By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)
Springer instruction manual of Enzymes offers information on enzymes sufficiently good characterised. It deals concise and entire descriptions of a few 5,000 enzymes and their software parts. facts sheets are prepared of their EC-Number series and the volumes themselves are prepared based on enzyme classes.
This new, moment variation displays massive growth in enzymology: many enzymes are newly categorized or reclassified. every one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the houses of enzymes the place the series has been changed). the complete volume of fabric inside the guide has greater than doubled in order that the full moment variation involves 39 volumes in addition to a Synonym Index. moreover, beginning in 2009, all newly labeled enzymes are handled in complement Volumes.
Springer instruction manual of Enzymes is a perfect resource of knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and foodstuff sciences, in addition to for medicinal applications.
Read or Download Class 2 · Transferases VI: EC 188.8.131.52–184.108.40.206 PDF
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Extra info for Class 2 · Transferases VI: EC 220.127.116.11–18.104.22.168
31 Di-trans,poly-cis-decaprenylcistransferase farnesyl diphosphate is 3% of that of the wild-type enzyme. 4fold higher than that for the wild-type enzyme. 8fold lower than that of the wild-type enzyme. 1fold higher than that of the wild-type enzyme. 4fold higher than that for the wild-type enzyme. 3fold lower than that of the wild-type enzyme. 3fold higher than that of the wild-type enzyme. 4fold higher than that of the wild-type enzyme )  S74A <4> (<4>, comparable Km -values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme.
J. Mol. Catal. : Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations. Biochem. Biophys. Res. : Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase. J. : Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. J. 34 Systematic name dimethylallyl-diphosphate:l-tryptophan dimethylallyltransferase Recommended name tryptophan dimethylallyltransferase Synonyms 4-(g,g-dimethylallyl)tryptophan synthase DMAT synthase DMAT synthetase dimethylallylpyrophosphate:l-tryptophan dimethylallyltransferase dimethylallylpyrophosphate:tryptophan dimethylallyl transferase dimethylallylpyrophosphate:tryptophan dimethylallyltransferase dimethylallyltransferase, tryptophan dimethylallyltryptophan synthetase CAS registry number 55127-01-0 2 Source Organism <1> Claviceps sp.
Expression of an active phytoene synthase from Erwinia uredovora and biochemical properties of the enzyme. Biochim. Biophys. 32 Phytoene synthase functional analysis of the various truncated gene products. J. : Phytoene synthase from Narcissus pseudonarcissus: functional expression, galactolipid requirement, topological distribution in chromoplasts and induction during flowering. : Transgenic rice (Oryza sativa) endosperm expressing daffodil (Narcissus pseudo-narcissus) phytoene synthase accumulates phytoene, a key intermediate of provitamin A biosynthesis.
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