Download e-book for kindle: Class 2 · Transferases VI: EC 2.4.2.1–2.5.1.30 by Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje

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

ISBN-10: 3540325883

ISBN-13: 9783540325888

ISBN-10: 3540497536

ISBN-13: 9783540497530

Springer guide of Enzymes presents information on enzymes sufficiently good characterised. It deals concise and whole descriptions of a few 5,000 enzymes and their program components. information sheets are prepared of their EC-Number series and the volumes themselves are prepared in accordance with enzyme classes.

This new, moment version displays massive growth in enzymology: many enzymes are newly categorised or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: program and engineering (for the homes of enzymes the place the series has been changed). the whole volume of fabric inside the guide has greater than doubled in order that the whole moment variation includes 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorised enzymes are handled in complement Volumes.

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

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Extra resources for Class 2 · Transferases VI: EC 2.4.2.1–2.5.1.30

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Biochem. : Chinese hamster purine-nucleoside phosphorylase: purification, structural, and catalytic properties. : Purine nucleoside phosphorylase from human erythrocytes: physiocochemical properties of the crystalline enzyme. : Bovine brain purine-nucleoside phosphorylase purification, characterization, and catalytic mechanism. : Purine nucleoside phosphorylase. Structure-activity relationships for substrate and inhibitor properties of N-1-, N-7-, and C-8-substituted analogues; differentiation of mammalian and bacterial enzymes with N-1-methylinosine and guanosine.

Biol. : Properties of nucleoside phosphorylase from Enterobacter aerogenes. Agric. Biol. : Properties of purine nucleoside phosphorylase from Enterobacter cloacae. Agric. Biol. : Purification and characterization of a purine-nucleoside phosphorylase from bovine thyroid. Arch. Biochem. : Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992. Agric. Biol. : Purification and characterization of second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859.

J. Mol. : Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. J. Mol. : Purification and partial characterization of purine nucleoside phosphorylase from Serratia marcescens. Biosci. Biotechnol. 1 [55] [56] [57] [58] [59] [60] [61] Purine-nucleoside phosphorylase phosphorylase from Escherichia coli. Protein Expr. : Purine nucleoside phosphorylase. 1. Structurefunction Studies. : Design of an adenosine phosphorylase by active-site modification of murine purine nucleoside phosphorylase: enzyme kinetics and molecular dynamics simulation of Asn-243 and Lys-244 substitutions of purine nucleoside phosphorylase.

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Class 2 · Transferases VI: EC 2.4.2.1–2.5.1.30 by Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)


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