structure of BACE1 ... ß-site amyloid precursor protein cleaving enzyme, a single membrane-spanning aspartic protease, is responsible for ß-secretase ... The γ-secretase complex is an aspartic intramembrane protease comprised of presenilin as a catalytic subunit, nicastrin, ...
A partial amino acid sequence of a vigor-related protein and osmopriming-enhanced expression of putative aspartic protease. ... has published an article entitled(Promotive Effect of Ascorbic Acid, Gallic Acid, Selenium and Nano-Selenium on Seed ... Exogenous ascorbic acid mitigates accumulation of abscisic acid, proline and polyamine under osmotic stress in maize leaves. ... Exogeneous application of ascorbic acid, salicylic acid and hydrogen peroxide improves the productivity of hybrid maize at low ...
Ácido Aspártico Proteases. Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. ... Cisteína Proteases. Cysteine Proteases. Proteasas de Cisteína. Coativador 1 do Receptor Nuclear. Nuclear Receptor Coactivator 1 ...
... three other aspartic proteases involved in hemoglobin metabolism but has a histidine in place of one of the two aspartic acids ... One of these proteases (Histidine Aspartic Protease, HAP) is homologous to ... Louis, MO) showed how the Malaria Genome Project helped to find novel proteases, several of which appear to function in ... Despite this change, HAP is an active protease with distinct properties, and together with a series of cysteine and ...
Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two ... This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a ... This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a ... Protease. / Cysteine Protease. / Caspase-7 Protein / Enzyme Modulator. / Protease Inhibitor. / Caspase-7. ...
Moreover, the active site of the Pep4um has the two characteristic aspartic acid residues of aspartyl proteases. The pep4um ... Pep4um-rec was confirmed to be an aspartic protease by specifically inhibiting its enzymatic activity with pepstatin A. Pep4um- ... The pep4um gene (um04926) of Ustilago maydis encodes a protein related to either vacuolar or lysosomal aspartic proteases. ... To the best of our knowledge this is the first report about the heterologous expression of an aspartic protease from a ...
A gene on chromosome 11q22.2-q22.3 that encodes a protein belonging to the cysteine-aspartic acid protease (caspase) family ...
... of higher Rabbit polyclonal to Caspase 3.This gene encodes a protein which is a member of the cysteine-aspartic acid protease ( ... Although basic in structure, lysophosphatidic acid (LPA) is a powerful bioactive. * Post author By cancerhugs ... Although basic in structure, lysophosphatidic acid (LPA) is a powerful bioactive lipid that profoundly influences mobile ... and polyunsaturated essential fatty acids, seem to be Istradefylline well-absorbed in the mouse and rat intestine [59,63]. ...
Aspartic Acid Proteases UI - D057055 MN - D8.811.277.656.74 MS - A subclass of peptide hydrolases that depend on an ASPARTIC ... HN - 2010; use ASPARTIC ACID ENDOPEPTIDASES 1991-2009 BX - Aspartic Acid Proteinases BX - Aspartic Proteinases BX - Aspartyl ... The amino acid sequence of thyrotropin alfa is identical to that of human pituitary thyroid stimulating hormone. HN - 2010 MH ... Lactic acid is the main product of their carbohydrate metabolism. HN - 2010 BX - Weisella MH - Leukoencephalopathies UI - ...
Accordingly, the amino acid sequence alignment of the aspartic protease gene from Aspergillus oryzae DRDFS 13 showed 98% ... Aspartic protease gene amplification and sequencingAmplification of the aspartic protease gene was done using forward primers ... cDNA synthesis and amplification of aspartic protease gene. The concentration of RNA and aspartic protease gene was 140.1ng/µL ... The gene sequence results showed 98% similarity with aspartic protease gene from A. oryzae RIB40. The aspartic protease gene ...
... cysteine-aspartic acid protease (caspase) 9 and hypoxia-inducible factor 1α messenger ribonucleic acid (mRNA) gene expression ... cysteine-aspartic acid protease (caspase) 9 and hypoxia-inducible factor 1α messenger ribonucleic acid (mRNA) gene expression ... Total ribonucleic acid was extracted from these samples. Quantitative real-time polymerase chain reaction was performed, and ... Total ribonucleic acid was extracted from these samples. Quantitative real-time polymerase chain reaction was performed, and ...
This provector was generated by inserting a tetra-aspartic acid inactivating motif flanked by the MMP-14 cleavage sequence ... In order to target tumors, we have engineered an MMP-14 protease-activatable AAV vector that responds to both membrane-bound ... This proof-of-concept study illustrates the possibilities of membrane-bound protease-activatable gene therapies to target ... Membrane-bound MMP-14 protease-activatable adeno-associated viral vectors for gene delivery to pancreatic tumors.. ...
Ácido Aspártico Proteases. Aspartic Acid Proteases. Proteasas de Ácido Aspártico. D09 - Carboidratos. Prebióticos. Prebiotics. ... Cisteína Proteases. Cysteine Proteases. Proteasas de Cisteína. Coativador 1 do Receptor Nuclear. Nuclear Receptor Coactivator 1 ...
Aspartic Acid Endopeptidases/metabolism*; Aspartic Acid/drug effects; Aspartic Acid/metabolism*; Catalysis; Enzyme Activation/ ... Computer modeling of 1 bound in the crystal structure of the SIV protease using DOCK 3.5 indicates that 1 has appropriate ... MeSH Terms: Alkylation/drug effects; Antiviral Agents/pharmacology*; Aspartic Acid Endopeptidases/antagonists & inhibitors*; ... able to align in an orientation that allows a proton to be transferred to the epoxide from one of the catalytic aspartic acid ...
have proposed that the H-bond between aspartic acid 102 and histidine 57 in the catalytic triad of serine proteases is an ... Urocanic Acid) RN - 56-84-8 (Aspartic Acid) RN - 71-00-1 (Histidine) RN - 94242-73-6 (O-methyl-succinyl-alanyl-alanyl-prolyl- ... Aspartic Acid/chemistry MH - Binding Sites MH - Boronic Acids/metabolism MH - Catalysis MH - Histidine/chemistry MH - Hydrogen ... Abscisic Acid) RN - 69-72-7 (Salicylic Acid) RN - 7647-14-5 (Sodium Chloride) SB - IM MH - Abscisic Acid/pharmacology MH - ...
Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition ... Microbial exposure of rural school children, as assessed by levels of N-acetyl-muramic acid in mattress dust, and its ... Structural model of MD-2 and functional role of its basic amino acid clusters involved in cellular lipopolysaccharide ...
... three other aspartic proteases involved in hemoglobin metabolism but has a histidine in place of one of the two aspartic acids ... One of these proteases (Histidine Aspartic Protease, HAP) is homologous to ... Louis, MO) showed how the Malaria Genome Project helped to find novel proteases, several of which appear to function in ... Despite this change, HAP is an active protease with distinct properties, and together with a series of cysteine and ...
1995) Characteristics of YAP3, a new prohormone processing aspartic protease from S. cerevisiae. In: Aspartic Proteinases. ... Bamberger AM, Bamberger CM, Pu L-P, Puy LA, Loh YP and Asa SL (1995) Expression of Pit-1 messenger ribonucleic acid and protein ... basic residue-specific aspartic proteases in prohormone conversion." In: Aspartic Proteinases. Takahashi, K. (ed) Plenum Press ... Cawley NX, Wong M, Pu L-P, Tam W and Loh YP (1995) Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminus ...
Ectopic expression of a grape aspartic protease gene, AP13, in Arabidopsis thaliana improves resistance to powdery mildew but ... Overexpression of VqWRKY31 enhances powdery mildew resistance in grapevine by promoting salicylic acid signaling and specific ... Keywords: Chinese wild Vitis; Disease resistance; JAZ protein; Powdery mildew; Salicylic acid. ... and salicylic acid (SA). The upregulation of VqJAZ4 after inoculation was dependent on its promoter sequences. Expression of ...
Aspartate-tRNA Ligase N0000006508 Aspartic Acid N0000007954 Aspartic Acid Endopeptidases N0000180269 Aspartic Acid Proteases ... Neutral N0000006806 Amino Acids N0000011372 Amino Acids, Acidic N0000011248 Amino Acids, Aromatic N0000011332 Amino Acids, ... Acyclic N0000008269 Acids, Aldehydic N0000007628 Acids, Carbocyclic N0000007629 Acids, Heterocyclic N0000007630 Acids, ... Amino Acid Isomerases N0000167825 Amino Acid Oxidoreductases N0000169801 Amino Acid Transport System A N0000169803 Amino Acid ...
Secreted Aspartic Proteases. D000097790. Community of Practice. D000097163. Kir5.1 Channel. D000097062. Sigma-1 Receptor. ... Rosmarinic Acid. D000097123. Cold Urticaria. D000096703. Iodothyronine Deiodinase Type II. D000097564. Ross River Virus ... Retinoic Acid Receptor gamma. D000097768. Channa punctatus. D000095982. Inosine Triphosphatase. D000097630. Retrograde ...
... and 48 amino acids of the p6pol, separated by a protease cleavage site. The intact precursor (TFP-p6pol-PR) has very low dimer ... the 99-amino acid protease is flanked at its N-terminus by a transframe region (TFR) composed of the transframe octapeptide ( ... unlike proregions found in zymogen forms of monomeric aspartic proteases. Cleavage at the p6pol-PR site to release a free N- ... In the Gag-Pol polyprotein of HIV-1, the 99-amino acid protease is flanked at its N-terminus by a transframe region (TFR) ...
Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site.. Eizert H; Bander P; ... Bovine leukemia virus: purification and characterization of the aspartic protease.. Menard A; Mamoun RZ; Geoffre S; Castroviejo ... 3. Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites.. Bagossi P ... 1. Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. ...
... x ORTHO-AMINOBENZOIC ACID xx ANESTHETICS, LOCAL xx BENZOATES AMINOBUTYRIC ACID see BUTYRATES AMINOPEPTIDASES see PROTEASES ... ASPARTIC ACID ASPERGILLOSIS ASPERGILLUS ASPHYXIA x SUFFOCATION ASPHYXIA NEONATORUM xx INFANT, NEWBORN, diseases ASPIDIUM xx ... see also LINOLEIC ACID see also OLEIC ACID see also RICINOLEIC ACID see also STEARIC ACID see also UNDECYLENIC ACID xx ACIDS ... ACIDS see also AMINO ACIDS see also FATTY AC IDS see also KETONE ACIDS sr, also NICLEK ACIDS ACNE ACNE KELOID see FOLLICULITIS ...
  • Unlike serine or cysteine proteases these proteases do not form a covalent intermediate during cleavage. (wikipedia.org)
  • BZAR (Rhodamine 110, bis-(N-CBZ-L-arginine amide), dihydrochloride) is a substrate for serine proteases (1-5) and is also an inhibitor for quanidinobenzoatase. (biotium.com)
  • 5. Bochenska O., Rapala-Kozik M., Wolak N., Kamysz W., Grzywacz D., Aoki W., Ueda M., Kozik A. , Inactivation of human kininogen-derived antimicrobial peptides by secreted aspartic proteases produced by the pathogenic yeast Candida albicans. (lipopharm.pl)
  • 7. Bochenska O., Rapala-Kozik M., Wolak N., Kamysz W., Grzywacz D., Aoki W., Ueda M., Kozik A. , Contribution of secreted aspartic proteases of pathogenic yeast Candida albicans to the neutralization of antimicrobial function of human high molecular weight kininogen. (lipopharm.pl)
  • Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. (moonlightingproteins.org)
  • Aspartic proteases (also "aspartyl proteases", "aspartic endopeptidases") are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. (wikipedia.org)
  • In modern-day enzymes, although the three-dimensional structures are very similar, the amino acid sequences are more divergent, except for the catalytic site motif, which is very conserved. (wikipedia.org)
  • Acid proteases, commonly known as aspartic proteases are degredative enzymes which catalyze the cleavage reaction of peptide bonds in proteins with a pH optimum in the acidic range (pH 3-4). (metu.edu.tr)
  • 8 Proteases as the important enzymes in the cells, can disclose this diversity. (microbiologyjournal.org)
  • We selected from the crystal structures of holo aspartic proteases a library of nearly 350 inhibitors for in silico screening. (bvsalud.org)
  • 9. Ostrowska K., Kamysz W., Dawgul M., Rozalski A. , Synthetic Amphibian Peptides and Short Amino-Acids Derivatives Against Planktonic Cells and Mature Biofilm of Providencia stuartii Clinical Strains. (lipopharm.pl)
  • 11. Bras G., Bochenska O., Rapala-Kozik M., Guevara-Lora I., Faussner A., Kamysz W., Kozik A. , Release of biologically active kinin peptides, Met-Lys-bradykinin and Leu-Met-Lys-bradykinin from human kininogens by two major secreted aspartic proteases of Candida parapsilosis. (lipopharm.pl)
  • Aspartic endopeptidases EC 3.4.23. (wikipedia.org)
  • More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin and archaean preflagellin have been described. (wikipedia.org)
  • Omptin family) Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. (wikipedia.org)
  • A compound which inhibits or antagonizes the biosynthesis or actions of proteases (endopeptidases). (mcw.edu)
  • HIV-1 protease - a major drug-target for treatment of HIV Plasmepsin - a group of aspartyl proteases found in the Malaria-causing parasite Plasmodium Glutamic protease The Proteolysis Map Fusek M, Mares M, Vetvicka V (2013-01-01). (wikipedia.org)
  • The Dutch type, the most common of all the types, is caused by the replacement of the amino acid glutamic acid with the amino acid glutamine at position 22 in the protein sequence (written as Glu22Gln or E22Q). (medlineplus.gov)
  • The Italian type and Arctic type are also caused by changes to glutamic acid at position 22. (medlineplus.gov)
  • In the Italian type, glutamic acid is replaced with the amino acid lysine (written as Glu22Lys or E22K) and in the Arctic type, glutamic acid is replaced with the amino acid glycine (written as Glu22Gly or E22G). (medlineplus.gov)
  • [ 8 ] The enzyme gamma-glutamyl carboxylase, in the presence of vitamin K, converts the N- terminal glutamic acid residues to gamma-carboxyglutamic acid residues. (medscape.com)
  • EDANS is one of the most popular donors for developing FRET-based nucleic acid probes and protease substrates. (zjhandybio.com)
  • Nearly all known aspartyl proteases are inhibited by pepstatin. (wikipedia.org)
  • Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. (wikipedia.org)
  • Aspartyl proteases are a highly specific family of proteases - they tend to cleave dipeptide bonds that have hydrophobic residues as well as a beta-methylene group. (wikipedia.org)
  • While a number of different mechanisms for aspartyl proteases have been proposed, the most widely accepted is a general acid-base mechanism involving coordination of a water molecule between the two highly conserved aspartate residues. (wikipedia.org)
  • Its substrate binding site features a non-catalytical pair of aspartic acids which resembles the catalytic dyad of aspartic proteases. (bvsalud.org)
  • Effect of nucleic acid type and concentration was characterised in LNPs formulated with a benchmark LNP composition and four different NAs (polyadenylic acid, polyuridylic acid, double stranded and single stranded DNA). (lu.se)
  • Encapsulation in self-assembled lipid structures has been shown to increase the stability of large biomolecules, including proteins and nucleic acids (NAs), which has many potential applications in the food and pharmaceutical industries. (lu.se)
  • Comparison between the effect on the L3 phase of encapsulated beta-galactosidase (238 kDa), aspartic protease (34 kDa), myoglobin (17.6 kDa) and phytoglobin BvPgb 1.2 (38.4 kDa) demonstrated the importance of specific lipid-protein interactions on the L3 structure both in bulk and dispersions, as well as the stability of the encapsulated proteins. (lu.se)
  • Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. (wikipedia.org)
  • One aspartate activates the water by abstracting a proton, enabling the water to perform a nucleophilic attack on the carbonyl carbon of the substrate scissile bond, generating a tetrahedral oxyanion intermediate stabilized by hydrogen-bonding with the second aspartic acid. (wikipedia.org)
  • Pepstatin is an inhibitor of aspartate proteases. (wikipedia.org)
  • This variant replaces the amino acid valine with the amino acid isoleucine at protein position 717 (written as Val717Ile or V717I). (medlineplus.gov)
  • The Flemish type is caused by replacement of the amino acid alanine with glycine at position 21 (written as Ala21Gly or A21G). (medlineplus.gov)
  • In the Iowa type, the amino acid aspartic acid is switched with the amino acid asparagine at position 23 (written as Asp23Asn or D23N). (medlineplus.gov)
  • The Piedmont type of hereditary cerebral amyloid angiopathy is caused by the replacement of the amino acid leucine at position 34 with the amino acid valine (written as Leu34Val or L34V). (medlineplus.gov)
  • Metabolic syndrome' in the brain: deficiency in omega-3 fatty acid exacerbates dysfunctions in insulin receptor signalling and cognition. (annualreviews.org)
  • The most common APP gene variant changes one of the protein building blocks (amino acids) in the amyloid precursor protein. (medlineplus.gov)
  • These variants change single amino acids in the amyloid precursor protein. (medlineplus.gov)
  • 2017 . Effect of long-term omega 3 polyunsaturated fatty acid supplementation with or without multidomain intervention on cognitive function in elderly adults with memory complaints (MAPT): a randomised, placebo-controlled trial. (annualreviews.org)
  • D 2 R (Rhodamine 110, bis-(L-aspartic acid amide), ditrifluoroacetic acid salt) is a general substrate for caspases including caspases 3 and 7. (biotium.com)
  • Acid proteases have crucial roles in metabolism. (metu.edu.tr)
  • We describe a ribonucleic acid (RNA) reporter system for live-cell imaging of gene expression to detect changes in polymerase II activity on individual promoters in individual cells. (metu.edu.tr)
  • The substrate has been reported to enter live cells and be hydrolyzed by lysosomal proteases (3). (biotium.com)
  • The presence and position of disulfide bridges are other conserved features of aspartic peptidases. (wikipedia.org)
  • 2013 . Omega-3 fatty acids and domain-specific cognitive aging: secondary analyses of data from WHISCA. (annualreviews.org)
  • 11,12 Particularly microbial proteases that are used in many industries such as food processing and detergent. (microbiologyjournal.org)
  • 13 Many proteases investigated by researchers 14 , although protease (carboxypeptidase A1, CPA1) in Neurospora crassa gained inevitable and unavoidable position as it is from one easy culturing model fungus ( N. crassa ) besides its variety of approved functions in the cell. (microbiologyjournal.org)