What are RARE RESTRICTION enzymes?
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Restriction Enzymes: \n\n \n\nThese are enzymes that cleave the strands of DNA at specific sites, according to the nucleotide sequence. They are counterparts of proteolytic enzymes such as trypsin, chymotrypsin in the world of nucleic acids. They are highly specific, and the sites they recognize may be very rare. Restriction enzymes are found in nature, primarily produced by bacteria as part of a defense system. \n\nThere are several types of restriction enzymes. We will focus on Type II, which is the type most widely used experimentally. \n\nNuclease: an enzyme that cleaves a nucleic acid\n\nRestriction Endonuclease: an enzyme that cleaves within a segment of nucleic acid, when it recognizes a specific sequences of bases. (Restriction enzyme)\n\nTypically, they are dimeric, and cleave at symmetrical sequences of DNA.\n\nExamples EcoR I and BamH I\n\n(See Chime link)\n\nHow do Restriction Enzymes recognize particular sequences of DNA?\n\nDo they open up the strands, in order to see the bases?\n\nNo, they bind along the major or minor grooves, and interact with the edges of the bases, for sequences specificity, \n\nand also with the sugars and the phosphates, for non-specific binding. This involves, H-bonding, hydrophobic contacts, and electrostatic interactions (ion pairs).
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http://www.amano-enzyme.co.jp/english/productuse/others.html
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In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. For example, an enzyme that catalyzed this reaction would be a lyase:\n\nATP → cAMP + PPi \nLyases differ from other enzymes in that they only require one substrate for the reaction in one direction, but two substrates for the reverse reaction.
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Transglutaminases are a family of enzymes (EC 2.3.2.13) that catalyze the formation of a covalent bond between a free amine group (e.g., protein- or peptide-bound lysine) and the gamma-carboxamid group of protein- or peptide bound glutamine. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation.\n\nTransglutaminases were first described in 1957.[1]. The exact biochemical activity of transglutaminases was discovered in blood coagulation protein factor XIII in 1968.[2]\n\nPhysiological transglutaminases\nEight transglutaminases have been characterised.[3]\n\nName Activity Chromosome OMIM \nFactor XIII (fibrin-stabilizing factor) coagulaton 6p25-p24 Mendelian Inheritance in Man (OMIM) 134570 \nKeratinocyte transglutaminase (TGM1) skin 14q11.2 Mendelian Inheritance in Man (OMIM) 190195 \nTissue transglutaminase (TGM2) ubiquitous 20q11.2-q12 Mendelian Inheritance in Man (OMIM) 190196 \nEpidermal transglutaminase (TGM3) skin 20q12 Mendelian Inheritance in Man (OMIM) 600238 \nProstate transglutaminase (TGM4) prostate 3p22-p21.33 Mendelian Inheritance in Man (OMIM) 600585 \nTGM X or TGM5[4] skin 15q15.2 Mendelian Inheritance in Man (OMIM) 603805 \nTGM Y or TGM 6 unclear 20q11-15 not assigned \nTGM Z or TGM 7 testis, lung 15q15.2 Mendelian Inheritance in Man (OMIM) 606776 \n\nMechanism of action\nTransglutaminases form extensively cross linked generally insoluble protein polymers. These biological polymers are indispensable for the organism in order to create barriers and stable structures. Examples are blood clots (coagulation factor XIII) as well as skin and hair. The catalytic reaction is generally viewed as being irreversible and must be closely monitored through extensive control mechanisms.\n\nRole in disease\nDeficiency of factor XIII (a rare genetic condition) predisposes to hemorrhage; concentrated enzyme can be used to correct the abnormality and reduce bleeding risk.\n\nAntibodies to tissue transglutaminase are found in coeliac disease and may play a role in the small bowel damage in response to dietary gliadin that characterises this condition.\n\nRecent research indicates that sufferers from neurological diseases like Huntington's,[5] and Parkinson's[6] may have unusually high levels of one type of transglutaminase, tissue transglutaminase. It is hypothesized that tissue transglutaminase may be involved in the formation of the protein aggregates that causes Huntington's disease, although it is most likely not required.[7]\n\nIndustrial applications\nIndustrial transglutaminase is produced by Streptoverticillium mobaraense fermentation in commercial quantities and is used in a variety of processes, including the production of processed meat and fish products. It can be used as a binding agent to improve the texture of protein-rich foods such as surimi or ham.\n\nTransglutaminase can be used in these applications:\n\nBinding small chunks of meats into a big one ("portion control"), such as in sausages, hot dogs, restructured steaks \nImproving the texture of low-grade meat such as so-called "PSE meat" (pale, soft, and exudative meat; caused by stress and a rapid postmortem pH decline) \nMaking milk and yogurt creamier \nMaking noodles firmer \nBesides its "orthodox" uses, transglutaminase can be used to create some unusual foods. "Cold Set Bound Fish Kebabs" are made from alternating layers of salmon and cod which are "glued" together by transglutaminase. Wylie Dufresne, chef of New York's avant-garde restaurant WD-50, invented a "pasta" made by over 95% shrimps thanks to transglutaminase.
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You have to identify two sequences that are >6kb apart from one another that flank the sequence you are attempting to amplify. Better yet, you can get you a well understood cloning vector (plasmid) that already has primers develped for it that flank the polyrestriction site region (ie. puc19 [see link below], find the needed restriction enzyme sites that flank your desired 6kb sequence and clone the DNA into the vector. Be sure to check your sequence for any internal restriction sites. This may require you to do a partial digestion and recovery.
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http://biotech.icmb.utexas.edu/search/dict-search.html
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intrinsic red cell enzyme defect.\nRed cells normally lose their nuclei and also lose their ability to produse proteins {enzymes} the conditions occures in heterozygous females
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If you are in Europe try Novozime (Netherland)\nIf you are in USA try Genencor \n\nTelomerase is an enzyme that take part in replication mechanism, especial in cancer cells (they do not lose a part of its DNA when the two strands are copied)
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enzyme catalysis, defense, transport, support, motion, regulation, and storage.
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It's a strain designation.  BL21 is deficient in a protease, and DE3 can be used with vectors containing the CcdB gene, which is toxic to other bacteria.
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OK, so if you don't digest plasmid you'll get three bands:\n\nlinear, nicked and supercoiled.\n\nHowever, you did digest it, with 2 enzymes with 1 site each (I think?).\n\nA complete digestion would yield 2 bands.  Incomplete digestion would give those two bands, plus linearized (single cut, either enzyme).
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It is an enzyme that make possible to transcribe DNA from RNA.\nThanks
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Prime Rib.\nMedium rare.
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restriction enzymes only work in proper salt and pH condtions.  The buffer is there to mimic the conditions the enzymes normall work in.
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I think your questions is how are genes methylated? There is a class of enzymes called DNA methytransferases that does this.
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Are you looking for all known orthologues of the individual genes in the operon (I assume) or for all occurences of these particular genes in an operon in other organisms (bacteria)?\n\n\n\n/////////\nI would try to look at "HomoloGENE", "Genome" and "UniGene" at the Entrez gateway at the US National Library of Medicine, Nat'l Ctr. for Biotechnology Info. (NCBI) \n\nhttp://www.ncbi.nlm.nih.gov/gquery/gquery.fcgi?itool=toolbar
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baby enzymes can deal with those long chains very well