Download e-book for kindle: Class 3 Hydrolases: EC 3.1–3.4.21 by Dr. Antje Chang (eds.)

By Dr. Antje Chang (eds.)

ISBN-10: 3540857028

ISBN-13: 9783540857020

ISBN-10: 3540857036

ISBN-13: 9783540857037

Springer instruction manual of Enzymes presents information on enzymes sufficiently good characterised. It bargains concise and whole descriptions of a few 5,000 enzymes and their program components. info sheets are prepared of their EC-Number series and the volumes themselves are prepared based on enzyme classes.

This new, moment version displays significant growth in enzymology: many enzymes are newly categorized or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: program and engineering (for the houses of enzymes the place the series has been changed). the whole quantity of fabric inside the guide has greater than doubled in order that the total moment variation comprises 39 volumes in addition to a Synonym Index. moreover, beginning in 2009, all newly categorized enzymes are taken care of in complement Volumes.

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

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Extra info for Class 3 Hydrolases: EC 3.1–3.4.21

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With a virus-based plant expression system, it was possible to express the enzyme functionally in leaves of Nicotiana benthamiana Domin. : Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system. : Characterization of 2b(R)-17-O-acetylajmalan: acetylesterase - a specific enzyme involved in the biosynthesis of the Rauwolfia alkaloid ajmaline. Z. Naturforsch. 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.

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).

And predicted homologues in other bacteria. : Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. : Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. : Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proc. Natl. Acad. Sci. : The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-l-homoserine lactone hydrolase.

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