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Download Class 2 Transferases II: EC 2.1.2.1 - 2.3.1.59 (Springer by Dietmar Schomburg, A. Chang, Ida Schomburg PDF

By Dietmar Schomburg, A. Chang, Ida Schomburg

The Springer guide of Enzymes presents concise facts on a few 5,000 enzymes sufficiently good characterised – and this is the second one, up-to-date variation. Their program in analytical, artificial and biotechnology strategies in addition to in meals undefined, and for medicinal remedies is extra. info sheets are prepared of their EC-Number series. the hot version displays massive development in enzymology: the full fabric has greater than doubled, and the total 2d version contains 39 volumes plus Synonym Index. beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes.

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Extra resources for Class 2 Transferases II: EC 2.1.2.1 - 2.3.1.59 (Springer Handbook of Enzymes)

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1-4, 6-16> [128, 30-32]; r <5> [29]) [1-32] P tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide S 10-formyltetrahydrofolate + glycinamide ribonucleotide <5, 8> (Reversibility: ? 2 Phosphoribosylglycinamide formyltransferase Substrates and products S (6R)-N10 -formyltetrahydrofolate + 5-phospho-d-ribosylglycinamide <2, 5> (Reversibility: ? <2, 5> [8, 11]) [8, 11] P (6R)-tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide <2, 5> [8, 11] S 10-formyl-5,8-dideazafolate + carbocyclic b-glycinamide ribonucleotide <5, 7, 8> (Reversibility: ?

Glycidaldehyde, an inhibitor directed towards the C1 -units-binding site of serine transhydoxymethylase. Biochem. Soc. : Kinetic mechanism of the interaction of d-cycloserine with serine hydroxymethyltransferase. : A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine. Biochem. : 5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase.

J. Mol. : Purification of glycineamide ribonucleotide transformylase. Biochem. Biophys. Res. : Carbocyclic glycinamide ribonucleotide is a substrate for glycinamide ribonucleotide transformylase. Arch. Biochem. : Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. : Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Proc. Natl. Acad. Sci. : Preliminary crystallographic investigations of glycinamide ribonucleotide transformylase.

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