Class 2 · Transferases VI: EC 2.5.1.31–2.6.1.57 by Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje

By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)

Springer instruction manual of Enzymes offers info on enzymes sufficiently good characterised. It deals concise and whole 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 in line with enzyme classes.

This new, moment version displays enormous development in enzymology: many enzymes are newly labeled or reclassified. every one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the homes of enzymes the place the series has been changed). the entire quantity of fabric inside the instruction manual has greater than doubled in order that the whole moment version involves 39 volumes in addition to a Synonym Index. additionally, beginning in 2009, all newly categorized enzymes are taken care of in complement Volumes.

Springer guide of Enzymes is a perfect resource of data for researchers in biochemistry, biotechnology, natural and analytical chemistry, and foodstuff sciences, in addition to for medicinal applications.

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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. SD58. J. Biol. : The Claviceps purpurea gene encoding dimethylallyltryptophan synthase, the committed step for ergot alkaloid biosynthesis. Biochem. Biophys. Res. 35 Systematic name dimethylallyl-diphosphate:aspulvinone-E dimethylallyltransferase Recommended name aspulvinone dimethylallyltransferase Synonyms dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase dimethylallyltransferase, aspulvinone CAS registry number 67584-68-3 2 Source Organism <1> Aspergillus terreus (IAM 2054 [1,2]) [1, 2] 3 Reaction and Specificity Catalyzed reaction 2 dimethylallyl diphosphate + aspulvinone E = 2 diphosphate + aspulvinone H Reaction type alkenyl group transfer Natural substrates and products S Additional information <1> (<1>, enzyme is involved in biosynthesis of aspulvinone pigments [1]) [1] P ?

In order to overcome the poor growth characteristics of the phytoene expressing strain, the enzyme level is increased by co-expressing the isoprenoid biosynthetic genes crtE and idi, encoding Erwinia geranylgeranyl diphosphate synthase and Rhodobacter isopentenyl diphosphate isomerase, respectively [11]; Agrobacterium-mediated transformation of hypocotyl explants of Brassica napus, 50fold increase in carotenoid levels [20]; overexpression in Lycopersicon esculentum, fruit-specific expression is achieved by using the tomato polygalacturonase promoter, and the enzyme is targeted to the chromoplast by the tomato phytoene synthase-1 transit sequence, total fruit carotenoids of primary transformants are 2-4fold higher than the control [21]) [10, 11, 20, 21] <8> (overexpressed in insect Sf9 cells using the baculovirus lipofection system.

Biol. : Lactobacillus plantarum undecaprenyl pyrophosphate synthetase: purification and reaction requirements. Arch. Biochem. : Prenyl transferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetase. Arch. Biochem. : Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. J. : Substrate specificity of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum. : Lipid activation of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum.

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