Class 3 Hydrolases: EC 3.4.22—3.13 by Dr. Antje Chang (eds.)

By Dr. Antje Chang (eds.)

Springer instruction manual of Enzymes offers facts 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 in keeping with enzyme classes.

This new, moment variation displays significant development 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 full volume of fabric inside the guide has greater than doubled in order that the whole moment version includes 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly labeled enzymes are handled 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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J. : The high stability of cruzipain against pH-induced inactivation is not dependent on its C-terminal domain. : On the post-translational modifications at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi. FEMS Microbiol. : Cruzipain, a major Trypanosoma cruzi antigen, promotes arginase-2 expression and survival of neonatal mouse cardiomyocytes. Am. J. : Probing the cruzain S2 recognition subsite: a kinetic and binding energy calculation study. : Synthesis and evaluation of isatins and thiosemicarbazone derivatives against cruzain, falcipain-2 and rhodesain.

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3, 5] P ? ) [24] P ? ) [24] P ? ) [4, 5, 14] P ? ) [2, 7, 9] P ? ) [2] P ? ) [3, 4, 5, 13] P ? ) [24] P ? ) [24] P ? ) [2] P ? ) [24] P ? ) [7] P ? ) [24] P ? ) [24] P ? ) [24] P ? ) [2, 7, 10, 11, 14, 17] P ? ) [24] P ? ) [27] P ? ) [5] P ? ) [5] P ? ) [6] P ? ) [24] P ? ) [1, 4, 5, 10, 15, 16, 19] P ? 0: about 45% of maximal activity, hydrolysis of 2-aminobenzoyl-FRA-(2,4-dinitrophenyl)-eNH2 -lysine-NH2 [23]) [23] Temperature optimum ( C) 37 <2> (<2> assay at [2,6,9,11,13]) [2, 6, 9, 11, 13] 4 Enzyme Structure Molecular weight 23540 <2> (<2> electrospray mass spectrometry [7]) [7] 33000 <2, 3> (<2,3> SDS-PAGE [10,15]) [10, 15] 35000-60000 <2> (<2> SDS-PAGE, depending on electrophoretic conditions [4]) [4] 36300 <2> (<2> calculated from nucleotide sequence [4]) [4] 43000 <2> (<2> deglycosylated enzyme, SDS-PAGE [1]) [1] 51000 <2> (<2> glycosylated enzyme, SDS-PAGE [1]) [1] Subunits ?

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