Class 2 · Transferases VI: EC 2.4.2.1–2.5.1.30 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 facts on enzymes sufficiently good characterised. It bargains concise and entire descriptions of a few 5,000 enzymes and their software components. info sheets are prepared of their EC-Number series and the volumes themselves are prepared in response to enzyme classes.

This new, moment variation displays significant development in enzymology: many enzymes are newly categorized 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 quantity of fabric inside the instruction manual has greater than doubled in order that the total moment variation comprises 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 knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and foodstuff sciences, in addition to for medicinal applications.

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Naturforsch. : Rabbit brain purine nucleoside phosphorylase. Physical and chemical properties. Inhibition studies with aminopterin, folic acid and structurally related compounds. Arch. Biochem. : Adenosine phosphyorylase activity as distinct from inosineguanosine phosphorylase activity in Sarcoma 180 cells and rat liver. Biochim. Biophys. : Expression of human malaria parasite purine nucleoside phosphorylase in host enzyme-deficient erythrocyte culture. Enzyme characterization and identification of novel inhibitors.

1,2> [2, 4, 5, 7]) [1, 2, 4, 5, 6, 7] P uracil + a-d-ribose 1-phosphate <1> [1] S Additional information <1> (<1>, no activity with deoxycytidine [1]) [1] P ? : Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J. Biol. : The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. : Cloning, expression and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. Acta Crystallogr.

3 Uridine phosphorylase S 5-fluoro-2'-deoxyuridine + phosphate <2, 3> (<2> 14% of the activity with uridine [22]; <3> 15% of the activity with uridine [29]) (Reversibility: ? <2, 3> [22, 29]) [22, 29] P 5-fluorouracil + 2-deoxyribose-1-phosphate S 5-fluorouridine + phosphate <3, 5, 14> (<5> 15% of the activity with uridine [29]; <3> 85% of the activity with uridine [29]) (Reversibility: ? <3, 5, 14> [29,33]) [29, 33] P 5-fluorouracil + a-d-ribose-1-phosphate <5> [31] S 5-methyluridine + phosphate <3, 8, 9> (<8> 27% of the activity with uridine [25]) (Reversibility: ?

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