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Download Class 1 Oxidoreductases XI: EC 1.14.11 - 1.14.14, Second by Dietmar Schomburg, Ida Schomburg, Antje Chang PDF

By Dietmar Schomburg, Ida Schomburg, Antje Chang

The Springer instruction manual of Enzymes presents concise facts on a few 5,000 enzymes sufficiently good characterised – and here's the second one, up-to-date variation. Their program in analytical, artificial and biotechnology techniques in addition to in meals undefined, and for medicinal remedies is extra. info sheets are prepared of their EC-Number series. the recent version displays massive development in enzymology: the entire fabric has greater than doubled, and the whole 2d version comprises 39 volumes plus Synonym Index. beginning in 2009, all newly categorised enzymes are handled in complement Volumes.

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Additional info for Class 1 Oxidoreductases XI: EC 1.14.11 - 1.14.14, Second Edition (Springer Handbook of Enzymes, 26)

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6fold stimulation at 1 mM [21]) [21] nucleoside triphosphates <1, 3, 5> (<1,3,5> stimulate [2,21]) [2, 21] pyridine 2,6-dicarboxylate <20> (<20> activator [63]) [63] thymol <1, 3> (<1,3> activation [2]) [2] Additional information <1> (protein disulfide-isomerase is able to activate the purified enzyme, the activation is probably due to the repairing of disulfide exchanges ocurring in the prolyl 4-hydroxylase structure during purification and storage. 004 mM [62]; <20> the maximal rate of hydroxylation is attained at a ferrous ion concentration of approx.

2 Procollagen-proline dioxygenase P 4-hydroxyproline containing peptide + succinate + CO2 <1> [12] S Additional information <1, 4, 5, 6, 9-12, 16, 17, 20, 27, 29-33> (<4> no activity with poly-l-proline or the unhydroxylated decapeptide analog (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) of the polyphenolic protein [10]; <1> in the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by the enzyme is stoichiometrically coupled to the oxidation of ascorbate [15]; <1> characterization of the 2oxoglutarate binding site of the enzyme, 2-oxosuccinate, 2-oxovalerate, 2oxobutyrate, 3-oxoglutarate or pyridine 2,5-dicarboxylate do not replace 2-oxoglutarate as cosubstrates [16]; <1, 5, 6> thermal denaturing of the triple-helical conformation of the substrate before hydroxylation [16-19, 24, 26-28, 33, 37, 60]; <6> effect of substrate on activity [26]; <1> the enzyme is specific for proline in the second position after glycine, the position in which the hydroxyproline in collagen is found.

1> [12]) [12] P 4-hydroxyproline containing peptide + succinate + CO2 <1> [12] S tert-butyloxycarbonyl-Pro-Pro-Gly-Pro-Pro-OH + 2-oxoglutarate + O2 <1> (Reversibility: ? 4% relative activity with respect to poly(l-proline) of MW 2000 [42, 43]) (Reversibility: ? <10> [42, 43]) [42, 43] P 4-hydroxyproline containing peptide <10> [42, 43] S tert-butyloxycarbonyl-Val-Pro-Gly-Val-OH + 2-oxoglutarate + O2 <1> (Reversibility: ? 2 Procollagen-proline dioxygenase P 4-hydroxyproline containing peptide + succinate + CO2 <1> [12] S Additional information <1, 4, 5, 6, 9-12, 16, 17, 20, 27, 29-33> (<4> no activity with poly-l-proline or the unhydroxylated decapeptide analog (Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Tyr-Lys) of the polyphenolic protein [10]; <1> in the absence of a peptidylproline substrate, the oxidative decarboxylation of 2-oxoglutarate by the enzyme is stoichiometrically coupled to the oxidation of ascorbate [15]; <1> characterization of the 2oxoglutarate binding site of the enzyme, 2-oxosuccinate, 2-oxovalerate, 2oxobutyrate, 3-oxoglutarate or pyridine 2,5-dicarboxylate do not replace 2-oxoglutarate as cosubstrates [16]; <1, 5, 6> thermal denaturing of the triple-helical conformation of the substrate before hydroxylation [16-19, 24, 26-28, 33, 37, 60]; <6> effect of substrate on activity [26]; <1> the enzyme is specific for proline in the second position after glycine, the position in which the hydroxyproline in collagen is found.

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