Download Class 2 Transferases XI: EC 2.7.6 - 2.7.7 by Dietmar Schomburg, Ida Schomburg, Antje Chang PDF

By Dietmar Schomburg, Ida Schomburg, Antje Chang

The Springer guide of Enzymes offers concise information on a few 5,000 enzymes sufficiently good characterised – and here's the second one, up-to-date version. Their program in analytical, man made and biotechnology approaches in addition to in foodstuff undefined, and for medicinal remedies is extra. information sheets are prepared of their EC-Number series. the recent version displays substantial growth in enzymology: the whole fabric has greater than doubled, and the entire second variation involves 39 volumes plus Synonym Index. beginning in 2009, all newly labeled enzymes are handled in complement Volumes.

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Extra info for Class 2 Transferases XI: EC 2.7.6 - 2.7.7

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Phosphoribosylpyrophosphate synthetase and related pyrophosphokinases. The Enzymes, 3rd Ed. : Phosphoribosylpyrophosphate synthetase (ribose-5-phosphate pyrophosphokinase) from Salmonella typhimurium. : Ribosephosphate pyrophosphokinase (rat liver). : Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis. Eur. J. : Studies of the quaternary structure and the chemical properties of phosphoribosylpyrophosphate synthetase from Salmonella typhimurium. J. Biol.

J. Mol. : Biosynthesis of folic acid compounds in plasmodia. Hoppe-Seyler's Z. Physiol. : 7,8-Dihydropteroate-synthesizing enzyme from Plasmodium chabaudi. : The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J. Biol. : The hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein of Pneumocystis carnii expressed as an independent enzyme in Escherichia coli: refolding and characterization of the recombinant enzyme.

Biophys. : Crystal structure of thiamin pyrophosphokinase. J. Mol. : Schizosaccharomyces pombe thiamin pyrophosphokinase is encoded by gene tnr3 and is a regulator of thiamin metabolism, phosphate metabolism, mating, and growth. J. Biol. 3 2-Amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase 2 Source Organism <1> Escherichia coli (MC4100 [13]) [1, 2, 5, 6, 10, 11, 13] <2> Pneumocystis carinii (multifunctional folic acid synthesis fas gene of encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase [12]) [3, 12] <3> Pisum sativum [4] <4> Haemophilus influenzae (Brookhaven Protein Data Bank: 1cbk [7]) [7] <5> Plasmodium chabaudi [8, 9] 3 Reaction and Specificity Catalyzed reaction ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine Reaction type diphosphate transfer Natural substrates and products S ATP + 6-hydroxymethyl-7,8-dihydropteridine <1> (<1> the product 6-hydroxymethyl-7,8-dihydropterin diphosphate is an intermediate in the pathway for folic acid biosynthesis [2]) (Reversibility: ?

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