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Dissimilatory Sulfite Reductase
Dissimilatory sulfite reductase () is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction. The enzyme is essential in prokaryotic sulfur-based energy metabolism, including sulfate/sulfite reducing organisms, sulfur-oxidizing bacteria, and organosulfonate reducers. In sulfur reducers it catalyses the reduction of sulfite to sulfide (reaction 1), while in sulfur oxidizers it catalyses the opposite reaction (reaction 2). The reaction involves the small protein DsrC, which is present in all the organisms that contain dissimilatory sulfite reductase. During the process an intramolecular trisulfide is formed between two L-cysteine residues of DsrC and the sulfur atom from sulfite. This trisulfide can be reduced by a number of proteins including DsrK and TcmB. Reaction in organisms performing dissimilatory sulfate reduction: : (1) sulfite + a srC proteindithiol + 2 reduced acceptor + 2 H+ = hydrogen sulfide + a srC proteindisulfide + 2 acceptor + 3 H2O ...
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Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the 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 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 are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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Sulfur Metabolism
Sulfur is metabolism, metabolized by all organisms, from bacteria and archaea to plants and animals. Sulfur is redox, reduced or redox, oxidized by organisms in a variety of forms. The chemical element, element is present in proteins, organosulfate, sulfate esters of polysaccharides, steroids, phenols, and sulfur-containing coenzymes. Oxidation Reduced sulfur compounds are oxidized by most organisms, including higher animals and higher plants. Some organisms can conserve energy (i.e., produce adenosine triphosphate, ATP) from the oxidation of sulfur. Sulfur is the sole energy source for some lithotrophic bacteria and archaea. Reduced sulfur compounds, such as hydrogen sulfide, elemental sulfur, sulfite, thiosulfate, and various polythionates (e.g., tetrathionate), are used by various lithotrophic bacteria and are all oxidized by ''Acidithiobacillus''. Sulfur oxidizers use enzymes such as Sulfide:quinone reductase, sulfur dioxygenase and sulfite oxidase to oxidize sulfur compoun ...
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Dissimilatory Sulfate Reduction
Dissimilatory sulfate reduction is a form of anaerobic respiration that uses sulfate as the terminal electron acceptor to produce hydrogen sulfide. This metabolism is found in some types of bacteria and archaea which are often termed sulfate-reducing organisms. The term "''dissimilatory''" is used when hydrogen sulfide is produced in an anaerobic respiration process. By contrast, the term "''assimilatory''" would be used in relation to the biosynthesis of organosulfur compounds, even though hydrogen sulfide may be an intermediate. Dissimilatory sulfate reduction occurs in four steps: # Conversion (activation) of sulfate to adenosine 5’-phosphosulfate (APS) via sulfate adenylyltransferase # Reduction of APS to sulfite via adenylyl-sulfate reductase # Transfer of the sulfur atom of sulfite to the DsrC protein creating a trisulfide intermediate catalyzed by DsrAB # Reduction of the trisulfide to sulfide and reduced DsrC via a membrane bound enzyme, DsrMKJOP Which requires the cons ...
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List Of Enzymes
This article lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system. * List of EC numbers (EC 5) * List of EC numbers (EC 6) :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-phosphate 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 disul ...
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Iron Enzymes
Iron () is a chemical element with symbol Fe (from la, ferrum) 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, right in front of oxygen (32.1% and 30.1%, respectively), forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust. In its metallic state, iron is rare in the Earth's crust, limited mainly to deposition by meteorites. Iron ores, by contrast, are among the most abundant in the Earth's crust, although extracting usable metal from them requires kilns or furnaces capable of reaching or higher, about higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BCE and the use of iron tools and weapons began to displace copper alloys, in some regions, only around 1200 BCE. That event is considered the transition from the Bronze Age to the Iron Age. In ...
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