By Dr. Antje Chang (eds.)

ISBN-10: 3540857028

ISBN-13: 9783540857020

ISBN-10: 3540857036

ISBN-13: 9783540857037

Springer instruction manual of Enzymes offers info 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 version displays substantial growth in enzymology: many enzymes are newly categorised or reclassified. every one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the homes of enzymes the place the series has been changed). the full quantity of fabric inside the guide has greater than doubled in order that the entire moment version involves 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorized enzymes are taken care of 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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Additional info for Class 3 Hydrolases: EC 3.1–3.4.21

Sample text

79 Engineering D644-658 <3> (<3> reduced basal hydrolytic activity, no activation by cyclic AMP-dependent protein kinase [30]) [30] D657-664 <3> (<3> reduced basal hydrolytic activity, no activation by cyclic AMP-dependent protein kinase [30]) [30] D666-683 <3> (<3> very low basal and stimulated hydrolytic activity. Vmax with cholesteryl ester is 29fold lower than wild-type value. Vmax with p-nitrophenylbutyrate is 8fold lower than wild-type value [30]) [30] F650C <3> (<3> reduced activity against lipid-soluble but not water-soluble substrates [30]) [30] F654D <3> (<3> reduced activity against lipid-soluble but not water-soluble substrates [30]) [30] P651A <3> (<3> reduced activity against lipid-soluble but not water-soluble substrates [30]) [30] S423A <3> (<3> 99% loss of cholesteryl oleate hydrolysis, more than 80% loss of trioleoylglycerol hydrolysis and more than 90% loss of dioleoylglycerol hydrolysis [14]) [14] S563A <3> (<3> 98% loss of cholesteryl oleate hydrolysis, more than 80% loss of trioleoylglycerol hydrolysis and more than 90% loss of dioleoylglycerol hydrolysis [14]) [14] S563A/S565A <3> (<3> 70% loss of cholesteryl oleate hydrolysis, 10% loss of trioleoylglycerol hydrolysis and 80% loss of dioleoylglycerol hydrolysis [14]) [14] S563D <3> (<3> approx.

Proc. Natl. Acad. Sci. : The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-l-homoserine lactone hydrolase. Proc. Natl. Acad. Sci. : AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. 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).

Environ. : Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis. Appl. Environ. : The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-acyl homoserine lactonase activity. Appl. Environ. : Quorum quenching: Enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. Appl. Environ. : Identification of QuiP, the product of gene PA1032, as the second acyl-homoserine lactone acylase of Pseudomonas aeruginosa PAO1.

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Class 3 Hydrolases: EC 3.1–3.4.21 by Dr. Antje Chang (eds.)


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