Download e-book for iPad: Class 3 Hydrolases : EC 3.4.22-3.13 by Antje Chang; SpringerLink (Online service)

By Antje Chang; SpringerLink (Online service)

ISBN-10: 3540857044

ISBN-13: 9783540857044

ISBN-10: 3540857052

ISBN-13: 9783540857051

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Extra info for Class 3 Hydrolases : EC 3.4.22-3.13

Example text

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 ?

E. 49 Separase Activating compounds securin <1, 5, 7> (<5,7> activation may be due to separase localization [7]; <5> securin is required to support separase activity in anaphase [9]; <7> the central domain of securin has a functionally essential specific sequence that may directly interact with the catalytic region of separase. This central securin domain is unrelated to destruction by polyubiquitination, but essential for the activation of separase [22]) [7, 9, 22] Additional information <9> (<9> separase shows self-cleavage upon activation [19]) [19] Metals, ions Ca2+ <4, 5, 7> (<4,5,7> Ca2+ -levels affect separase function, C-terminal region contains a Ca2+ -binding motif [7]) [7] 4 Enzyme Structure Molecular weight 225000 <4> (<4> recombinant separase, immunoblotting [14]) [14] Subunits ?

Eur. J. : Congopain from Trypanosoma congolense: drug target and vaccine candidate. Biol. : Heparan sulfate modulates kinin release by Trypanosoma cruzi through the activity of cruzipain. J. Biol. : The crystal structure of cruzain: a therapeutic target for Chagas’ disease. J. Mol. : Trypanosoma cruzi: cruzipain and membrane-bound cysteine proteinase isoform(s) interacts with human a2 macroglobulin and pregnancy zone protein. Exp. : Modulation of the catalytic activity of cruzipain, the major cysteine proteinase from Trypanosoma cruzi, by temperature and pH.

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Class 3 Hydrolases : EC 3.4.22-3.13 by Antje Chang; SpringerLink (Online service)


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