By Antje Chang, Dietmar Schomburg, Ida Schomburg

ISBN-10: 3540857028

ISBN-13: 9783540857020

Content material: v. 1. classification five: Isomerases -- v. 2. type 6: Ligases -- v. three. classification four: Lyases I -- v. four. category four: Lyases II -- v. five. classification four: Layases III -- v. 6. category 3.4: Hydrolases I -- v. 7. type 3.4: Hydrolases II -- v. eight. classification 3.4: Hydrolases III -- Index A: Synonym -- v. nine. classification 3.1: Hydrolases IV -- v. 10. classification 3.1: Hydrolases V -- v. eleven. category 3.1: Hydroclass VI EC 3.1.4 -- 3.1.31 -- v. 12. classification 3.2: Hydrolases VII EC 3.2.1.1-3.2.1.47 -- v. thirteen. category 3.2: Hydrolases VIII, EC 3.2.1.48-3.2.1.149 -- v. 14. category 3.2-3.5: Hydrolases IX EC 3.2.2-3.5.3 -- v. 15. category 3.5.-3.12, hydrolases X, EC 3.5.4-3.12.1 -- v. sixteen. type 1. Oxidoreductases I, EC 1.1.1.1-1.1.1.50 -- v. 17. type 1: Oxidoreductases II, EC 1.1.1.51-1.1.1.154 -- v. 18. classification 1: Oxidoreductases III, EC 1.1.1.155-1.1.1.274 -- v. 19. type 1: Oxidoreductases IV, EC 1.1.2-1.1.99 -- v. 20. category 1. Oxidoreductases V, EC 1.2 -- v. 21. type 1. Oxidoreductases VI, EC 1.3 -- v. 22. classification 1. Oxidoreductases VII, EC 1.4 -- v. 23. classification 1. Oxidoreductases VIII, EC 1.5 -- v. 24. classification 1. Oxidoreductases IX, EC 1.6-1.8 -- v. 25. category 1. Oxidoreductases X, EC 1.9-1.13 -- v. 26. classification 1. Oxidoreductases XI EC 1.14.11-1.14.14 -- v. 27. category 1. Oxidoreductases XII, EC 1.14.15-1.97 -- v. 28. type 2. Transferases I EC 2.1.1 -- v. 29. category 2. Transferases II EC 2.1.2.1-2.3.1.59 -- v. 30. classification 2. Transferases III EC 2.3.1.60-2.3.3.15 -- v. 31. type 2. Transferases IV EC 2.4.1.1-2.4.1.89. -- suppl. v. S2. category 2. Transferases EC 2.1-2.7.10 -- suppl. v. S3. classification 2. Transferases EC 2.7.11.1-2.7.11.16.-- suppl. v. S4. classification 2 Transferases EC 2.7.11.17-2.8

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Content material: v. 1. classification five: Isomerases -- v. 2. category 6: Ligases -- v. three. type four: Lyases I -- v. four. classification four: Lyases II -- v. five. category four: Layases III -- v. 6. type three. four: Hydrolases I -- v. 7. type three. four: Hydrolases II -- v. eight. classification three. four: Hydrolases III -- Index A: Synonym -- v. nine. type three. 1: Hydrolases IV -- v.

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Extra info for Class 3 Hydrolases, EC 3.1-3.4.21 (Springer Handbook of Enzymes, S5)

Sample text

Proc. Natl. Acad. Sci. ) [6] P ? S pheophorbide a + H2 O <1, 4, 9> (<9> constitutively expressed [3]; <4> Phedase type 1 is senescence-induced [2]; <4> Phedase type 2 is constitutively produced [2]; <4> PPD type 1 [6]; <4> PPD type 2 [6]; <9> the enzyme catalyzes the conversion of pheophorbide a to a precursor of pyropheophorbide a (C-132-carboxyl-pyropheophorbide a). ) [6] P ? ) [6] P ?

Environ. : The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. : Crystallization and preliminary crystallographic analysis of Bacillus thuringiensis AHL-lactonase. Biochim. Biophys. : Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. : Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase). J. Biol. , and predicted homologues in other bacteria. : Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes.

Appl. Environ. : Identification of QuiP, the product of gene PA1032, as the second acyl-homoserine lactone acylase of Pseudomonas aeruginosa PAO1. Appl. Environ. : A quorum-quenching approach to investigate the conservation of quorumsensing-regulated functions within the Burkholderia cepacia complex. Appl. Environ. : The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. : Crystallization and preliminary crystallographic analysis of Bacillus thuringiensis AHL-lactonase.

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Class 3 Hydrolases, EC 3.1-3.4.21 (Springer Handbook of Enzymes, S5) by Antje Chang, Dietmar Schomburg, Ida Schomburg


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