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

By Dr. Antje Chang (eds.)

Springer guide of Enzymes offers info on enzymes sufficiently good characterised. It bargains concise and whole descriptions of a few 5,000 enzymes and their software parts. facts sheets are prepared of their EC-Number series and the volumes themselves are prepared in accordance with enzyme classes.

This new, moment version displays massive development in enzymology: many enzymes are newly categorised or reclassified. each 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 complete volume of fabric inside the instruction manual has greater than doubled in order that the full moment version contains 39 volumes in addition to a Synonym Index. additionally, beginning in 2009, all newly labeled enzymes are taken care of in complement Volumes.

Springer guide of Enzymes is a perfect resource of data for researchers in biochemistry, biotechnology, natural and analytical chemistry, and meals sciences, in addition to for medicinal applications.

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Extra resources for Class 3 Hydrolases: EC 3.1–3.4.21

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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.

J. : Effect of dietary saturated fatty acids on intracellular free fatty acids and kinetic properties of hormone-sensitive lipase of rat adipocytes. J. : Hormone-sensitive lipase: structure, function, evolution and overproduction in insect cells using the baculovirus expression system. : Mutational analysis of the “regulatory module“ of hormone-sensitive lipase. 79 [32] [33] [34] [35] [36] [37] [38] [39] [40] [41] Hormone-sensitive lipase non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys.

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 ? : Chlorophyll degradation during senescence. Annu. Rev. : Two enzymatic reaction pathways in the formation of pyropheophorbide a.

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