Download Class 3 Hydrolases, EC 3.1-3.4.21 (Springer Handbook of by Antje Chang, Dietmar Schomburg, Ida Schomburg PDF

By Antje Chang, Dietmar Schomburg, Ida Schomburg

Content material: v. 1. classification five: Isomerases -- v. 2. type 6: Ligases -- v. three. classification four: Lyases I -- v. four. classification four: Lyases II -- v. five. category four: Layases III -- v. 6. type 3.4: Hydrolases I -- v. 7. classification 3.4: Hydrolases II -- v. eight. category 3.4: Hydrolases III -- Index A: Synonym -- v. nine. type 3.1: Hydrolases IV -- v. 10. type 3.1: Hydrolases V -- v. eleven. category 3.1: Hydroclass VI EC 3.1.4 -- 3.1.31 -- v. 12. category 3.2: Hydrolases VII EC 3.2.1.1-3.2.1.47 -- v. thirteen. classification 3.2: Hydrolases VIII, EC 3.2.1.48-3.2.1.149 -- v. 14. type 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. category 1. Oxidoreductases I, EC 1.1.1.1-1.1.1.50 -- v. 17. category 1: Oxidoreductases II, EC 1.1.1.51-1.1.1.154 -- v. 18. category 1: Oxidoreductases III, EC 1.1.1.155-1.1.1.274 -- v. 19. category 1: Oxidoreductases IV, EC 1.1.2-1.1.99 -- v. 20. classification 1. Oxidoreductases V, EC 1.2 -- v. 21. type 1. Oxidoreductases VI, EC 1.3 -- v. 22. type 1. Oxidoreductases VII, EC 1.4 -- v. 23. category 1. Oxidoreductases VIII, EC 1.5 -- v. 24. type 1. Oxidoreductases IX, EC 1.6-1.8 -- v. 25. type 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. category 2. Transferases III EC 2.3.1.60-2.3.3.15 -- v. 31. classification 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. type 2. Transferases EC 2.7.11.1-2.7.11.16.-- suppl. v. S4. type 2 Transferases EC 2.7.11.17-2.8

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

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

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

Example text

81 quorum-quenching enzyme <7, 13, 35> [10, 12, 13] quorum-quenching lactonase <15> [7] quorum-sensing enzyme Additional information <13> (<13> the enzyme belongs to the quorumquenching enzymes [12]) [12] CAS registry number 389867-43-0 2 Source Organism <1> <2> <3> <4> <5> <6> <7> <8> <9> <10> <11> <12> <13> <14> <15> <16> <17> <18> <19> <20> <21> <22> <23> <24> <25> <26> <27> <28> <29> <30> <31> <32> <33> <34> <35> 24 Mus musculus (no sequence specified) [9] Homo sapiens (no sequence specified) [9] Bos taurus (no sequence specified) [9] Oryctolagus cuniculus (no sequence specified) [9] Pseudomonas aeruginosa (no sequence specified) [5] Bacillus cereus (no sequence specified) [1,4] Bacillus sp.

UNIPROT accession number: Q7X3T2) [11] Klebsiella pneumoniae (UNIPROT accession number: Q7X477) [11] Bacillus thuringiensis subsp. kurstaki (no sequence specified) [15] no activity in Gallus gallus serum [9] Bacillus thuringiensis subsp. 81 <35> the enzyme AiiA inactivates the acylhomoserine lactone quorumsensing signal and attenuates the virulence of Erwinia carotovora, acylhomoserine lactones are autoinducers of quorum-sensing signaling, the inhibition of which is a feasible approach for prevention of bacterial infection [13]; <39> the enzyme AiiA inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of pathogenic bacteria [11]; <11> the isozymes AttM, AiiB, and AiiC inactivate the acylhomoserine lactone quorum-sensing signaling and attenuate the virulence of Erwinia carotovora subsp.

Biophys. : Hormonesensitive lipase from swine adipose tissue: identification and some properties. Comp. Biochem. Physiol. : Letting lipids go: hormonesensitive lipase. Curr. Opin. : Structure-function relationships of hormone-sensitive lipase. Eur. J. : Expression of biologically active hormone-sensitive lipase in mammalian (COS) cells. : Lipoprotein and hormone-sensitive lipases in porcine adipose tissue. J. Anim. : Positional specificity of hormone-sensitive lipase from rat adipose tissue. J.

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