Cyanophycinase
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Cyanophycinase
Cyanophycinase (, ''cyanophycin degrading enzyme'', ''beta-Asp-Arg hydrolysing enzyme'', ''CGPase'', ''CphB'', ''CphE'', ''cyanophycin granule polypeptidase'', ''extracellular CGPase'') is an enzyme. It catalyses the following chemical reaction : -Asp(4-L-Arg)sub>n + H2O \rightleftharpoons -Asp(4-L-Arg)sub>n-1 + L-Asp(4-L-Arg) The enzyme is highly specific for the branched polypeptide cyanophycin. It is similar to Dipeptidase E, another S51 family serine protease. Structure The asymmetric unit of cyanophycinase consists of three identical chains, each containing 291 residues. The structure of cyanophycinase was determined from the freshwater cyanobacterium Synechocystis sp. PCC 6803 at 1.5-A resolution, which showed that the structure is dimeric. Enzyme function Cyanophycinase is a carboxy terminal specific exopeptidase, meaning it catalyzes the cleavage of the carboxy terminal peptide bond of cyanophycin. It was hypothesized that cyanophycinase was a serine protease ...
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Biological Assembly Of Cyanophycinase
Biology is the scientific study of life. It is a natural science with a broad scope but has several unifying themes that tie it together as a single, coherent field. For instance, all organisms are made up of cells that process hereditary information encoded in genes, which can be transmitted to future generations. Another major theme is evolution, which explains the unity and diversity of life. Energy processing is also important to life as it allows organisms to move, grow, and reproduce. Finally, all organisms are able to regulate their own internal environments. Biologists are able to study life at multiple levels of organization, from the molecular biology of a cell to the anatomy and physiology of plants and animals, and evolution of populations.Based on definition from: Hence, there are multiple subdisciplines within biology, each defined by the nature of their research questions and the tools that they use. Like other scientists, biologists use the scientific metho ...
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The Active Site And Catalytic Triad Of Cyanophycinase
''The'' () is a grammatical article in English, denoting persons or things that are already or about to be mentioned, under discussion, implied or otherwise presumed familiar to listeners, readers, or speakers. It is the definite article in English. ''The'' is the most frequently used word in the English language; studies and analyses of texts have found it to account for seven percent of all printed English-language words. It is derived from gendered articles in Old English which combined in Middle English and now has a single form used with nouns of any gender. The word can be used with both singular and plural nouns, and with a noun that starts with any letter. This is different from many other languages, which have different forms of the definite article for different genders or numbers. Pronunciation In most dialects, "the" is pronounced as (with the voiced dental fricative followed by a schwa) when followed by a consonant sound, and as (homophone of the archaic ...
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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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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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Chemical Reaction
A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the Atomic nucleus, nuclei (no change to the elements present), and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive Chemical element, elements where both electronic and nuclear changes can occur. The substance (or substances) initially involved in a chemical reaction are called reagent, reactants or reagents. Chemical reactions are usually characterized by a chemical change, and they yield one or more Product (chemistry), products, which usually have properties different from the reactants. Reactions often consist of a sequence o ...
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Polypeptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides ...
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Cyanophycin
Cyanophycin, also known as CGP (cyanophycin granule polypeptide) or multi-L-arginyl-poly (L-aspartic acid), is a non-protein, non-ribosomally produced amino acid polymer composed of an aspartic acid backbone and arginine side groups. Cyanophycin was first detected in 1887 by the Italian botanist ''Antonino Borzì'' and can be found in most cyanobacteria and a few heterotrophic bacteria such as ''Acinetobacter'' sp. Cyanophycin is largely insoluble under physiological conditions and is accumulated in the form of granules in the cytoplasm during phosphate or sulfur starvation, generally in the early and mid-stationary phase. It is used as a nitrogen- and possibly carbon-storage compound and also serves as a dynamic buffer for fixed nitrogen in cyanobacterial heterocysts. Nitrogen and carbon are mobilized from cyanophycin by intracellular cyanophycinase in the form of aspartate-arginine dipeptides. Cyanophycin is synthesized from arginine and aspartate in an ATP-dependent reaction ...
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Dipeptidase E
Dipeptidase E (, ''aspartyl dipeptidase'', ''peptidase E'', ''PepE gene product ( Salmonella typhimurium)'') is an enzyme. This enzyme catalyses the following chemical reaction : Dipeptidase E catalyses the hydrolysis of dipeptides A dipeptide is an organic compound derived from two amino acids. The constituent amino acids can be the same or different. When different, two isomers of the dipeptide are possible, depending on the sequence. Several dipeptides are physiologicall ... Asp!Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides A free carboxy group is not absolutely required in the substrate. References External links * EC 3.4.13 {{Enzyme-stub ...
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Serine Protease
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. Classification The MEROPS protease classification system counts 16 superfamilies (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. The majority belong to the S1 family of the PA clan (superfamily) of proteases. For superfamilies, P: superfamily, containing a mixture of nucleophile class families, S: purely serine proteases. superfamily. Within each superfamily, families are designated by their catalytic nucleophile, (S: serine proteases). Substrate specificity Serine ...
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Synechocystis Sp
''Synechocystis'' is a genus of unicellular, freshwater cyanobacteria in the family Merismopediaceae. It includes a strain, ''Synechocystis'' sp. PCC 6803, which is a well studied model organism. Like all cyanobacteria, ''Synechocystis'' branches on the evolutionary tree from its ancestral root, '' Gloeobacter violaceus''. ''Synechocystis'' is not diazotrophic, and is closely related to another model organism, ''Cyanothece ''Cyanothece'' is a genus of unicellular, diazotrophic, oxygenic photosynthesizing cyanobacteria. Modern organisms and cellular organization In 1976, Jiří Komárek defined the prokaryotic cyanobacteria genus ''Cyanothece'' as distinct from ' ...'' ATCC 51442. It has been suggested that originally ''Synechocystis'' possessed the ability to fix atmospheric nitrogen, but lost the genes required for the process. See also * ''Synechocystis'' run-and-tumble References {{Taxonbar, from=Q7662346 Cyanobacteria genera Synechococcales Bacteria gene ...
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Cyanophycin
Cyanophycin, also known as CGP (cyanophycin granule polypeptide) or multi-L-arginyl-poly (L-aspartic acid), is a non-protein, non-ribosomally produced amino acid polymer composed of an aspartic acid backbone and arginine side groups. Cyanophycin was first detected in 1887 by the Italian botanist ''Antonino Borzì'' and can be found in most cyanobacteria and a few heterotrophic bacteria such as ''Acinetobacter'' sp. Cyanophycin is largely insoluble under physiological conditions and is accumulated in the form of granules in the cytoplasm during phosphate or sulfur starvation, generally in the early and mid-stationary phase. It is used as a nitrogen- and possibly carbon-storage compound and also serves as a dynamic buffer for fixed nitrogen in cyanobacterial heterocysts. Nitrogen and carbon are mobilized from cyanophycin by intracellular cyanophycinase in the form of aspartate-arginine dipeptides. Cyanophycin is synthesized from arginine and aspartate in an ATP-dependent reaction ...
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