Haloacid Dehydrogenase Superfamily
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Haloacid Dehydrogenase Superfamily
The haloacid dehydrogenase superfamily (HAD superfamily) is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification. Examples A HAD domain is found in several distinct proteins including: * Phospholipid-translocating ATPase , a putative lipid-flipping enzyme involved in cold tolerance in '' Arabidopsis'' * 3-deoxy-D-manno-octulosonate (KDO) 8-phosphate phosphatase (), which catalyses the final step in the biosynthesis of KDO - a component of lipopolysaccharide in Gram-negative bacteria * Mannosyl-3-phosphoglycerate phosphatase (), which hydrolyses mannosyl-3-phosphoglycerate to form the osmolyte mannosylglycerate * Phosphoglycolate phosphatase (), which catalyses the dephosphorylation of 2-phosphoglycolate *5´-Nucleotidase (EC 3.1.3.5) which either catalyzes the hydro ...
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Protein Superfamily
A protein superfamily is the largest grouping (clade) of proteins for which common ancestry can be inferred (see homology (biology), homology). Usually this common ancestry is inferred from structural alignment and mechanistic similarity, even if no sequence similarity is evident. Sequence homology can then be deduced even if not apparent (due to low sequence similarity). Superfamilies typically contain several protein families which show sequence similarity within each family. The term ''protein clan'' is commonly used for protease and glycosyl hydrolases superfamilies based on the MEROPS and CAZy classification systems. Identification Superfamilies of proteins are identified using a number of methods. Closely related members can be identified by different methods to those needed to group the most evolutionarily divergent members. Sequence similarity Historically, the similarity of different amino acid sequences has been the most common method of inferring Sequence homology, h ...
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Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some s ...
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ATP10A
Phospholipid-transporting ATPase VA also known as ATPase class V type 10A or aminophospholipid translocase VA is an enzyme that in humans is encoded by the ''ATP10A'' gene. Function The protein encoded by ''ATP10A'' belongs to the family of P-type cation transport ATPases, and to the subfamily of aminophospholipid-transporting ATPases. The aminophospholipid translocases transport phosphatidylserine and phosphatidylethanolamine Phosphatidylethanolamine (PE) is a class of phospholipids found in biological membranes. They are synthesized by the addition of cytidine diphosphate- ethanolamine to diglycerides, releasing cytidine monophosphate. ''S''-Adenosyl methionine can ... from one side of a bilayer to another. This gene is maternally expressed. It maps within the most common interval of deletion responsible for Angelman syndrome, also known as 'happy puppet syndrome'. See also * Haloacid dehydrogenase superfamily References External links * Further reading * * * ...
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ATP8B3
The human gene ATP8B3 encodes the protein ATPase, aminophospholipid transporter, class I, type 8B, member 3. The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of aminophospholipid-transporting ATPases. The aminophospholipid translocases transport phosphatidylserine and phosphatidylethanolamine from one side of a bilayer to another. This gene encodes the member 3 of the phospholipid-transporting ATPase 8B. Alternatively spliced transcript variants encoding different isoform A protein isoform, or "protein variant", is a member of a set of highly similar proteins that originate from a single gene or gene family and are the result of genetic differences. While many perform the same or similar biological roles, some isof ...s have been found for this gene. References External links * Further reading * * * * EC 7.6.2 {{gene-19-stub ...
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Dephosphorylation
In biochemistry, dephosphorylation is the removal of a phosphate (PO43−) group from an organic compound by hydrolysis. It is a reversible post-translational modification. Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate. Dephosphorylation employs a type of hydrolytic enzyme, or hydrolase, which cleaves ester bonds. The prominent hydrolase subclass used in dephosphorylation is phosphatase, which removes phosphate groups by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl (-OH) group. The reversible phosphorylation-dephosphorylation reaction occurs in every physiological process, making proper function of protein phosphatases necessary for organism viability. Because protein dephosphorylation is a key process involved in cell signallin ...
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Phosphoglycolate Phosphatase
Phosphoglycolate phosphatase(EC 3.1.3.18; systematic name 2-phosphoglycolate phosphohydrolase), also commonly referred to as phosphoglycolate hydrolase, 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for catalyzing the conversion of 2-phosphoglycolate into glycolate and phosphate: : 2-phosphoglycolate + H2O = glycolate + phosphate First studied and purified within plants, phosphoglycolate phosphatase plays a major role in photorespiratory 2-phosphoglycolate metabolism, an essential pathway for photosynthesis in plants. The occurrence of photorespiration in plants, due to the lack of substrate specificity of rubisco, leads to the formation of 2-phosphoglycolate and 3-phosphoglycerate. 3-phosphogylcerate is the normal product of carboxylation and will enter the Calvin cycle. Phosphoglycolate, which is a potent inhibitor of phosphofructokinase and triosephosphate isomerase, must be quickly metabolized and transf ...
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Osmolyte
Osmolytes are low-molecular weight organic compounds that influence the properties of biological fluids. Their primary role is to maintain the integrity of cells by affecting the viscosity, melting point, and ionic strength of the aqueous solution. When a cell swells due to external osmotic pressure, membrane channels open and allow efflux of osmolytes which carry water with them, restoring normal cell volume. Osmolytes also interact with the constituents of the cell, e.g. they influence protein folding. Common osmolytes include amino acids, sugars and polyols, methylamines, methylsulfonium compounds, and urea. Case studies Natural osmolytes that can act as osmoprotectants include trimethylamine ''N''-oxide (TMAO), dimethylsulfoniopropionate, sarcosine, betaine, glycerophosphorylcholine, myo-inositol, taurine, glycine, and others. Remarkably, TMAO has the capacity to restore glucocorticoid binding to mutant receptors. Bacteria accumulate osmolytes for protection against a high o ...
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Hydrolysis
Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water is the nucleophile. Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. Hydrolysis reactions can be the reverse of a condensation reaction in which two molecules join into a larger one and eject a water molecule. Thus hydrolysis adds water to break down, whereas condensation builds up by removing water. Types Usually hydrolysis is a chemical process in which a molecule of water is added to a substance. Sometimes this addition causes both the substance and w ...
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Mannosyl-3-phosphoglycerate Phosphatase
The enzyme mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) catalyzes the reaction :2-''O''-(α-D-mannosyl)-3-phosphoglycerate + H2O = 2-''O''-(α-D-mannosyl)-D-glycerate + phosphate This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2-''O''-(α-D-mannosyl)-3-phosphoglycerate phosphohydrolase. Structural studies As of late 2007, two structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... have been solved for this class of enzymes, with PDB accession codes and . References EC 3.1.3 Enzymes of known structure {{3.1-enzyme-stub ...
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