EC 2.8.1.7
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EC 2.8.1.7
In enzymology, a cysteine desulfurase () is an enzyme that catalyzes the chemical reaction :L-cysteine + nzymecysteine \rightleftharpoons L-alanine + nzymeS-sulfanylcysteine Thus, the two substrates of this enzyme are L-cysteine and nzymecysteine], whereas its two product (chemistry), products are L-alanine and nzymeS-sulfanylcysteine. One group of authors has given it the acronym hapE, for hydrogen sulfide, alanine, and pyruvate producing enzyme. This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine: nzyme cysteinesulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase. Function Bacteria contain cysteine desulfurases to form iron sulfur clusters in proteins. However recently it has been shown that the enzyme, which produces hydrogen sulfide from cysteine, is also a virulence factor, namely for ...
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Enzymology
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Iron Sulfur Cluster
Iron is a chemical element; it has symbol Fe () and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, forming much of Earth's outer and inner core. It is the fourth most abundant element in the Earth's crust, being mainly deposited by meteorites in its metallic state. Extracting usable metal from iron ores requires kilns or furnaces capable of reaching , about 500 Â°C (900 Â°F) higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BC and the use of iron tools and weapons began to displace copper alloys – in some regions, only around 1200 BC. That event is considered the transition from the Bronze Age to the Iron Age. In the modern world, iron alloys, such as steel, stainless steel, cast iron and special steels, are by far the most common industrial metals, due to their mechanical proper ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules such as proteins and nucleic acids, which is overseen by the Worldwide Protein Data Bank (wwPDB). This structural data is obtained and deposited by biologists and biochemists worldwide through the use of experimental methodologies such as X-ray crystallography, Nuclear magnetic resonance spectroscopy of proteins, NMR spectroscopy, and, increasingly, cryo-electron microscopy. All submitted data are reviewed by expert Biocuration, biocurators and, once approved, are made freely available on the Internet under the CC0 Public Domain Dedication. Global access to the data is provided by the websites of the wwPDB member organizations (PDBe, PDBj, RCSB PDB, and BMRB). The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other ...
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Tertiary Structure
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demon ...
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Thiamine Metabolism
Thiamine, also known as thiamin and vitamin B1, is a vitamin – an Nutrient#Micronutrients, essential micronutrient for humans and animals. It is found in food and commercially synthesized to be a dietary supplement or medication. Phosphorylated forms of thiamine are required for some Metabolism, metabolic reactions, including the breakdown of Carbohydrate metabolism, glucose and amino acids. Food sources of thiamine include whole grains, legumes, and some meats and fish. Refined grain, Grain processing removes much of the vitamin content, so in many countries cereals and flours are food fortification, enriched with thiamine. Supplements and medications are available to treat and prevent thiamine deficiency and the disorders that result from it such as Thiamine deficiency#Dry beriberi, beriberi and Wernicke encephalopathy. They are also used to treat maple syrup urine disease and Leigh syndrome. Supplements and medications are typically taken Route of administration#Oral ...
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β-haemolysis
Hemolysis is the breakdown of red blood cells. The ability of bacterial colonies to induce hemolysis when grown on blood agar is used to classify certain microorganisms. This is particularly useful in classifying streptococcal species. A substance that causes hemolysis is called a hemolysin. Types Alpha-hemolysis When alpha-hemolysis (α-hemolysis) is present, the agar under the colony is light and greenish. ''Streptococcus pneumoniae'' and a group of oral streptococci ( ''Streptococcus'' viridans or viridans streptococci) display alpha-hemolysis. This is sometimes called ''green hemolysis'' because of the color change in the agar. Other synonymous terms are ''incomplete hemolysis'' and ''partial hemolysis''. Alpha-hemolysis is caused by the bacteria's production of hydrogen peroxide, which oxidizes hemoglobin and produces the green oxidized derivative methemoglobin. Beta-hemolysis Beta-hemolysis (β-hemolysis), sometimes called ''complete hemolysis'', is a complete lysis of re ...
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Virulence Factor
Virulence factors (preferably known as pathogenicity factors or effectors in botany) are cellular structures, molecules and regulatory systems that enable microbial pathogens (bacteria, viruses, fungi, and protozoa) to achieve the following: * colonization of a niche in the host (this includes movement towards and attachment to host cells) * immunoevasion, evasion of the host's immune response * immunosuppression, inhibition of the host's immune response (this includes leukocidin-mediated cell death) * entry into and exit out of cells (if the pathogen is an intracellular one) * obtain nutrition from the host Specific pathogens possess a wide array of virulence factors. Some are chromosomally encoded and intrinsic to the bacteria (e.g. capsules and endotoxin), whereas others are obtained from mobile genetic elements like plasmids and bacteriophages (e.g. some exotoxins). Virulence factors encoded on mobile genetic elements spread through horizontal gene transfer, and can con ...
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Hydrogen Sulfide
Hydrogen sulfide is a chemical compound with the formula . It is a colorless chalcogen-hydride gas, and is toxic, corrosive, and flammable. Trace amounts in ambient atmosphere have a characteristic foul odor of rotten eggs. Swedish chemist Carl Wilhelm Scheele is credited with having discovered the chemical composition of purified hydrogen sulfide in 1777. Hydrogen sulfide is toxic to humans and most other animals by inhibiting cellular respiration in a manner similar to hydrogen cyanide. When it is inhaled or its salts are ingested in high amounts, damage to organs occurs rapidly with symptoms ranging from breathing difficulties to convulsions and death. Despite this, the human body produces small amounts of this sulfide and its mineral salts, and uses it as a signalling molecule. Hydrogen sulfide is often produced from the microbial breakdown of organic matter in the absence of oxygen, such as in swamps and sewers; this process is commonly known as anaerobic digestio ...
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List Of Enzymes
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: :Oxidoreductases (EC 1) ( Oxidoreductase) * Dehydrogenase * Luciferase * DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) ** Homoserine dehydrogenase ** Aminopropanol oxidoreductase ** Diacetyl reductase ** Glycerol dehydrogenase ** Propanediol-phosphate dehydrogenase ** glycerol-3-phoshitiendopene dehydrogenase (NAD+) ** D-xylulose reductase ** L-xylulose reductase ** Lactate dehydrogenase ** Malate dehydrogenase ** Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) ** Glucose oxidase ** L-gulonolactone oxidase ** Thiamine oxidase ** Xanthine oxidase * EC 1.1.4 (with a disulfide as accep ...
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Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Sulfurtransferase
A sulfurtransferase is a transferase enzyme that act upon atoms of sulfur. An example is thiosulfate sulfurtransferase Rhodanese is a mitochondrion, mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate"). In enzymatology, the common name is listed as thiosulfate sulfurtransferase (). The diagram o .... References External links * EC 2.8 Sulfur metabolism {{2.8-enzyme-stub ...
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