Download Class 2 Transferases VII: EC 2.5.1.31 - 2.6.1.57 (Springer by Dietmar Schomburg, A. Chang, Ida Schomburg PDF

By Dietmar Schomburg, A. Chang, Ida Schomburg

The Springer instruction manual of Enzymes presents concise info on a few 5,000 enzymes sufficiently good characterised – and this is the second one, up to date variation. Their program in analytical, man made and biotechnology procedures in addition to in foodstuff undefined, and for medicinal remedies is additional. info sheets are prepared of their EC-Number series. the recent variation displays huge growth in enzymology: the full fabric has greater than doubled, and the full second variation includes 39 volumes plus Synonym Index. beginning in 2009, all newly categorized enzymes are taken care of in complement Volumes.

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Read or Download Class 2 Transferases VII: EC 2.5.1.31 - 2.6.1.57 (Springer Handbook of Enzymes) PDF

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Extra info for Class 2 Transferases VII: EC 2.5.1.31 - 2.6.1.57 (Springer Handbook of Enzymes)

Example text

SD 58. Arch. Biochem. : Stereochemistry of the isoprenylation of tryptophan catalyzed by 4-(g,g-dimethylallyl)tryptophan synthase from Claviceps, the first pathway-specific enzyme in ergot alkaloid biosynthesis. J. Am. Chem. : Dimethylallylpyrophosphate: l-tryptophan dimethylallyltransferase. : Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea. Arch. Biochem. : Crystallization and partial characterization of dimethylallyl pyrophosphate: l-tryptophan dimethylallyltransferase from Claviceps sp.

Coli mostly exists in pellet in the absence of detergents, a low quantity of soluble enzyme is purified [14]) [14] Purification <1> (partial [5,8]) [1, 3, 5, 8] <2> (partial [10]) [7, 10, 21] <3> (partial [2]) [2] <4> [9, 15, 16] <6> [14] Renaturation <6> (the recombinant protein in the pellet is solubilized with 7 M urea and purified using nickel-nitrilotriacetic acid under denaturing conditions. 31 ant in the presence of 6 mM b-mercaptoethanol. Alternatively, on-column refolding is carried out in a single step to obtain the active protein in large quantities.

6fold lower than that of the wild-type enzyme. 5fold higher than that of the wild-type enzyme. 2fold higher than that for the wild-type enzyme. 3fold lower than that of the wild-type enzyme. 98fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 65% of that of the wild-type enzyme [20]) [20] F73A <4> (<4>, comparable Km -values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. 32fold increase in Km -value for isopentenyl diphosphate and about 17fold decrease in turnovernumber.

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